Term IRI Term label Parent term IRI Parent term label Alternative term Definition http://purl.obolibrary.org/obo/HP_0031292 cutaneous abscess http://purl.obolibrary.org/obo/ARO_3004430 antimicrobial resistance tissue specificity A circumscribed area of pus or necrotic debris in the skin. http://purl.obolibrary.org/obo/ARO_3004837 OXA-724 http://purl.obolibrary.org/obo/ARO_3007699 OXA-12-like beta-lactamase An OXA-12-family class D beta-lactamase identified from Aeromonas hydrophila. http://purl.obolibrary.org/obo/ARO_3004838 LEN-30 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase A class-A beta-lactamase from Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3004839 LEN-32 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase A class-A beta-lactamase from Klebsiella variicola. http://purl.obolibrary.org/obo/ARO_3004840 LEN-34 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase A class-A beta-lactamase from Klebsiella variicola. http://purl.obolibrary.org/obo/ARO_3004841 LEN-38 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase A class-A beta-lactamase from Klebsiella. http://purl.obolibrary.org/obo/ARO_3004842 LEN-39 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase A class-A broad-spectrum beta-lactamase identified from Klebsiella sp. http://purl.obolibrary.org/obo/ARO_3004843 LEN-40 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase A class-A broad-spectrum beta-lactamase identified from Klebsiella sp. http://purl.obolibrary.org/obo/ARO_3004844 LEN-41 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase A class-A broad-spectrum beta-lactamase identified from Klebsiella. http://purl.obolibrary.org/obo/ARO_3004845 LEN-42 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase A class-A broad-spectrum beta-lactamase from Klebsiella. http://purl.obolibrary.org/obo/ARO_3004846 LEN-43 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase A class-A broad-spectrum beta-lactamase from Klebsiella. http://purl.obolibrary.org/obo/ARO_3004847 LEN-51 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase A class-A broad-spectrum beta-lactamase from Klebsiella. http://purl.obolibrary.org/obo/ARO_3004848 LEN-55 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase A class-A broad-spectrum beta-lactamase from Klebsiella. http://purl.obolibrary.org/obo/ARO_3004849 LEN-58 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase A class-A broad-spectrum beta-lactamase from Klebsiella. http://purl.obolibrary.org/obo/ARO_3005004 Neisseria gonorrhoeae mtrC with mutation conferring resistance to azithromycin http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance Mutation in the mtrC efflux pump of Neisseria gonorrhoea shown to confer resistance to azithromycin, a macrolide type antibiotic. http://purl.obolibrary.org/obo/ARO_3005005 antibiotic-resistant emb arabinosyltransferase http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Known antibiotic-resistant variants of emb arabinosyltransferases, primarily in Mycobacterium and conferring resistance to ethambutol through point mutation. http://purl.obolibrary.org/obo/ARO_3005006 tet(57) http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump A tetracycline efflux MFS Transporter from Providencia sp. Y14. http://purl.obolibrary.org/obo/ARO_3005207 SHV-205 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase A beta-lactamase gene found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3005208 SHV-222 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase A beta-lactamase gene from Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3005209 SHV-198 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase A beta-lactamase gene from Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3005210 SHV-195 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase Beta-lactamase gene from Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3005211 SHV-201 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase Beta-lactamase gene from Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3005212 SHV-212 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase A beta-lactamase gene from Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3005213 SHV-204 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase A beta-lactamase gene from Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3005214 SHV-197 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase A beta-lactamase gene from Escherichia coli. http://purl.obolibrary.org/obo/ARO_3005215 SHV-216 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase A beta-lactamase gene from Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3005216 CMY-152 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-152 is a beta-lactamase found in Citrobacter freundii. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3005217 CMY-151 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-151 is a beta-lactamase found in Citrobacter freundii. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3005218 CMY-153 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-89 is a beta-lactamase found in Escherichia coli. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3005219 CMY-144 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-144 is a beta-lactamase found in Citrobacter freundii. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3005220 CMY-138 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-138 is a beta-lactamase found in Proteus mirabilis. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3005221 MCR-3.41 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase Novel mcr-3.41 gene identified in an Aeromonas veronii C198 isolate from a patient with Septicemia in Thailand by Hatrongjit et. al. http://purl.obolibrary.org/obo/ARO_3005222 OXA-544 http://purl.obolibrary.org/obo/ARO_3007704 OXA-2-like beta-lactamase OXA-544 is a beta-lactamase in the OXA-2 family of OXA beta-lactamases that confers resistance to ampicillin and cephalothin. http://purl.obolibrary.org/obo/ARO_3005223 SHV-194 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase Beta-lactamase gene from Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3005224 SHV-220 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase Beta-lactamase gene from Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3005225 SHV-210 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase Beta-lactamase gene from Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3005226 SHV-208 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase A beta-lactamase gene found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3005227 SHV-206 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase A beta-lactamase gene from Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3005228 SHV-226 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase A beta-lactamase gene found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3005229 SHV-196 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase A beta-lactamase gene found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3005230 SHV-211 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase A beta-lactamase gene found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3005231 SHV-219 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase Beta-lactamase gene from Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3005232 SHV-199 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase A beta-lactamase gene found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3005233 SHV-227 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase Beta-lactamase gene from Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3005234 SHV-223 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase A beta-lactamase gene found in Klebsiella pneumonia. http://purl.obolibrary.org/obo/ARO_3005235 SHV-214 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase A beta-lactamase gene found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3005236 SHV-207 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase A beta-lactamase gene found in Klebsiella penumoniae. http://purl.obolibrary.org/obo/ARO_3005237 SHV-1b-b http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase A beta-lactamase gene found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3005238 SHV-218 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase A beta-lactamase gene found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3005239 SHV-193 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase A beta-lactamase gene found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3005240 SHV-224 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase A beta-lactamase gene found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3005241 SHV-225 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase A beta-lactamase gene found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3005242 SHV-209 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase A beta-lactamase gene found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3005243 SHV-215 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase A beta-lactamase gene found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3005244 ADC-181 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC ortholog described by Nodari et al. 2020. http://purl.obolibrary.org/obo/ARO_3005245 ADC-182 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC ortholog described by Nodari et al. 2020. http://purl.obolibrary.org/obo/ARO_3005246 ADC-183 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC ortholog described by Nodari et al. 2020. http://purl.obolibrary.org/obo/ARO_3005247 SHV-228 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase A beta-lactamase gene found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3005248 SHV-200 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase A beta-lactamase gene found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3005249 SHV-203 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase A beta-lactamase gene found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3005250 SHV-217 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase A beta-lactamase gene found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3005251 SHV-213 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase A beta-lactamase gene found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3005252 SHV-221 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase A beta-lactamase gene found in Klebsiella pneumonia. http://purl.obolibrary.org/obo/ARO_3005253 SHV-202 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase A beta-lactamase gene found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3005255 TEM-224 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-224 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005256 TEM-225 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-225 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005257 TEM-226 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-226 is a beta lactamase. http://purl.obolibrary.org/obo/ARO_3005258 TEM-227 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-227 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005259 TEM-228 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-228 is a beta lactamase. http://purl.obolibrary.org/obo/ARO_3005260 TEM-229 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-229 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005261 TEM-230 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-230 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005262 TEM-231 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-231 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005263 TEM-232 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-232 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005264 TEM-233 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-233 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005265 TEM-234 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-234 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005266 TEM-235 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-235 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005267 TEM-236 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-236 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005268 TEM-237 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-237 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005269 TEM-238 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-238 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005270 TEM-240 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-240 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005271 TEM-241 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-241 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005272 TEM-242 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-242 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005273 TEM-243 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-243 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005274 PDC-225 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-225 is a class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005275 PDC-438 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-438 is class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005276 PDC-284 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-284 is a class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005277 PDC-105 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-105 is a class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005278 PDC-118 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-118 is a class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005279 PDC-324 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-324 is a class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005280 PDC-323 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-323 is a class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005281 PDC-258 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-258 is a class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005282 PDC-413 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-413 is a class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005283 PDC-384 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-384 is a class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005284 PDC-264 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-264 is a class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005285 PDC-201 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-201 is a class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005286 PDC-346 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-346 is a class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005287 PDC-285 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-285 is a class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005288 PDC-337 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-337 is a class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005289 PDC-212 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-212 is a class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005290 PDC-352 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-352 is a class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005291 PDC-464 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-464 is a class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005292 PDC-19b http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-19b is a class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005293 PDC-380 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-380 is a class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005294 PDC-461 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-461 is a class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005295 PDC-19a http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-19a is a class C beta-lactamase found in Pseudomonas (multispecies). http://purl.obolibrary.org/obo/ARO_3005296 PDC-272 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-272 is a class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005297 PDC-255 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-255 is a class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005298 PDC-293 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-293 is a class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005299 PDC-183 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-183 is a class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005300 PDC-207 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-207 is a class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005301 PDC-306 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-306 is a class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005302 PDC-376 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-376 is a class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005303 PDC-117 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-117 is a class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005304 PDC-231 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-231 is a class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005305 PDC-104 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-104 is a class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005306 PDC-173 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-173 is a class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005307 PDC-292 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-292 is a class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005308 PDC-393 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-393 is a class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005309 PDC-119 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-119 is a class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005310 PDC-313 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-313 is a class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005311 PDC-257 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-257 is a class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005312 PDC-429 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-429 is a class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005313 PDC-449 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-449 is a class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005314 OXA-540 http://purl.obolibrary.org/obo/ARO_3007704 OXA-2-like beta-lactamase OXA-540 is a beta-lactamase in the OXA-2 family of OXA beta-lactamases that confers resistance to ampicillin and cephalothin. http://purl.obolibrary.org/obo/ARO_3005315 OXA-779 http://purl.obolibrary.org/obo/ARO_3007720 OXA-46-like beta-lactamase OXA-779 is a beta-lactamase in the OXA-46 family of OXA beta-lactamases that confers resistance to ampicillin and cephalothin. http://purl.obolibrary.org/obo/ARO_3005316 OXA-838 http://purl.obolibrary.org/obo/ARO_3007704 OXA-2-like beta-lactamase OXA-838 is a beta-lactamase in the OXA-2 family of OXA beta-lactamases that confers resistance to ampicillin and cephalothin. http://purl.obolibrary.org/obo/ARO_3005317 OXA-539 http://purl.obolibrary.org/obo/ARO_3007704 OXA-2-like beta-lactamase OXA-539 is a beta-lactamase in the OXA-2 family of OXA beta-lactamases that confers resistance to ampicillin and cephalothin. http://purl.obolibrary.org/obo/ARO_3005318 OXA-543 http://purl.obolibrary.org/obo/ARO_3007704 OXA-2-like beta-lactamase OXA-543 is a beta-lactamase in the OXA-2 family of OXA beta-lactamases that confers resistance to ampicillin and cephalothin. http://purl.obolibrary.org/obo/ARO_3005319 OXA-681 http://purl.obolibrary.org/obo/ARO_3007704 OXA-2-like beta-lactamase OXA-681 is a beta-lactamase in the OXA-2 family of OXA beta-lactamases that confers resistance to ampicillin and cephalothin. http://purl.obolibrary.org/obo/ARO_3005320 OXA-737 http://purl.obolibrary.org/obo/ARO_3007704 OXA-2-like beta-lactamase OXA-737 is a beta-lactamase in the OXA-2 family of OXA beta-lactamases that confers resistance to ampicillin and cephalothin. http://purl.obolibrary.org/obo/ARO_3005321 OXA-541 http://purl.obolibrary.org/obo/ARO_3007704 OXA-2-like beta-lactamase OXA-541 is a beta-lactamase in the OXA-2 family of OXA beta-lactamases that confers resistance to ampicillin and cephalothin. http://purl.obolibrary.org/obo/ARO_3005322 OXA-835 http://purl.obolibrary.org/obo/ARO_3007720 OXA-46-like beta-lactamase OXA-835 is a beta-lactamase in the OXA-46 family of OXA beta-lactamases that confers resistance to ampicillin and cephalothin. http://purl.obolibrary.org/obo/ARO_3005323 OXA-926 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-926 is a class D beta-lactamase in the family of OXA beta-lactamases that confers resistance to ampicillin and cephalothin. http://purl.obolibrary.org/obo/ARO_3005324 OXA-570 http://purl.obolibrary.org/obo/ARO_3007729 OXA-60-like beta-lactamase OXA-570 is a beta-lactamase in the OXA-60 family of OXA beta-lactamases that confers resistance to ampicillin and cephalothin. http://purl.obolibrary.org/obo/ARO_3005325 OXA-573 http://purl.obolibrary.org/obo/ARO_3007729 OXA-60-like beta-lactamase OXA-573 is a beta-lactamase in the OXA-60 family of OXA beta-lactamases that confers resistance to ampicillin and cephalothin. http://purl.obolibrary.org/obo/ARO_3005326 OXA-571 http://purl.obolibrary.org/obo/ARO_3007729 OXA-60-like beta-lactamase OXA-571 is a beta-lactamase in the OXA-60 family of OXA beta-lactamases that confers resistance to ampicillin and cephalothin. http://purl.obolibrary.org/obo/ARO_3005327 OXA-672 http://purl.obolibrary.org/obo/ARO_3007714 OXA-286-like beta-lactamase OXA-672 is a beta-lactamase in the OXA-286 family of OXA beta-lactamases that confers resistance to ampicillin and cephalothin. http://purl.obolibrary.org/obo/ARO_3005328 OXA-671 http://purl.obolibrary.org/obo/ARO_3007714 OXA-286-like beta-lactamase OXA-671 is a beta-lactamase in the OXA-286 family of OXA beta-lactamases that confers resistance to ampicillin and cephalothin. http://purl.obolibrary.org/obo/ARO_3005329 OXA-673 http://purl.obolibrary.org/obo/ARO_3007714 OXA-286-like beta-lactamase OXA-673 is a beta-lactamase in the OXA-286 family of OXA beta-lactamases that confers resistance to ampicillin and cephalothin. http://purl.obolibrary.org/obo/ARO_3005330 OXA-931 http://purl.obolibrary.org/obo/ARO_3007709 OXA-229-like beta-lactamase OXA-931 is a beta-lactamase in the OXA-229 family of OXA beta-lactamases that confers resistance to ampicillin and cephalothin. http://purl.obolibrary.org/obo/ARO_3005331 OXA-930 http://purl.obolibrary.org/obo/ARO_3007709 OXA-229-like beta-lactamase OXA-930 is a beta-lactamase in the OXA-229 family of OXA beta-lactamases that confers resistance to ampicillin and cephalothin. http://purl.obolibrary.org/obo/ARO_3005332 OXA-895 http://purl.obolibrary.org/obo/ARO_3007709 OXA-229-like beta-lactamase OXA-895 is a beta-lactamase in the OXA-229 family of OXA beta-lactamases that confers resistance to ampicillin and cephalothin. http://purl.obolibrary.org/obo/ARO_3005333 OXA-641 http://purl.obolibrary.org/obo/ARO_3007717 OXA-372-like beta-lactamase OXA-641 is a beta-lactamase in the OXA-372 family of OXA beta-lactamases that confers resistance to ampicillin and cephalothin. http://purl.obolibrary.org/obo/ARO_3005334 Trimethoprim-resistant dihydrofolate reductase DfrA42 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr DfrA42 is a dihydrofolate reductase that confers resistant to Trimethoprim. http://purl.obolibrary.org/obo/ARO_3005335 OXA-496 http://purl.obolibrary.org/obo/ARO_3007700 OXA-134-like beta-lactamase OXA-496 is a beta-lactamase in the OXA-134 family of OXA beta-lactamases that confers resistance to ampicillin and cephalothin. http://purl.obolibrary.org/obo/ARO_3005336 OXA-915 http://purl.obolibrary.org/obo/ARO_3007700 OXA-134-like beta-lactamase OXA-915 is a beta-lactamase in the OXA-134 family of OXA beta-lactamases that confers resistance to ampicillin and cephalothin. http://purl.obolibrary.org/obo/ARO_3005337 OXA-647 http://purl.obolibrary.org/obo/ARO_3007700 OXA-134-like beta-lactamase OXA-647 is a beta-lactamase in the OXA-134 family of OXA beta-lactamases that confers resistance to ampicillin and cephalothin. http://purl.obolibrary.org/obo/ARO_3005338 OXA-648 http://purl.obolibrary.org/obo/ARO_3007700 OXA-134-like beta-lactamase OXA-648 is a beta-lactamase in the OXA-134 family of OXA beta-lactamases that confers resistance to ampicillin and cephalothin. http://purl.obolibrary.org/obo/ARO_3005339 OXA-646 http://purl.obolibrary.org/obo/ARO_3007700 OXA-134-like beta-lactamase OXA-646 is a beta-lactamase in the OXA-134 family of OXA beta-lactamases that confers resistance to ampicillin and cephalothin. http://purl.obolibrary.org/obo/ARO_3005340 OXA-649 http://purl.obolibrary.org/obo/ARO_3007701 OXA-143-like beta-lactamase OXA-649 is a beta-lactamase in the OXA-143 family of OXA beta-lactamases that confers resistance to ampicillin and cephalothin. http://purl.obolibrary.org/obo/ARO_3005341 OXA-897 http://purl.obolibrary.org/obo/ARO_3007711 OXA-24-like beta-lactamase OXA-897 is a beta-lactamase in the OXA-24 family of OXA beta-lactamases that confers resistance to ampicillin and cephalothin. http://purl.obolibrary.org/obo/ARO_3005342 OXA-653 http://purl.obolibrary.org/obo/ARO_3007711 OXA-24-like beta-lactamase OXA-653 is a beta-lactamase in the OXA-24 family of OXA beta-lactamases that confers resistance to ampicillin and cephalothin. http://purl.obolibrary.org/obo/ARO_3005343 OXA-499 http://purl.obolibrary.org/obo/ARO_3007701 OXA-143-like beta-lactamase OXA-499 is a beta-lactamase in the OXA-143 family of OXA beta-lactamases that confers resistance to ampicillin and cephalothin. http://purl.obolibrary.org/obo/ARO_3005344 OXA-825 http://purl.obolibrary.org/obo/ARO_3007701 OXA-143-like beta-lactamase OXA-825 is a beta-lactamase in the OXA-143 family of OXA beta-lactamases that confers resistance to ampicillin and cephalothin. http://purl.obolibrary.org/obo/ARO_3005345 Trimethoprim-resistant dihydrofolate reductase DfrA43 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr DfrA43 is a dihydrofolate reductase that confers resistance to Trimethoprim. Originially described by Shi YZ et al, 2016, and isolated from Proteus penneri. http://purl.obolibrary.org/obo/ARO_3005346 DfrA34 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr DfrA34 is a dihydrofolate reductase that confers resistant to Trimethoprim. http://purl.obolibrary.org/obo/ARO_3005347 DfrA37 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr DfrA37 is a dihydrofolate reductase that confers resistant to Trimethoprim. http://purl.obolibrary.org/obo/ARO_3005348 DfrA36 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr DfrA36 is a dihydrofolate reductase that confers resistant to Trimethoprim. Originally described by Wuthrich et al., 2019, and isolated from Escherichia coli. http://purl.obolibrary.org/obo/ARO_3005349 DfrA38 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr DfrA38 is a dihydrofolate reductase that confers resistant to Trimethoprim. http://purl.obolibrary.org/obo/ARO_3005350 DfrB9 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr DfrB9 is a dihydrofolate reductase that confers resistant to Trimethoprim. http://purl.obolibrary.org/obo/ARO_3005351 DfrA39 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr DfrA39 is a dihydrofolate reductase that confers resistant to Trimethoprim. http://purl.obolibrary.org/obo/ARO_3005354 dfr22 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr Dfr22 is a dihydrofolate reductase that confers resistant to Trimethoprim. Originally detected by Grape et al., (2005) and isolated from Escherichia coli. http://purl.obolibrary.org/obo/ARO_3005356 KPC-23 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase kpc-23 [Klebsiella pneumoniae] Accession: WP_111672911.1. http://purl.obolibrary.org/obo/ARO_3005357 KPC-25 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase kpc-25 [Klebsiella pneumoniae] Accession: WP_065419571.1. http://purl.obolibrary.org/obo/ARO_3005358 KPC-26 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase kpc-26 [Klebsiella pneumoniae] Accession: WP_068981634.1. http://purl.obolibrary.org/obo/ARO_3005359 KPC-27 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase kpc-27 [Klebsiella pneumoniae] Accession: WP_077064886.1. http://purl.obolibrary.org/obo/ARO_3005360 KPC-29 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase kpc-29 [Klebsiella pneumoniae] Accession: WP_096807439.1. http://purl.obolibrary.org/obo/ARO_3005361 KPC-28 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant class A extended-spectrum beta-lactamase kpc-28 [Escherichia coli] Accession: WP_072081992.1. http://purl.obolibrary.org/obo/ARO_3005362 KPC-31 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase kpc-31 [Klebsiella] Accession: WP_073668892.1. http://purl.obolibrary.org/obo/ARO_3005363 KPC-32 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase kpc-32 [Klebsiella pneumoniae] Accession: WP_073800284.1. http://purl.obolibrary.org/obo/ARO_3005364 KPC-30 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase kpc-30 [Klebsiella pneumoniae] Accession: WP_085562399.1. http://purl.obolibrary.org/obo/ARO_3005365 KPC-33 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant class A extended-spectrum beta-lactamase kpc-33 [Klebsiella pneumoniae] Accession: WP_101140102.1. http://purl.obolibrary.org/obo/ARO_3005366 KPC-34 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase kpc-34 [Klebsiella pneumoniae] Accession: WP_109545044.1. http://purl.obolibrary.org/obo/ARO_3005367 KPC-35 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase kpc-35 [Klebsiella pneumoniae] Accession: WP_111273852.1. http://purl.obolibrary.org/obo/ARO_3005368 KPC-36 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase kpc-36 [Klebsiella pneumoniae] Accession: WP_114699267.1. http://purl.obolibrary.org/obo/ARO_3005369 KPC-37 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase kpc-37 [Klebsiella pneumoniae] Accession: WP_116786832.1. http://purl.obolibrary.org/obo/ARO_3005370 KPC-38 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase kpc-38 [Klebsiella pneumoniae] Accession: WP_123002101.1. http://purl.obolibrary.org/obo/ARO_3005371 KPC-39 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase kpc-39 [Klebsiella pneumoniae] Accession: WP_128268237.1. http://purl.obolibrary.org/obo/ARO_3005372 KPC-40 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase kpc-40 [Enterobacter hormaechei] Accession: WP_115470049.1. http://purl.obolibrary.org/obo/ARO_3005373 KPC-41 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase kpc-41 [Klebsiella pneumoniae] Accession: WP_148044419.1. http://purl.obolibrary.org/obo/ARO_3005374 KPC-42 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase kpc-42 [Klebsiella pneumoniae] Accession: WP_136512070.1. http://purl.obolibrary.org/obo/ARO_3005375 KPC-43 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase kpc-43 [Klebsiella pneumoniae] Accession: WP_136512071.1. http://purl.obolibrary.org/obo/ARO_3005376 KPC-45 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase kpc-45 [Enterobacter cloacae] Accession: WP_148044420.1. http://purl.obolibrary.org/obo/ARO_3005377 KPC-46 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant class A extended-spectrum beta-lactamase kpc-46 [Klebsiella pneumoniae] Accession: WP_148044421.1. http://purl.obolibrary.org/obo/ARO_3005378 KPC-49 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase kpc-49 [Escherichia coli] Accession: WP_197749402.1. http://purl.obolibrary.org/obo/ARO_3005379 KPC-50 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant class A beta-lactamase kpc-50 [Klebsiella pneumoniae] Accession: WP_171476788.1. http://purl.obolibrary.org/obo/ARO_3005380 KPC-51 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant class A extended-spectrum beta-lactamase kpc-51 [Klebsiella pneumoniae] Accession: WP_158208923.1. http://purl.obolibrary.org/obo/ARO_3005381 KPC-52 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant class A extended-spectrum beta-lactamase kpc-52 [Klebsiella pneumoniae] Accession: WP_158208806.1. http://purl.obolibrary.org/obo/ARO_3005382 KPC-54 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase kpc-54 [Klebsiella pneumoniae] Accession: WP_160164839.1. http://purl.obolibrary.org/obo/ARO_3005383 KPC-55 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase kpc-55 [Klebsiella pneumoniae] Accession: WP_168247883.1. http://purl.obolibrary.org/obo/ARO_3005384 KPC-56 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase kpc-56 [Klebsiella pneumoniae] Accession: WP_087744800.1. http://purl.obolibrary.org/obo/ARO_3005385 KPC-57 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase kpc-57 [Klebsiella pneumoniae] Accession: WP_171476789.1. http://purl.obolibrary.org/obo/ARO_3005386 disinfecting agents and antiseptics http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule Disinfectants that can also interact with antimicrobial resistance mechanisms, e.g. molecule efflux, and thus are the targets of disinfectant resistance. http://purl.obolibrary.org/obo/ARO_3007128 serine beta-lactamase inhibitor http://purl.obolibrary.org/obo/ARO_3000042 beta-lactamase inhibitor Serine beta-lactamase inhibitors are molecules that inhibit the function of Ambler class A, C, and D beta-lactamases, preventing the inactivation of beta-lactam antibiotics by these enzymes. http://purl.obolibrary.org/obo/ARO_3007129 metallo-beta-lactamase inhibitor http://purl.obolibrary.org/obo/ARO_3000042 beta-lactamase inhibitor Metallo-beta-lactamase inhibitors are molecules that inhibit the function of Ambler class B (metallo-) beta-lactamases, preventing the inactivation of beta-lactam antibiotics by these enzymes. http://purl.obolibrary.org/obo/ARO_3007130 beta-lactam derived beta-lactamase inhibitor http://purl.obolibrary.org/obo/ARO_3007128 serine beta-lactamase inhibitor Beta-lactam derived beta-lactamase inhibitors are molecules possessing structural similarity to beta-lactam antibiotics (i.e. beta-lactam ring) that inhibit the function of serine beta-lactamases. http://purl.obolibrary.org/obo/ARO_3007131 boronic acid beta-lactamase inhibitor http://purl.obolibrary.org/obo/ARO_3007128 serine beta-lactamase inhibitor A class of serine beta-lactamase inhibitors. http://purl.obolibrary.org/obo/ARO_3007132 unclassified serine beta-lactamase inhibitor http://purl.obolibrary.org/obo/ARO_3007128 serine beta-lactamase inhibitor Serine beta-lactamase inhibitors with unknown or undefined classification. http://purl.obolibrary.org/obo/ARO_3007133 polypyridine metallo-beta-lactamase inhibitor http://purl.obolibrary.org/obo/ARO_3007129 metallo-beta-lactamase inhibitor A class of metallo-beta-lactamase inhibitors. http://purl.obolibrary.org/obo/ARO_3007134 phosphonate metallo-beta-lactamase inhibitor http://purl.obolibrary.org/obo/ARO_3007129 metallo-beta-lactamase inhibitor A class of metallo-beta-lactamase inhibitors. http://purl.obolibrary.org/obo/ARO_3007135 bisthiazolidine metallo-beta-lactamase inhibitor http://purl.obolibrary.org/obo/ARO_3007129 metallo-beta-lactamase inhibitor A class of metallo-beta-lactamase inhibitors. http://purl.obolibrary.org/obo/ARO_3007136 unclassified metallo-beta-lactamase inhibitor http://purl.obolibrary.org/obo/ARO_3007129 metallo-beta-lactamase inhibitor Metallo-beta-lactamase inhibitors with unknown or undefined classification. http://purl.obolibrary.org/obo/ARO_3007137 mcr-10.1 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-10-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007138 S02030 http://purl.obolibrary.org/obo/ARO_3007136 unclassified metallo-beta-lactamase inhibitor S02030 is an experimental metallo-beta-lactamase inhibitor that exhibits activity against MOX-1. http://purl.obolibrary.org/obo/ARO_3007139 cordycepin http://purl.obolibrary.org/obo/ARO_3000034 nucleoside antibiotic Cordycepin is an experimental nucleoside antibiotic which has been shown to exhibit activity against H. pylori. It is produced by the Cordyceps fungus, which is used in traditional Chinese medicine. http://purl.obolibrary.org/obo/ARO_3007140 unithiol http://purl.obolibrary.org/obo/ARO_3007136 unclassified metallo-beta-lactamase inhibitor Unithiol is an experimental chelating agent that forms complexes with heavy metals. It has been shown to inhibit the action of the metallo-beta-lactamases NDM-1 and VIM-2. http://purl.obolibrary.org/obo/ARO_3007141 BLI-489 http://purl.obolibrary.org/obo/ARO_3007130 beta-lactam derived beta-lactamase inhibitor BLI-489 is an experimental beta-lactamase inhibitor that exhibits broad spectrum activity against class A, B, and D carbapenemases. http://purl.obolibrary.org/obo/ARO_3007142 plantacirin A http://purl.obolibrary.org/obo/ARO_3007223 adjuvants enhancing antibiotic entry Plantacirin A is a short cationic bacteriocin that increases permeability of the bacterial outer membrane, thus enhancing the effect of accompanying antibiotics. It is derived from Lactiplantibacillus plantarum. http://purl.obolibrary.org/obo/ARO_3007143 sulopenem http://purl.obolibrary.org/obo/ARO_0000020 carbapenem Sulopenem is a carbapenem derivative in phase III clinical trials (2022) for the treatment of various gram-positive and gram-negative infections. http://purl.obolibrary.org/obo/ARO_3007144 PBT2 http://purl.obolibrary.org/obo/ARO_3007223 adjuvants enhancing antibiotic entry PBT2 is a former Alzheimer's and Huntington's disease candidate drug that has since been shown to increase susceptibility to colistin, polymyxin B, and tetracycline in N. gonorrhoeae. It is thought to inactivate lipooligosaccharide phosphoethanolamine transferase A, resulting in alteration of cell membrane charge. http://purl.obolibrary.org/obo/ARO_3007145 imipenem-cilastatin-relebactam http://purl.obolibrary.org/obo/ARO_3000707 antibiotic mixture An antibiotic-adjuvant admixture of the beta-lactam antibiotic imipenem, beta-lactam potentiator cilastatin, and beta-lactamase inhibitor relebactam. http://purl.obolibrary.org/obo/ARO_3007146 meropenem-vaborbactam http://purl.obolibrary.org/obo/ARO_3000707 antibiotic mixture An antibiotic-adjuvant admixture of the beta-lactam antibiotic meropenem and the beta-lactamase inhibitor vaborbactam. http://purl.obolibrary.org/obo/ARO_3007147 taniborbactam http://purl.obolibrary.org/obo/ARO_3007136 unclassified metallo-beta-lactamase inhibitor Taniborbactam is a broad-spectrum beta-lactamase inhibitor. As of 2022, it is in phase III clinical trials in combination with cefepime and is the only beta-lactamase inhibitor exhibiting activity against all four classes of beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007148 cefepime-taniborbactam http://purl.obolibrary.org/obo/ARO_3000707 antibiotic mixture An antibiotic cocktail containing the beta-lactam antibiotic cefepime and the beta-lactamase inhibitor taniborbactam. As of 2022, this antibiotic-adjuvant mixture is in phase III clinical trials for the treatment of various bacterial infections. http://purl.obolibrary.org/obo/ARO_3007149 phosphonic acid antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule A group of antibiotics derived from phosphonic acids. http://purl.obolibrary.org/obo/ARO_3007150 bicyclomycin-like antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule A group of antibiotics including bicyclomycin and its analogues. http://purl.obolibrary.org/obo/ARO_3007151 mupirocin-like antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule A group of antibiotics including mupirocin and similar mixtures (such as those including pseudomonic acid A). http://purl.obolibrary.org/obo/ARO_3007152 isoniazid-like antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule A group of antibiotics containing isoniazid and its derivatives. http://purl.obolibrary.org/obo/ARO_3007153 fusidane antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule A group of antibiotics possessing steroid rings or steroid-like structures. http://purl.obolibrary.org/obo/ARO_3007154 cycloserine-like antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule A group of antibiotics including cycloserine and its derivatives. http://purl.obolibrary.org/obo/ARO_3007155 pyrazine antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule A group of antibiotics derived from pyrazine. http://purl.obolibrary.org/obo/ARO_3007156 thioamide antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule A group of antibiotics possessing the thioamide functional group. http://purl.obolibrary.org/obo/ARO_3007157 nybomycin-like antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule A group of antibiotics including nybomycin and its derivatives. http://purl.obolibrary.org/obo/ARO_3007158 pactamycin-like antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule A group of antibiotics including pactamycin and its derivatives. http://purl.obolibrary.org/obo/ARO_3007159 salicylic acid antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule A group of antibiotics derived from salicylic acid. http://purl.obolibrary.org/obo/ARO_3007160 zoliflodacin-like antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule A group of antibiotics including the experimental compound zoliflodacin and its derivatives. http://purl.obolibrary.org/obo/ARO_3007161 thiosemicarbazone antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule A group of antibiotics derived from thiosemicarbazide (possessing the thiosemicarbazone functional group). http://purl.obolibrary.org/obo/ARO_3007162 protegrin-1-like antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule A group of peptidomimetic antibiotics based on the peptide protegrin-1. http://purl.obolibrary.org/obo/ARO_3007163 albendazole-like antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule A group of antibiotics including albendazole and similar antiparasitic compounds that exhibit antibacterial activity. http://purl.obolibrary.org/obo/ARO_3007164 triazaacenaphthylene antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule A group of antibiotics derived from triazaacenaphthylene. http://purl.obolibrary.org/obo/ARO_3007165 gemifloxacin http://purl.obolibrary.org/obo/ARO_0000001 fluoroquinolone antibiotic Gemifloxacin is a broad-spectrum, fourth generation, oral fluoroquinolone antibiotic used in the treatment of various bacterial infections, primarily in the lungs. It has been discontinued for therapeutic use in the US over concerns of tendon and peripheral neuron toxicity, although it is still available for experimental application and elsewhere for therapeutic use. It is usually administered as a mesylate salt, gemifloxacin mesylate. http://purl.obolibrary.org/obo/ARO_3007166 orthosomycin antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule Orthosomycins are a group of experimental/veterinary orthoester and oligosaccharide antibiotics that target the 70s ribosomal subunit. They are generally no longer considered potential clinical antibiotics, but continue to be used in livestock feed and for experimental purposes. http://purl.obolibrary.org/obo/ARO_3007167 evernimicin http://purl.obolibrary.org/obo/ARO_3007166 orthosomycin antibiotic Evernimicin is a veterinary oligosaccharide antibiotic of the orthosomycin group of orthoester antibiotics. Along with avilamycin, it exhibits activity against a variety of Gram-positive and -negative bacteria and is primarily used in livestock feed. http://purl.obolibrary.org/obo/ARO_3007168 avalimycin http://purl.obolibrary.org/obo/ARO_3007166 orthosomycin antibiotic Avilamycin is an experimental oligosaccharide antibiotic of the orthosomycin group of orthoester antibiotics. Along with evernimicin, it exhibits activity against a variety of Gram-positive and -negative bacteria. http://purl.obolibrary.org/obo/ARO_3007169 pirlimycin http://purl.obolibrary.org/obo/ARO_0000017 lincosamide antibiotic Pirlimycin is an experimental/veterinary lincosamide antibiotic. Although not approved for use in humans, pirlimycin is commonly used to treat mammary gland infections in cattle. http://purl.obolibrary.org/obo/ARO_3007171 enmetazobactam http://purl.obolibrary.org/obo/ARO_3007130 beta-lactam derived beta-lactamase inhibitor Enmetazobactam is a beta-lactamase inhibitor which exhibits activity against class A extended spectrum beta-lactamases. It is currently in clinical trials in combination with cefepine for the treatment of urinary tract infections and acute pyelonephritis. http://purl.obolibrary.org/obo/ARO_3007172 methimazole http://purl.obolibrary.org/obo/ARO_3007136 unclassified metallo-beta-lactamase inhibitor Methimazole is thiamide usually used to treat hyperthyroidism. It has also demonstrated potent inhibition of NDM-1 and synergistic effects against other metallo-beta-lactamases when paired with meropenem. http://purl.obolibrary.org/obo/ARO_3007173 lipoic acid http://purl.obolibrary.org/obo/ARO_3007136 unclassified metallo-beta-lactamase inhibitor Lipoic acid is a compound used for diabetic neuropathy and as a nutritional supplement. It has also demonstrated potent inhibition of NDM-1 and synergistic effects against other metallo-beta-lactamases when paired with meropenem. http://purl.obolibrary.org/obo/ARO_3007174 scutellarin http://purl.obolibrary.org/obo/ARO_3007222 inhibitor of antibiotic resistance mechanism Scutellarin is an experimental antibiotic potentiator that inhibits bacterial sortase A and caseinolytic peptidase P. When used in combination with vancomycin against methicillin-resistant Staphylococcus aureus, scutellarin improves activity of the antibiotic, making it an effective adjuvant in the treatment of such infections. http://purl.obolibrary.org/obo/ARO_3007175 TP0586532 http://purl.obolibrary.org/obo/ARO_3007223 adjuvants enhancing antibiotic entry TP0586532 is an antibiotic potentiator that acts by inhibiting bacterial LpxC, interfering with the production of lipopolysaccharides. It has been shown to increase the effects of several antibiotics, such as meropenem, amikacin, cefepime, and tigecycline. The disruption of lipopolysaccharide synthesis is suspected to lead to increased membrane permeability. http://purl.obolibrary.org/obo/ARO_3007176 TNP-2198 http://purl.obolibrary.org/obo/ARO_3004115 nitroimidazole antibiotic TNP-2198 is an experimental rifamycin-nitroimidazole conjugate currently in development for treatment of several bacterial infections. It exhibits greater activity than rifamycin and nitroimidazole antibiotics administered together and is effective against bacteria resistant to both drug classes. http://purl.obolibrary.org/obo/ARO_3007177 thiazolide antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule Antibiotics belonging to the thiazolide group. Note that many thiazolides are used as antiviral compounds, however some have also exhibited antibacterial activity. http://purl.obolibrary.org/obo/ARO_3007178 nitazoxanide http://purl.obolibrary.org/obo/ARO_3007177 thiazolide antibiotic Nitazoxanide is a thiazolide antiparatasitic and antiviral drug that has demonstrated antibacterial activity against Helicobacter pylori. It is well tolerated and exhibits a synergistic effect with other antibiotics, such as clarithromycin. http://purl.obolibrary.org/obo/ARO_3007179 class A Mycobacterium abscessus beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase Class A beta-lactamse from M. abscessus. http://purl.obolibrary.org/obo/ARO_3007180 MAB http://purl.obolibrary.org/obo/ARO_3007179 class A Mycobacterium abscessus beta-lactamase MAB is a broad-spectrum class A beta-lactamase produced by Mycobacterium abscessus that has been shown to hydrolyze a large number of beta-lactam antibiotics. http://purl.obolibrary.org/obo/ARO_3007181 class A Mycobacterium tuberculosis bla beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase Class A beta-lactamase from M. tuberculosis. http://purl.obolibrary.org/obo/ARO_3007182 blaC http://purl.obolibrary.org/obo/ARO_3007181 class A Mycobacterium tuberculosis bla beta-lactamase blaC is a broad-spectrum class A beta-lactamase coded in the chromosome of Mycobacterium tuberculosis. It has been shown to hydrolyze a large number of beta-lactam antibiotics and is a major obstacle in the treatment of tuberculosis with such drugs. http://purl.obolibrary.org/obo/ARO_3007183 antibiotic resistant Rv1258c http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations in the Rv1258c (Tap) efflux pump contributing to antibiotic resistance. http://purl.obolibrary.org/obo/ARO_3007184 multidrug resistant Rv1258c http://purl.obolibrary.org/obo/ARO_3007183 antibiotic resistant Rv1258c Mutations in the Rv1258c efflux pump contributing to resistance to multiple antibiotics. http://purl.obolibrary.org/obo/ARO_3007185 Mycobacterium tuberculosis Rv1258c mutations confer resistance to ethambutol and capreomycin http://purl.obolibrary.org/obo/ARO_3007184 multidrug resistant Rv1258c Mutations in the M. tuberculosis efflux pump Rv1258c (Tap) conferring resistance to multiple ethambutol and capreomycin. http://purl.obolibrary.org/obo/ARO_3007186 Mycobacterium tuberculosis Rv1258c mutations confer resistance to pyrazinamide, isoniazid, and streptomycin http://purl.obolibrary.org/obo/ARO_3007184 multidrug resistant Rv1258c Mutations in the M. tuberculosis efflux pump Rv1258c (Tap) conferring resistance to pyrazinamide, isoniazid, and streptomycin. http://purl.obolibrary.org/obo/ARO_3007187 glycopeptide resistance gene cluster vanP http://purl.obolibrary.org/obo/ARO_3000234 glycopeptide resistance gene cluster This cluster confers resistance to both vancomycin and teicoplanin by allowing restructuring of peptidoglycan precursors to end in D-Ala-D-Lac. Resistance is acquired after multiple treatments with sub-minimum inhibitory concentrations of vancomycin. Gene orientation: vanHPXRS. http://purl.obolibrary.org/obo/ARO_3007188 vanH gene in vanP cluster http://purl.obolibrary.org/obo/ARO_3000006 vanH vanH variant in the vanP cluster. http://purl.obolibrary.org/obo/ARO_3007189 vanP http://purl.obolibrary.org/obo/ARO_3002978 D-Ala-D-Lac ligase vanP is a D-Ala-D-Ala ligase homolog that synthesizes D-Ala-D-Lac, an alternative substrate for peptidoglycan synthesis that reduces vancomycin binding affinity. It is associated with both vancomycin and teicoplanin resistance. http://purl.obolibrary.org/obo/ARO_3007190 vanX gene in vanP cluster http://purl.obolibrary.org/obo/ARO_3000011 vanX vanX variant in the vanP cluster. http://purl.obolibrary.org/obo/ARO_3007191 vanR gene in vanP cluster http://purl.obolibrary.org/obo/ARO_3000574 vanR vanR variant in the vanP cluster. http://purl.obolibrary.org/obo/ARO_3007192 vanS gene in vanP cluster http://purl.obolibrary.org/obo/ARO_3000071 vanS vanS variant in the vanP cluster. http://purl.obolibrary.org/obo/ARO_3007194 antimicrobial resistance surveillance systems http://purl.obolibrary.org/obo/ARO_3000045 component of AMR genotypic or phenotypic terminology Groups, organizations, and government bodies dedicated to the surveillance of antimicrobial resistance. http://purl.obolibrary.org/obo/ARO_3007195 National Antimicrobial Resistance Monitoring System (NARMS) http://purl.obolibrary.org/obo/ARO_3007194 antimicrobial resistance surveillance systems The National Antimicrobial Resistance Monitoring System for Enteric Bacteria (NARMS) is a US public health surveillance system that tracks antimicrobial resistance in foodborne and other enteric bacteria. http://purl.obolibrary.org/obo/ARO_3007685 nifuratel http://purl.obolibrary.org/obo/ARO_3004116 nitrofuran antibiotic Nifuratel is a nitrofuran antibiotic already in use for parasitic infections. It was effective against different serovars, including multidrug-resistant strains of Salmonella Typhimurium, and in macrophages from different host species and against Listeria monocytogenes and Shigella flexneri. It reduced IL-10 and STAT3 production in infected macrophages which should increase the inflammatory response against Salmonella. http://purl.obolibrary.org/obo/ARO_3007686 mutanobactin http://purl.obolibrary.org/obo/ARO_3000053 peptide antibiotic Mutanobactin is produced by a polyketide synthase-nonribosomal peptide synthetase hybrid system encoded by the mub locus. Mutanobactin-producing S. mutans inhibits planktonic and biofilm growth of E. faecalis and is active against other Enterococcus species and Staphylococcus aureus. http://purl.obolibrary.org/obo/ARO_3007687 zidovudine http://purl.obolibrary.org/obo/ARO_3000034 nucleoside antibiotic Zidovudine is an antibiotic used in the management and treatment of HIV-1. It is in the nucleoside reverse transcriptase inhibitor class of medications. http://purl.obolibrary.org/obo/ARO_3007688 menadione http://purl.obolibrary.org/obo/ARO_3007225 adjuvants which alter physiology Menadione exhibits antibacterial activity against methicillin-sensitive and methicillin-resistant S. aureus strains. When combined with oxacillin, it exhibited an additive and synergistic effect against the tested strains. Menadione demonstrated antibiofilm activity and effectively combated biofilms with reduced sensitivity to oxacillin alone. Its mechanism of action involves the production of reactive oxygen species (ROS) and DNA damage. It showed interactions with important targets, such as DNA gyrase and dehydroesqualene synthase. http://purl.obolibrary.org/obo/ARO_3007689 selamectin http://purl.obolibrary.org/obo/ARO_3001318 macrocyclic antibiotic Selamectin is a topical antiparasitic medication for dogs and cats prescribed for various parasite infections. Exposure caused relevant cell surface alterations. A synergistic effect was observed between ampicillin and selamectin. Selamectin may represent a timely and promising macrocyclic lactone for the treatment of S. aureus infections. http://purl.obolibrary.org/obo/ARO_3007690 antibiotic resistant Rv2535c http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Rv2535c or pepQ encodes a putative Xaa-Pro aminopeptidase and is a new genetic determinant of low-level bedaquiline and clofazimine cross-resistance in Mycobacterium tuberculosis when mutated. http://purl.obolibrary.org/obo/ARO_3007691 bedaquiline resistant Rv2535c http://purl.obolibrary.org/obo/ARO_3007690 antibiotic resistant Rv2535c Loss-of-function mutations in Rv2535c are a common mechanism of resistance. http://purl.obolibrary.org/obo/ARO_3007692 Mycobacterium tuberculosis Rv2535c with mutation conferring resistance to bedaquiline http://purl.obolibrary.org/obo/ARO_3007691 bedaquiline resistant Rv2535c These pepQ/Rv2535c mutations increase efflux through the mmpL5-mmpS5 (Rv0676c-Rv0677c) transporter, such as preventing degradation of MmpL5, which leads to reduced susceptibility to bedaquiline and clofazimine. http://purl.obolibrary.org/obo/ARO_3007693 AMZ beta-lactamase http://purl.obolibrary.org/obo/ARO_3000076 class C beta-lactamase The AMZ genes showed resistance against some beta-lactam antibiotics, including amoxicillin and cephalothin, and the beta-lactamase AMZ-1 exhibited a similar substrate spectrum response. Similar to other AmpC beta-lactamases, AMZ-1 is strongly inhibited by avibactam but much less strongly inhibited by tazobactam. http://purl.obolibrary.org/obo/ARO_3007694 AMZ-1 http://purl.obolibrary.org/obo/ARO_3007693 AMZ beta-lactamase Achromobacter mucicolens Y3, isolated from a goose on a farm in Wenzhou, showed resistance to multiple antibiotics, including penicillins and cephalosporins. AMZ-1 showed resistance to amoxicillin, penicillin G, ampicillin, cephalothin and cefoxitin, and the resistance activity could be inhibited by beta-lactamase inhibitors. http://purl.obolibrary.org/obo/ARO_3007695 CMY-185 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase We identified ceftazidime/avibactam resistance in E. coli associated with a novel CMY variant. Unlike other AmpC enzymes, CMY-185 appears to require an additional substitution on top of N346Y to confer ceftazidime/avibactam resistance. http://purl.obolibrary.org/obo/ARO_3007696 OXA-1-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase A subfamily of oxacillin-hydrolyzing class D OXA beta-lactamases derived from OXA-1. http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase A subfamily of extended-spectrum oxacillin-hydrolyzing class D OXA beta-lactamases derived from OXA-10. http://purl.obolibrary.org/obo/ARO_3007698 OXA-114-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase A subfamily of oxacillin-hydrolyzing class D OXA beta-lactamases derived from OXA-114. http://purl.obolibrary.org/obo/ARO_3007699 OXA-12-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase A subfamily of oxacillin-hydrolyzing class D OXA beta-lactamases derived from OXA-12. http://purl.obolibrary.org/obo/ARO_3007700 OXA-134-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase A subfamily of carbapenem-hydrolyzing class D OXA beta-lactamases derived from OXA-134. http://purl.obolibrary.org/obo/ARO_3007701 OXA-143-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase A subfamily of carbapenem-hydrolyzing class D OXA beta-lactamases derived from OXA-143. http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase A subfamily of oxacillin-hydrolyzing class D OXA beta-lactamases derived from OXA-184. http://purl.obolibrary.org/obo/ARO_3007703 OXA-198-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase A subfamily of carbapenem-hydrolyzing class D OXA beta-lactamases derived from OXA-198. http://purl.obolibrary.org/obo/ARO_3007704 OXA-2-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase A subfamily of extended-spectrum oxacillin-hydrolyzing class D OXA beta-lactamases derived from OXA-2. http://purl.obolibrary.org/obo/ARO_3007705 OXA-211-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase A subfamily of carbapenem-hydrolyzing class D OXA beta-lactamases derived from OXA-211. http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-213-like enzymes have been identified to be intrinsic to A. calcoaceticus and have been subsequently detected in A. pittii. Phylogenetic analysis of OXA-213-like proteins identified two distinct subgroups within the OXA family. The first group was linked to A. pittii and the second group to A. calcoaceticus. The carbapenemase activity of these OXAs may be related to the species-dependent effect. http://purl.obolibrary.org/obo/ARO_3007707 OXA-214-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase A subfamily of carbapenem-hydrolyzing class D OXA beta-lactamases derived from OXA-214. http://purl.obolibrary.org/obo/ARO_3007708 OXA-22-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase A subfamily of extended-spectrum oxacillin-hydrolyzing class D OXA beta-lactamases derived from OXA-22. http://purl.obolibrary.org/obo/ARO_3007709 OXA-229-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase A subfamily of carbapenem-hydrolyzing class D OXA beta-lactamases derived from OXA-229. http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase A subfamily of carbapenem-hydrolyzing class D OXA beta-lactamases, specifically imipenem, derived from OXA-23, first identified in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3007711 OXA-24-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase A subfamily of carbapenem-hydrolyzing class D OXA beta-lactamases derived from OXA-24. http://purl.obolibrary.org/obo/ARO_3007712 OXA-266-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase A subfamily of oxacillin-hydrolyzing class D OXA beta-lactamases derived from OXA-266. http://purl.obolibrary.org/obo/ARO_3007713 OXA-274-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase A subfamily of carbapenem-hydrolyzing class D OXA beta-lactamases derived from OXA-274. http://purl.obolibrary.org/obo/ARO_3007714 OXA-286-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase A subfamily of carbapenem-hydrolyzing class D OXA beta-lactamases derived from OXA-286. http://purl.obolibrary.org/obo/ARO_3007715 OXA-294-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase A subfamily of extended-spectrum oxacillin-hydrolyzing class D OXA beta-lactamases derived from OXA-294. http://purl.obolibrary.org/obo/ARO_3007716 OXA-364-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase A subfamily of oxacillin-hydrolyzing class D OXA beta-lactamases derived from OXA-364. http://purl.obolibrary.org/obo/ARO_3007717 OXA-372-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase A subfamily of carbapenem-hydrolyzing class D OXA beta-lactamases derived from OXA-372. http://purl.obolibrary.org/obo/ARO_3007718 OXA-42-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase A subfamily of extended-spectrum oxacillin-hydrolyzing class D OXA beta-lactamases derived from OXA-42. http://purl.obolibrary.org/obo/ARO_3007719 OXA-427-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase A subfamily of carbapenem-hydrolyzing class D OXA beta-lactamases derived from OXA-427. http://purl.obolibrary.org/obo/ARO_3007720 OXA-46-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase A subfamily of oxacillin-hydrolyzing class D OXA beta-lactamases derived from OXA-46. http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-48-type beta-lactamases are now routinely encountered in bacterial infections caused by carbapenam-resistant Enterobacterales. OXA-48-like proteins confer resistance to penicillin (which is efficiently hydrolyzed) and carbapenam antibiotics (which is more slowly broken down). The spectrum of activity of these variants varies, with some hydrolyzing expanded-spectrum oxyimino-cephalosporins. http://purl.obolibrary.org/obo/ARO_3007722 OXA-493-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase A subfamily of extended-spectrum oxacillin-hydrolyzing class D OXA beta-lactamases derived from OXA-493. http://purl.obolibrary.org/obo/ARO_3007723 OXA-5-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase A subfamily of oxacillin-hydrolyzing class D OXA beta-lactamases derived from OXA-5. http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase A subfamily of extended-spectrum oxacillin-hydrolyzing class D OXA beta-lactamases derived from OXA-50. http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase The maximum number of blaOXA belonged to the OXA-51-like subfamily. An earlier study had reported that OXA-51-like enzymes were present exclusively in A. baumannii. Similar to most of the other OXA-type carbapenemases, the OXA-51-like enzymes show weak carbapenemase activity; however, the presence of the insertion sequence ISAba1 upstream of the blaOXA-51-like gene may provide a promoter that allows the overproduction of carbapenemase, and this results in carbapenem resistance. http://purl.obolibrary.org/obo/ARO_3007726 OXA-548-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase A subfamily of oxacillin-hydrolyzing class D OXA beta-lactamases derived from OXA-548. http://purl.obolibrary.org/obo/ARO_3007727 OXA-55-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase A subfamily of carbapanem-hydrolyzing class D OXA beta-lactamases derived from OXA-55. http://purl.obolibrary.org/obo/ARO_3007728 OXA-58-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase A subfamily of carbapenem-hydrolyzing class D OXA beta-lactamases derived from OXA-58. http://purl.obolibrary.org/obo/ARO_3007729 OXA-60-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase A subfamily of carbapenem-hydrolyzing class D OXA beta-lactamases derived from OXA-60. http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase A subfamily of extended-spectrum oxacillin-hydrolyzing class D OXA beta-lactamases derived from OXA-61. http://purl.obolibrary.org/obo/ARO_3007731 OXA-62-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase A subfamily of carbapenem-hydrolyzing class D OXA beta-lactamases derived from OXA-62. http://purl.obolibrary.org/obo/ARO_3007732 OXA-63-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase A subfamily of extended-spectrum oxacillin-hydrolyzing class D OXA beta-lactamases derived from OXA-63. http://purl.obolibrary.org/obo/ARO_3007733 OXA-679-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase A subfamily of carbapenem-hydrolyzing class D OXA beta-lactamases derived from OXA-679. http://purl.obolibrary.org/obo/ARO_3007734 OXA-727-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase A subfamily of extended-spectrum oxacillin-hydrolyzing class D OXA beta-lactamases derived from OXA-727. http://purl.obolibrary.org/obo/ARO_3007735 OXA-9-like beta-lactamase http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase A subfamily of oxacillin-hydrolyzing class D OXA beta-lactamases derived from OXA-9. http://purl.obolibrary.org/obo/ARO_3007736 dexrazoxane http://purl.obolibrary.org/obo/ARO_3007222 inhibitor of antibiotic resistance mechanism Dexrazoxane is a medication used in the management and treatment of anthracycline-induced cardiotoxicity and extravasation injuries. It was demonstrated to inhibit all tested metallo-beta-lactamases and showed an in vitro synergistic bactericidal effect with meropenem against metallo-beta-lactamases-producing bacteria. Dexrazoxane is a metal ion chelating agent. http://purl.obolibrary.org/obo/ARO_3007745 nordihydroguaiaretic acid http://purl.obolibrary.org/obo/ARO_3007133 polypyridine metallo-beta-lactamase inhibitor Nordihydroguaiaretic acid (NDGA) is a phenolic lignan obtained from Larrea tridentata that has been used in traditional medicine for the treatment of diseases such as cancer, renal, cardiovascular, immunological, and neurological disorders, and even aging. The inhibition of NDM-1 by nordihydroguaiaretic acid involves its direct binding to the active region of NDM-1. http://purl.obolibrary.org/obo/ARO_3007746 embelin http://purl.obolibrary.org/obo/ARO_3007222 inhibitor of antibiotic resistance mechanism Embelin is a naturally occurring para-benzoquinone isolated from dried berries of Embelia ribes plants. Embelin has a wide spectrum of biological activities, including antioxidant, antitumor, anti-inflammatory, analgesic, anthelmintic, antifertility and antimicrobial. It was demonstrated to inhibit all tested metallo-beta-lactamases and showed an in vitro synergistic bactericidal effect with meropenem against metallo-beta-lactamases-producing bacteria. Embelin is a metal ion chelating agent. http://purl.obolibrary.org/obo/ARO_3007747 candesartan cilexetil http://purl.obolibrary.org/obo/ARO_3007222 inhibitor of antibiotic resistance mechanism Candesartan is an anti-hypertensive drug that was found to have antibacterial activity against MDR S. aureus. It was demonstrated to inhibit all tested metallo-beta-lactamases and showed an in vitro synergistic bactericidal effect with meropenem against metallo-beta-lactamases-producing bacteria. Candesartan is a metal ion chelating agent. http://purl.obolibrary.org/obo/ARO_3007748 oncocin http://purl.obolibrary.org/obo/ARO_3000053 peptide antibiotic The small proline-rich antimicrobial peptide, oncocin, selectively targets Gram-negative bacteria through special transporters such as SmbA to enter cytoplasm. It presents low toxicity to mammalian cells, because they cannot effectively penetrate the mammalian cellular membrane or they are internalized through an endocytotic process to minimize interaction with cytosolic ribosomes. http://purl.obolibrary.org/obo/ARO_3007749 Salmonella gallinarum folP with mutation conferring resistance to sulfonamides http://purl.obolibrary.org/obo/ARO_3003415 sulfonamide resistant dihydropteroate synthase folP Point mutations in Salmonella gallinarum dihydropteroate synthase folP altered the stability of the protein, thus conferring sulfonamide resistance. http://purl.obolibrary.org/obo/ARO_3007750 betaxolol http://purl.obolibrary.org/obo/ARO_3007136 unclassified metallo-beta-lactamase inhibitor Betaxolol is a selective beta1 receptor blocker used in the treatment of hypertension and angina, with a 50% inhibitory concentration (IC50) of 19.3 plus or minus 0.9 uM significantly inhibiting the hydrolytic activity of the NDM-1 enzyme and may represent a potential NDM-1 enzyme inhibitor. BET combined with meropenem (MEM) showed bactericidal synergism in vitro. BET inhibited NDM-1 by competitively binding to it and that it can be developed in combination with MEM as a new therapy. http://purl.obolibrary.org/obo/ARO_3007751 Salmonella isangi gyrA conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3003292 fluoroquinolone resistant gyrA Point mutations in Salmonella gyrA that confer resistance to ciprofloxacin and nalidixic acid which are fluoroquinolone antibiotics. http://purl.obolibrary.org/obo/ARO_3007752 Salmonella isangi gyrB conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3000864 fluoroquinolone resistant gyrB Point mutation in Salmonella isangi resulting in fluoroquinolone resistance. http://purl.obolibrary.org/obo/ARO_3007754 Lasalocid A http://purl.obolibrary.org/obo/ARO_3005171 polyketide with antibiotic activity Lasalocid is an antibacterial agent and a coccidiostat, which is produced by strains of Streptomyces lasaliensis. Lasalocid is able to make neutral complexes with monovalent and divalent cations and transport them through apolar phase. http://purl.obolibrary.org/obo/ARO_3007755 Calcimycin http://purl.obolibrary.org/obo/ARO_3005163 ionophore with antibiotic activity Calcimycin (A23187) is a polyether antibiotic and divalent cation ionophore, extracted from Streptomyces chartrecensis. http://purl.obolibrary.org/obo/ARO_3007756 ophiobolin A http://purl.obolibrary.org/obo/ARO_3005172 terpene with antibiotic activity Ophiobolin A is a sesterterpene which was initially isolated as fungal phytotoxins and subsequently shown to possess other biological activities, including anticancer activities. http://purl.obolibrary.org/obo/ARO_3007757 sphaeropsidin A http://purl.obolibrary.org/obo/ARO_3005172 terpene with antibiotic activity Sphaeropsidin A is a tetracyclic pimarane diterpene, first isolated as the main phytotoxin produced by Diplodia cupressir, the causal agent of a severe canker disease of Italian cypress, Cupressus sempervirens L. http://purl.obolibrary.org/obo/ARO_3007758 fengycin http://purl.obolibrary.org/obo/ARO_3000035 lipopeptide antibiotic Fengycin is an antifungal lipopeptide complex produced by Bacillus subtilis strain F-29-3. It inhibits filamentous fungi and is used as an agricultural fungicide. http://purl.obolibrary.org/obo/ARO_3007759 Treponema pallidum 23S rRNA with mutation conferring resistance to erythromycin http://purl.obolibrary.org/obo/ARO_3004125 23S rRNA with mutation conferring resistance to macrolide antibiotics Point mutations in 23S rRNA of Treponema pallidum subsp. pallidum (T. pallidum), the noncultivable agent of syphilis, shown clinically to confer resistance to erythromycin, a macrolide antibiotic. http://purl.obolibrary.org/obo/ARO_3009173 butenafine http://purl.obolibrary.org/obo/ARO_3009165 antifungal without defined classification This is a Benzylamine Antifungal which is believed to inhibit the squalene epoxidase enzyme that is essential in the formation of sterols necessary for fungal cell membranes. It is typically used in the treatment of dermatological infections. Butenafine is trimethylamine in which hydrogen atoms attached to different methyl groups are substituted by 1-naphthyl and 4-tert-butylphenyl groups. It is a tertiary amine and a member of naphthalenes. http://purl.obolibrary.org/obo/ARO_3009168 isopyrazam http://purl.obolibrary.org/obo/ARO_3009165 antifungal without defined classification A persisent and broad spectrum fungicide used for the control of Septoria tritici, rusts and other diseases in cereals and some other crops. It is tied to causing cancer. http://purl.obolibrary.org/obo/ARO_3009186 boscalid http://purl.obolibrary.org/obo/ARO_3009165 antifungal without defined classification Boscalid is a fungicide that is active against a broad range of fungal pathogens including Botrytis spp., Alternaria spp. and Sclerotinia spp. for use on a wide range of crops. It is functionally related to a nicotinic acid. Boscalid is unique in that it is a natural product derived from the fungi Ganoderma lucidum. http://purl.obolibrary.org/obo/ARO_3009178 diamide http://purl.obolibrary.org/obo/ARO_3009165 antifungal without defined classification Diamide is primarily used as an insecticide with evidence of mammalian toxicity. This compound is chemically classified as being part of the monoazo group. FungAMR listed this compound as having some anti-fungal properties. http://purl.obolibrary.org/obo/ARO_3009167 fludioxinil http://purl.obolibrary.org/obo/ARO_3009165 antifungal without defined classification A fungicide seed treatment for control of a range of diseases including Fusarium, Rhizoctonia and Alternaria. It has a role as an androgen antagonist, an estrogen receptor agonist and an antifungal agrochemical. It was noted as being the only fungicide still providing protection against multirestitant fungi. http://purl.obolibrary.org/obo/SYMP_0000092 skin lesion http://purl.obolibrary.org/obo/ARO_3004430 antimicrobial resistance tissue specificity Skin lesion is a skin and integumentary tissue symptom characterized as an abnormal change in structure of the skin that is especially circumscribed and well defined due to injury or disease. http://purl.obolibrary.org/obo/ARO_3004547 dfrA6 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr A dihydrofolate reductase and antibiotic resistance gene identified from an integron in Vibrio cholerae. http://purl.obolibrary.org/obo/ARO_3004548 dfrA9 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr A dihydrofolate reductase and trimethoprim resistance gene identified from porcine isolates of Esherichia coli. http://purl.obolibrary.org/obo/ARO_3004549 dfrB5 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr A dihydrofolate reductase and trimethoprim resistance gene identified from an integron in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3004550 dfrA27 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr A dihydrofolate reductase and trimethoprim resistance gene from non-O1, non-O139 Vibrio cholerae. http://purl.obolibrary.org/obo/ARO_3004551 dfrA28 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr A dihydrofolate reductase and trimethoprim resistance gene from Aeromonas hydrophilia. http://purl.obolibrary.org/obo/ARO_3004552 dfrA30 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr A dihydrofolate reductase and trimethoprim resistance gene from Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3004554 dfrA29 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr A dihydrofolate reductase and trimethoprim resistance gene isolated from canine Escherichia coli infection. http://purl.obolibrary.org/obo/ARO_3004555 dfrA32 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr A dihydrofolate reductase and trimethoprim resistance gene identified from non-typhoidal multidrug-resistant Salmonella enterica. http://purl.obolibrary.org/obo/ARO_3004556 dfrB7 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr A dihydrofolate reductase and trimethoprim resistance gene identified on an integron in multidrug-resistant gram-negative bacteria. http://purl.obolibrary.org/obo/ARO_3004558 CAM beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase CAM (Central Alberta Metallo) beta-lactamases are class B metallo-beta-lactamases and carbapenemases found to confer resistance to broad spectrum antibiotics in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3004559 CAM-1 http://purl.obolibrary.org/obo/ARO_3004558 CAM beta-lactamase CAM-1 is a CAM (Central Alberta Metallo) beta-lactamase and carbapenemase identified from 4 clinical isolates of Pseudomonas aeruginosa from a Canadian hospital. http://purl.obolibrary.org/obo/ARO_3004560 murG transferase http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant murG acetylglucosaminyltransferase enzymes inhibited by vancomycin. Mutations in murG confer resistance to vancomycin through antibiotic target alteration. http://purl.obolibrary.org/obo/ARO_3004561 Clostridioides difficile murG with mutation conferring resistance to vancomycin http://purl.obolibrary.org/obo/ARO_3004560 murG transferase Mutations in murG which confer resistance to vancomycin in Clostridioides difficile. http://purl.obolibrary.org/obo/ARO_3004562 Clostridioides difficile gyrB conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3000864 fluoroquinolone resistant gyrB Point mutations in gyrB of Clostridioides difficile conferring resistance to fluoroquinolone antibiotics. http://purl.obolibrary.org/obo/ARO_3004563 Clostridioides difficile rpoB with mutation conferring resistance to rifampicin http://purl.obolibrary.org/obo/ARO_3000210 rifamycin-resistant beta-subunit of RNA polymerase (rpoB) Point mutations in the rpoB region of Clostridioides difficile which confer resistance to rifampin and rifampicin antibiotics. http://purl.obolibrary.org/obo/ARO_3004564 unclassified resistance-modifying agents http://purl.obolibrary.org/obo/ARO_0000076 resistance-modifying agents Resistance-modifying agent (RMA) without characterized mechanism which do not exhibit antibiotic activity on their own, but improve the performance of antibiotic drugs. http://purl.obolibrary.org/obo/ARO_3004565 tetracyclic indoline http://purl.obolibrary.org/obo/ARO_3004564 unclassified resistance-modifying agents A class of resistance-modifying agents and beta-lactam potentiators which selectively potentiate beta-lactam antibiotics, specifically Amoxicillin-clavulanic acid, in methicillin-resistant Staphylococcus aureus (MRSA) without their own antimicrobial activity. http://purl.obolibrary.org/obo/ARO_3004566 Rifalazil http://purl.obolibrary.org/obo/ARO_3000157 rifamycin antibiotic Rifalazil is a rifamycin derivative antibiotic, sometimes used for treating Clostridioides difficile infections. http://purl.obolibrary.org/obo/ARO_3004567 Ramoplanin http://purl.obolibrary.org/obo/ARO_3000035 lipopeptide antibiotic Ramoplanin is a glycolipodepsipeptide antibiotic derived from gram-positive Actinoplanes used to treat infection with Clostridioides difficile. http://purl.obolibrary.org/obo/ARO_3004568 dfrA18 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr A trimethoprim-resistant dihydrofolate reductase identified from Vibrio cholerae. http://purl.obolibrary.org/obo/ARO_3004569 ICR-Mo http://purl.obolibrary.org/obo/ARO_3004465 intrinsic colistin resistant phosphoethanolamine transferase A chromosomally-encoded colistin resistance phosphoethanolamine (PEtN) transferase of Moraxella osloensis. ICR-Mo represents the closest known ortholog to the colistin resistance MCR-1 and MCR-2 PEtN transferases. http://purl.obolibrary.org/obo/ARO_3004570 PNGM beta-lactamase http://purl.obolibrary.org/obo/ARO_3000571 subclass B3 (metallo-) beta-lactamase PNGM is a family of metallo-beta-lactamases first identified from a deep-sea sediment metagenome and shown to reduce antibiotic susceptibility by hydrolysis of penicillins, carbapenems and extended- and broad-spectrum cephalosporins. http://purl.obolibrary.org/obo/ARO_3004571 PNGM-1 http://purl.obolibrary.org/obo/ARO_3004570 PNGM beta-lactamase PNGM-1 is a subclass B3 metallo-beta-lactamase first identified from a deep-sea sediment meta-genome. PNGM-1 is shown to reduce susceptibility to extended- and broad-spectrum cephalosporins, carbapenems, and penicillins. PNGM-1 is a novel metallo-beta-lactamase which predates the current antibiotic era. http://purl.obolibrary.org/obo/ARO_3004655 nimB http://purl.obolibrary.org/obo/ARO_3007103 nitroimidazole reductase nimB is a nitroimidazole reductase mainly found in Bacteroides fragilis that is associated with the deactivation of nitroimidazole antibiotics such as metronidazole. Minimum inhibitory concentrations observed in isolates vary greatly depending on species, strain, and nitroimidazole treatment. http://purl.obolibrary.org/obo/ARO_3007010 norC http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump NorC is a multidrug efflux pump in Staphylococcus aureus that confers resistance to fluoroquinolones and other structurally unrelated antibiotics like tetracycline. It shares 61% similarity with NorB, and is a structural homolog of Blt of Bacillus subtilis. Like NorA and NorB, NorC is regulated by mgrA, also known as NorR. http://purl.obolibrary.org/obo/ARO_3007011 mdeA http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump mdeA is a multidrug efflux pump that confers resistance in varying degrees to several unrelated antibiotics, including kanamycin, tetracycline, ampicillin, oxacillin, ciprofloxacin, nalidixic acid, acriflavine, and ethidium bromide. http://purl.obolibrary.org/obo/ARO_3007012 sepA http://purl.obolibrary.org/obo/ARO_0010003 small multidrug resistance (SMR) antibiotic efflux pump sepA is a multidrug efflux pump that confers resistance to disinfecting agents and dyes. http://purl.obolibrary.org/obo/ARO_3007013 sdrM http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump sdrM encodes an efflux pump that confers resistance to norfloxacin and ethidium bromide, making this a multidrug resistance gene. http://purl.obolibrary.org/obo/ARO_3007014 qacJ http://purl.obolibrary.org/obo/ARO_0010003 small multidrug resistance (SMR) antibiotic efflux pump qacJ is a small multidrug resistance (SMR) efflux pump that confers resistance to quaternary ammonium compounds. http://purl.obolibrary.org/obo/ARO_3007015 qacG http://purl.obolibrary.org/obo/ARO_0010003 small multidrug resistance (SMR) antibiotic efflux pump qacG is a small multidrug resistance efflux pump that confers resistance to benzalkonium chloride and ethidium bromide. http://purl.obolibrary.org/obo/ARO_3007016 SHD beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase SHD beta-lactamases are class B1 beta-lactamases found in Shewanella denitrificans. http://purl.obolibrary.org/obo/ARO_3007017 SHD-1 http://purl.obolibrary.org/obo/ARO_3007016 SHD beta-lactamase SHD-1 is a SHD beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007018 CARD Short Name http://purl.obolibrary.org/obo/ARO_3000045 component of AMR genotypic or phenotypic terminology A CARD-specific abbreviation for AMR gene names associated with Antibiotic Resistance Ontology terms, often not based on the literature. This is used for programmatic and compatibility purposes and is not ontologically relevant. Each ontology term with an associated AMR detection model has a CARD Short Name that appears in CARD data files and output generated by RGI. If the original gene name is less than 15 characters, the CARD short name is identical; if the gene name is greater than 15 characters, the CARD Short Name has been abbreviated by CARD curators specifically to identify the proper gene or protein name. All CARD Short Names are unique and have whitespace characters replaced by underscore characters. The convention for pathogen names is capitalized first letter of the genus followed by the lowercase first three letters of the species name. The antibiotic abbreviations are from https://journals.asm.org/journal/aac/abbreviations plus some custom abbreviations by the CARD curators. Simple CARD Short Names often do not involve either, e.g. CTX-M-15, but where applicable the CARD Short Names follow pathogen_gene or pathogen_gene_drug. The full lists of abbreviations can be found in the CARD Downloads: https://card.mcmaster.ca/latest/data. http://purl.obolibrary.org/obo/ARO_3007019 fexB http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump FexB is a plasmid-encoded exporter gene which confers resistance to florfenicol. Originally identified in Enterococcus sp. isolated from swine by Liu et al. 2012. http://purl.obolibrary.org/obo/ARO_3007021 PFM-4 http://purl.obolibrary.org/obo/ARO_3005432 PFM beta-lactamase PFM-4 (BioF) is a class B2 metallo-beta-lactamase first identified in Pseudomonas. It belongs to the PFM-like beta-lactamase gene family. It confers resistance to carbapenems and some cephalosporins. http://purl.obolibrary.org/obo/ARO_3007022 Prulifloxacin http://purl.obolibrary.org/obo/ARO_0000001 fluoroquinolone antibiotic Prulifloxacin is a 6-fluoroquinolone antibiotic with a C-2 sulfur atom. It is hydrolyzed by esterases to produce the active compound Ulifloxacin. The active compound has broad spectrum activity against most Gram-negative bacteria. Prulifloxacin displays strong bactericidal activity against Pseudomonas aeruginosa biofilms and persister cells. http://purl.obolibrary.org/obo/ARO_3007023 NDM-33 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase NDM-33 confers resistance to all beta-lactam antibiotics except aztreonam. It was first identified in an E. coli strain isolated from hospital sewage. It differs from NDM-5 by a single amino acid substitution (A72T). http://purl.obolibrary.org/obo/ARO_3007024 Lascufloxacin http://purl.obolibrary.org/obo/ARO_0000001 fluoroquinolone antibiotic Lascufloxacin is a fluoroquinolone antibiotic. http://purl.obolibrary.org/obo/ARO_3007025 Sarecycline http://purl.obolibrary.org/obo/ARO_3000050 tetracycline antibiotic Sarecycline is a tetracycline derivative. http://purl.obolibrary.org/obo/ARO_3007026 salB http://purl.obolibrary.org/obo/ARO_3007030 sal-type ABC-F protein salB is a ABC-F subfamily protein gene that confers resistance to lincosamides and class A streptogramins. http://purl.obolibrary.org/obo/ARO_3007027 salC http://purl.obolibrary.org/obo/ARO_3007030 sal-type ABC-F protein salC is a ABC-F subfamily protein gene that confers resistance to lincosamides and class A streptogramins. http://purl.obolibrary.org/obo/ARO_3007028 salD http://purl.obolibrary.org/obo/ARO_3007030 sal-type ABC-F protein salD is a ABC-F subfamily protein gene that confers resistance to lincosamides and class A streptogramins. http://purl.obolibrary.org/obo/ARO_3007029 salE http://purl.obolibrary.org/obo/ARO_3007030 sal-type ABC-F protein salE is a ABC-F subfamily protein gene that confers resistance to lincosamides and class A streptogramins. http://purl.obolibrary.org/obo/ARO_3007030 sal-type ABC-F protein http://purl.obolibrary.org/obo/ARO_3004469 ABC-F ATP-binding cassette ribosomal protection protein Sal proteins are a part of the ABC-F proteins, expressed in staphylococci that confer resistance to group A streptogramin, lincosamide, and pleuromutilin antibiotics through ribosomal protection. http://purl.obolibrary.org/obo/ARO_3007031 relebactam http://purl.obolibrary.org/obo/ARO_3007008 diazabicyclooctane A serine beta-lactamase inhibitor that prevents the degradation of imipenem in the body. http://purl.obolibrary.org/obo/ARO_3007032 Erm(50) http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase Erm(50) is an Erm ribosomal RNA methyltransferase. http://purl.obolibrary.org/obo/ARO_3007033 Erm(51) http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase Erm(51) is an Erm ribosomal RNA methyltransferase. http://purl.obolibrary.org/obo/ARO_3007034 tetracenomycin antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule Tetracenomycin antibiotics are aromatic polyketides that inhibit translation by binding to the large ribosomal subunit within the polypeptide exit tunnel. http://purl.obolibrary.org/obo/ARO_3007035 tetracenomycin C http://purl.obolibrary.org/obo/ARO_3007034 tetracenomycin antibiotic Tetracenomycin C is a tetracenomycin antibiotic, a methyl ester and a tertiary alpha-hydroxy ketone. http://purl.obolibrary.org/obo/ARO_3007036 tetracenomycin X http://purl.obolibrary.org/obo/ARO_3007034 tetracenomycin antibiotic Tetracenomycin X is a tetracenomycin antibiotic, a methyl ester and a tertiary alpha-hydroxy ketone. http://purl.obolibrary.org/obo/ARO_3007037 tetracenomycin A2 http://purl.obolibrary.org/obo/ARO_3007034 tetracenomycin antibiotic Tetracenomycin A2 is a tetracenomycin antibiotic, a methyl ester and a tertiary alpha-hydroxy ketone. http://purl.obolibrary.org/obo/ARO_3007039 chlorhexidine http://purl.obolibrary.org/obo/ARO_3005386 disinfecting agents and antiseptics Chlorhexidine is a disinfectant and antiseptic that is used for skin disinfection, including mouthwashes (chlorhexidine gluconate). http://purl.obolibrary.org/obo/ARO_3007040 cefotaxime-ceftiofur-tazobactam-clavulanate http://purl.obolibrary.org/obo/ARO_3000707 antibiotic mixture A combination therapy for multidrug resistant pathogens consisting of two cephalosporin antibiotics (cefotaxime and ceftiofur) with two beta-lactamase inhibitors (tazobactam and clavulanate) encapsulated in a nanoparticle. They were shown to have efficient antimicrobial activity against multidrug resistant extended-spectrum beta-lactamase producing Enterobacteriaceae. http://purl.obolibrary.org/obo/ARO_3007041 Erm(52) http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase Erm(52) is an Erm ribosomal RNA methyltransferase. http://purl.obolibrary.org/obo/ARO_3007042 msr(G) http://purl.obolibrary.org/obo/ARO_3004471 msr-type ABC-F protein msr(G) is a part of the msr subfamily of ABC-F ribosomal protection proteins. http://purl.obolibrary.org/obo/ARO_3007043 msr(I) http://purl.obolibrary.org/obo/ARO_3004471 msr-type ABC-F protein msr(I) is part of the msr subfamily of ABC-F ribosomal protection proteins. http://purl.obolibrary.org/obo/ARO_3007044 mef(F) http://purl.obolibrary.org/obo/ARO_3000747 mef mef(F) is an mef efflux pump protein. http://purl.obolibrary.org/obo/ARO_3007045 enrofloxacin http://purl.obolibrary.org/obo/ARO_0000001 fluoroquinolone antibiotic Enrofloxacin is a broad-spectrum fluoroquinolone antibiotic. It is used in veterinary medicine predominately for dogs and cats but is sometimes used for other animals. http://purl.obolibrary.org/obo/ARO_3007046 marbofloxacin http://purl.obolibrary.org/obo/ARO_0000001 fluoroquinolone antibiotic Marbofloxacin is a broad-spectrum fluoroquinolone antibiotic. It is used in veterinary medicine predominately for dogs and cats. http://purl.obolibrary.org/obo/ARO_3007047 mef(H) http://purl.obolibrary.org/obo/ARO_3000747 mef mef(H) is an mef efflux pump protein. http://purl.obolibrary.org/obo/ARO_3007048 Xeruborbactam http://purl.obolibrary.org/obo/ARO_3007131 boronic acid beta-lactamase inhibitor Xeruborbactam is an experimental cyclic boronate ultrabroad-spectrum beta-lactamase inhibitor, with potent activity against both serine beta-lactamases and metallo-beta-lactamases. http://purl.obolibrary.org/obo/ARO_3007049 mef(J) http://purl.obolibrary.org/obo/ARO_3000747 mef mef(J) is an mef efflux pump protein. http://purl.obolibrary.org/obo/ARO_3007050 mreA http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump mreA is a macrolide efflux pump. http://purl.obolibrary.org/obo/ARO_3007051 Helicobacter pylori rpoB mutation conferring resistance to rifampicin http://purl.obolibrary.org/obo/ARO_3000210 rifamycin-resistant beta-subunit of RNA polymerase (rpoB) Rifampicin inhibits transcription by binding the beta subunit of RNA polymerase. Helicobacter pylori mutations associated with rifampicin resistance typically occur in the rifampicin resistance determining region of rpoB between codons 525 and 586. http://purl.obolibrary.org/obo/ARO_3007052 Helicobacter pylori gyrA conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3003292 fluoroquinolone resistant gyrA Point mutations in the quinolone resistance-determining regions of Helicobacter pylori observed to confer resistance to fluoroquinolone antibiotics. http://purl.obolibrary.org/obo/ARO_3007053 Helicobacter pylori gyrB conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3000864 fluoroquinolone resistant gyrB Point mutations in Helicobacter pylori conferring resistance to fluoroquinolone antibiotics. http://purl.obolibrary.org/obo/ARO_3007055 Helicobacter pylori rdxA mutation conferring resistance to metronidazole http://purl.obolibrary.org/obo/ARO_3007056 Antibiotic resistant Helicobacter pylori nitroreductase The rdxA gene in Helicobacter pylori encodes an NADPH nitroreductase. Mutations in this gene are associated with metronidazole resistance. http://purl.obolibrary.org/obo/ARO_3007056 Antibiotic resistant Helicobacter pylori nitroreductase http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Inactivation of the oxygen-insensitive NADPH nitroreductases in Helicobacter pylori play a role in metronidazole resistance. http://purl.obolibrary.org/obo/ARO_3007057 Helicobacter pylori pbp3 conferring resistance to amoxicillin http://purl.obolibrary.org/obo/ARO_3003938 Penicillin-binding protein mutations conferring resistance to beta-lactam antibiotics Point mutations in Helicobacter pylori pbp3 observed to confer resistance to amoxicillin. http://purl.obolibrary.org/obo/ARO_3007058 Helicobacter pylori pbp2 mutants conferring resistance to amoxicillin http://purl.obolibrary.org/obo/ARO_3003938 Penicillin-binding protein mutations conferring resistance to beta-lactam antibiotics Point mutations in Helicobacter pylori pbp2 observed to confer resistance to amoxicillin. http://purl.obolibrary.org/obo/ARO_3007059 Helicobacter pylori frxA mutation conferring resistance to metronidazole http://purl.obolibrary.org/obo/ARO_3007056 Antibiotic resistant Helicobacter pylori nitroreductase FrxA encodes an NADH-flavin oxidoreductase in Helicobacter pylori. Mutations in this gene confer resistance to nitrofuran antibiotics and metronidazole. http://purl.obolibrary.org/obo/ARO_3007060 Helicobacter pylori pbp1 mutants conferring resistance to amoxicillin http://purl.obolibrary.org/obo/ARO_3003938 Penicillin-binding protein mutations conferring resistance to beta-lactam antibiotics Point mutations in Helicobacter pylori pbp1 observed to confer resistance to amoxicillin. http://purl.obolibrary.org/obo/ARO_3007061 hp1165 http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump Hp1165 is a homolog of the Clostridium perfringes tetP gene and is part of the MFS efflux family but is not considered a true tetracycline resistance gene. Hp1165 confers low level resistance to tetracycline, however cessation of antibiotic treatment results in the host cell reverting to susceptibility. http://purl.obolibrary.org/obo/ARO_3007062 VAM-1 http://purl.obolibrary.org/obo/ARO_3007065 VAM beta-lactamase VAM-1 is a subclass B1 metallo-beta-lactamase, conferring resistance to beta-lactam antibiotics such as carbapenems and cephalosporins. http://purl.obolibrary.org/obo/ARO_3007063 cilastatin http://purl.obolibrary.org/obo/ARO_3007226 host-related antibiotic adjuvants Cilastatin is often prescribed with imipenem as a beta-lactam potentiator. Cilastatin inhibits enzymatic renal dehydropeptidase, which hydrolyzes imipenem, thereby preventing the metabolism of imipenem in vivo and maintaining longer antibiotic exposure and effect. http://purl.obolibrary.org/obo/ARO_3007065 VAM beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase VAM beta-lactamases are class B1 beta-lactamases found in Vibrio alginolyticus. http://purl.obolibrary.org/obo/ARO_3007066 mg/L http://purl.obolibrary.org/obo/ARO_3004372 MIC unit Milligrams per Litre (mg/L). http://purl.obolibrary.org/obo/ARO_3007067 mm http://purl.obolibrary.org/obo/ARO_3004372 MIC unit Millimeters (mm). http://purl.obolibrary.org/obo/ARO_3007068 Miscellaneous ABC-F subfamily ATP-binding cassette ribosomal protection proteins http://purl.obolibrary.org/obo/ARO_3004469 ABC-F ATP-binding cassette ribosomal protection protein ABC-F subfamily ATP-binding cassette ribosomal protection proteins of unknown, unclear or miscellaneous classification which nevertheless confer resistance to antibiotics through ribosomal protection and not through antibiotic efflux. These proteins should be further reviewed to elucidate associated genes, their function, origin and classification. http://purl.obolibrary.org/obo/ARO_3007069 FosY http://purl.obolibrary.org/obo/ARO_3000133 fosfomycin thiol transferase A thiol transferase isolated in Staphylococcus aureus that leads to resistance of fosfomycin. http://purl.obolibrary.org/obo/ARO_3007070 MCR-1.33 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-1-type colistin resistance gene variant, first described in a multi-drug-resistant Escherichia coli isolate recovered from a urinary tract infection, and co-occurring with the carbapenemase NDM-5. http://purl.obolibrary.org/obo/ARO_3007072 ceftazidime-avibactam http://purl.obolibrary.org/obo/ARO_3000707 antibiotic mixture An antibiotic-adjuvant admixture of the beta-lactam antibiotic ceftazidime and the non-beta-lactam beta-lactamase inhibitor avibactam. http://purl.obolibrary.org/obo/ARO_3007073 Bacillus subtilis rpoB mutants conferring resistance to rifampin http://purl.obolibrary.org/obo/ARO_3000210 rifamycin-resistant beta-subunit of RNA polymerase (rpoB) Point mutations that occur within the Bacillus subtilis rpoB gene resulting in resistance to rifampin. http://purl.obolibrary.org/obo/ARO_3007074 capreomycin phosphotransferase http://purl.obolibrary.org/obo/ARO_3000557 antibiotic inactivation enzyme Capreomycin family of phosphotransferases confer resistance to capreomycin antibiotics. http://purl.obolibrary.org/obo/ARO_3007075 cph http://purl.obolibrary.org/obo/ARO_3007074 capreomycin phosphotransferase cph is a phosphotransferase that confers resistance to capreomycin. http://purl.obolibrary.org/obo/ARO_3007076 emerione A http://purl.obolibrary.org/obo/ARO_3007136 unclassified metallo-beta-lactamase inhibitor A fungal secondary metabolite which inhibits the action of New Delhi metallo-beta-lactamase 1. http://purl.obolibrary.org/obo/ARO_3007077 inhibitors of MsrA efflux pump http://purl.obolibrary.org/obo/ARO_3003932 antibiotic efflux inhibitor Molecules and compounds that decrease resistance by inhibiting the action of the MrsA efflux pump. http://purl.obolibrary.org/obo/ARO_3007078 Luteolin http://purl.obolibrary.org/obo/ARO_3007077 inhibitors of MsrA efflux pump Luteolin is a flavonoid produced by a variety of plants that features a wide range of biological effects. It has been shown to inhibit the action of the MsrA drug efflux pump. http://purl.obolibrary.org/obo/ARO_3007079 Pellitorine http://purl.obolibrary.org/obo/ARO_3007077 inhibitors of MsrA efflux pump Pellitorine is a metabolite produced mainly in members of the Zanthoxylum, Tetradium, and Piper genera. It has been shown to inhibit the action of the MsrA drug efflux pump. http://purl.obolibrary.org/obo/ARO_3007080 Piperic acid http://purl.obolibrary.org/obo/ARO_3007077 inhibitors of MsrA efflux pump Piperic acid is a compound produced by members of the Piper genus. It has been shown to inhibit the action of the MsrA drug efflux pump. http://purl.obolibrary.org/obo/ARO_3007081 Tetrahydropiperine http://purl.obolibrary.org/obo/ARO_3007077 inhibitors of MsrA efflux pump Tetraydropiperine is a derivative of piperine produced by members of the Piper genus. It has been shown to inhibit the action of the MsrA drug efflux pump. http://purl.obolibrary.org/obo/ARO_3007082 Sesamin http://purl.obolibrary.org/obo/ARO_3007077 inhibitors of MsrA efflux pump Sesamin is a compound isolated from sesame oil and bark from plants in the Zanthoxylum genus. It has been shown to inhibit the action of the MsrA drug efflux pump. http://purl.obolibrary.org/obo/ARO_3007083 biapenem http://purl.obolibrary.org/obo/ARO_0000020 carbapenem Biapenem is a broad spectrum injectable antibiotic belonging to the carbapenem subgroup of beta-lactams. http://purl.obolibrary.org/obo/ARO_3007084 PRC beta-lactamase http://purl.obolibrary.org/obo/ARO_3000076 class C beta-lactamase PRC beta-lactamases are class C beta-lactamases. http://purl.obolibrary.org/obo/ARO_3007085 PRC-1 http://purl.obolibrary.org/obo/ARO_3007084 PRC beta-lactamase PRC-1 is a beta-lactamase that confers resistance to certain cephalosporins and penicillins. http://purl.obolibrary.org/obo/ARO_3007086 epinecidin-1 http://purl.obolibrary.org/obo/ARO_3000053 peptide antibiotic Epinecidin-1 is a peptide antibiotic derived from Epinephelus coioides with broad spectrum activity against a range or Gram positive and Gram negative bacteria. http://purl.obolibrary.org/obo/ARO_3007087 KPC-90 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-90 is a KPC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007088 murepavadin http://purl.obolibrary.org/obo/ARO_3007162 protegrin-1-like antibiotic A peptidomimetic antibiotic with specific, potent action against members of the Pseudomonas genus. Murepavadin disrupts lipopolysaccharide biosynthesis by binding to lypopolysaccharide transport protein D. http://purl.obolibrary.org/obo/ARO_3007089 KPC-83 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-83 is a KPC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007090 albendazole http://purl.obolibrary.org/obo/ARO_3007163 albendazole-like antibiotic Albendazole is a compound used in the treatment of parasitic worm infestations. It has been shown to exhibit antibiotic activity against Escherichia coli by inhibiting MurA (MurZ), thereby disrupting cell wall synthesis. http://purl.obolibrary.org/obo/ARO_3007091 diflunisal http://purl.obolibrary.org/obo/ARO_3007159 salicylic acid antibiotic Diflunisal is a salicylic acid derivative and aspirin analogue typically used as a nonsteroidal anti-inflammatory drug. It has been shown to exhibit antibiotic activity against Escherichia coli by inhibiting MurA (MurZ), thereby disrupting cell wall synthesis. http://purl.obolibrary.org/obo/ARO_3007092 gepotidacin http://purl.obolibrary.org/obo/ARO_3007164 triazaacenaphthylene antibiotic Gepotidacin is a triazaacenaphthylene bacterial type II topoisomerase inhibitor used experimentally. It has been in phase III of clinical trials since 2019 for the treatment of gonorrhea, however gepotidacin has demonstrated antibiotic activity against a variety of bacteria. http://purl.obolibrary.org/obo/ARO_3007093 klebsidin http://purl.obolibrary.org/obo/ARO_3000053 peptide antibiotic Klebsidin is a peptide antibiotic derived from Klebsiella pneumoniae that exhibits activity against members of the Enterobacteriaceae family of Gram-negative bacteria, including Escherichia and Salmonella species. Klebsidin acts by accumulating in the target cell and inhibiting RNA polymerase. http://purl.obolibrary.org/obo/ARO_3007094 fisetin http://purl.obolibrary.org/obo/ARO_3007136 unclassified metallo-beta-lactamase inhibitor Fisetin is a flavonoid produced mainly by plants in the Eudicotidae clade. It exhibits a range of biological activities such as anti-inflammatory and antioxidant properties, and fisetin has been shown to inhibit the action of metallo-beta-lactamases. http://purl.obolibrary.org/obo/ARO_3007095 risedronate http://purl.obolibrary.org/obo/ARO_3007134 phosphonate metallo-beta-lactamase inhibitor Risedronate is a bisphosphonate used as an oral medication to treat osteoperosis and Paget's disease of bone. It has been shown to inhibit the action of New Delhi metallo-beta-lactamase-1. http://purl.obolibrary.org/obo/ARO_3007096 methotrexate http://purl.obolibrary.org/obo/ARO_3007136 unclassified metallo-beta-lactamase inhibitor Methotrexate is an antifolate chemotherapeutic and immune suppressant used to treat a wide variety of cancers and autoimmune diseases. It has been shown to inhibit the action of New Delhi metallo-beta-lactamase-1. http://purl.obolibrary.org/obo/ARO_3007097 FosM1 http://purl.obolibrary.org/obo/ARO_3000133 fosfomycin thiol transferase FosM1 is a thiol transferase discovered in human gut microflora that leads to the resistance of fosfomycin. http://purl.obolibrary.org/obo/ARO_3007098 FosM2 http://purl.obolibrary.org/obo/ARO_3000133 fosfomycin thiol transferase FosM2 is a thiol transferase discovered in human gut microflora that leads to the resistance of fosfomycin. http://purl.obolibrary.org/obo/ARO_3007099 FosM3 http://purl.obolibrary.org/obo/ARO_3000133 fosfomycin thiol transferase FosM3 is a thiol transferase discovered in human gut microflora that leads to the resistance of fosfomycin. http://purl.obolibrary.org/obo/ARO_3007100 class A Bacillus cereus Bc beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase Class A Bacillus cereus Bc beta-lactamases are enzymes that break down beta-lactam antibiotics, particularly penicillins. http://purl.obolibrary.org/obo/ARO_3007101 BcIII http://purl.obolibrary.org/obo/ARO_3007100 class A Bacillus cereus Bc beta-lactamase Bacillus cereus beta-lactamase III is a class A beta-lactamase that breaks down a number of penicillins and cephalosporins in Bacillus cereus. http://purl.obolibrary.org/obo/ARO_3007102 KPC-93 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-93 is a KPC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007103 nitroimidazole reductase http://purl.obolibrary.org/obo/ARO_3000557 antibiotic inactivation enzyme Nitroimidazole reductases are a group of enzymes that deactivate nitroimidazole antibiotics by reducing their nitro functional group to an amino group. These enzymes are associated with resistance to nitroimidazole derivatives in Bacteroides fragilis but have also been reported in a variety of anaerobic Gram-negative and Gram-positive genera. The minimum inhibitory concentrations for these enzymes vary greatly depending on species, strain, and precise nitroimidazole treatment used. http://purl.obolibrary.org/obo/ARO_3007104 nimA http://purl.obolibrary.org/obo/ARO_3007103 nitroimidazole reductase nimA is a nitroimidazole reductase mainly found in Bacteroides fragilis that is associated with the deactivation of nitroimidazole antibiotics such as metronidazole. Minimum inhibitory concentrations observed in isolates vary greatly depending on species, strain, and nitroimidazole treatment. http://purl.obolibrary.org/obo/ARO_3007105 nimC http://purl.obolibrary.org/obo/ARO_3007103 nitroimidazole reductase nimC is a nitroimidazole reductase mainly found in Bacteroides fragilis that is associated with the deactivation of nitroimidazole antibiotics such as metronidazole. Minimum inhibitory concentrations observed in isolates vary greatly depending on species, strain, and nitroimidazole treatment. http://purl.obolibrary.org/obo/ARO_3007106 nimD http://purl.obolibrary.org/obo/ARO_3007103 nitroimidazole reductase nimD is a nitroimidazole reductase mainly found in Bacteroides fragilis that is associated with the deactivation of nitroimidazole antibiotics such as metronidazole. Minimum inhibitory concentrations observed in isolates vary greatly depending on species, strain, and nitroimidazole treatment. http://purl.obolibrary.org/obo/ARO_3007107 nimE http://purl.obolibrary.org/obo/ARO_3007103 nitroimidazole reductase nimE is a nitroimidazole reductase mainly found in Bacteroides fragilis that is associated with the deactivation of nitroimidazole antibiotics such as metronidazole. Minimum inhibitory concentrations observed in isolates vary greatly depending on species, strain, and nitroimidazole treatment. http://purl.obolibrary.org/obo/ARO_3007108 nimF http://purl.obolibrary.org/obo/ARO_3007103 nitroimidazole reductase nimF is a nitroimidazole reductase that shares significant identity with other nim genes which are associated with the deactivation of nitroimidazole antibiotics. http://purl.obolibrary.org/obo/ARO_3007109 nimG http://purl.obolibrary.org/obo/ARO_3007103 nitroimidazole reductase nimG is a nitroimidazole reductase that shares significant identity with other nim genes which are associated with the deactivation of nitroimidazole antibiotics. http://purl.obolibrary.org/obo/ARO_3007110 nimH http://purl.obolibrary.org/obo/ARO_3007103 nitroimidazole reductase nimH is a nitroimidazole reductase mainly found in Bacteroides fragilis that is associated with the deactivation of nitroimidazole antibiotics such as metronidazole. Minimum inhibitory concentrations observed in isolates vary greatly depending on species, strain, and nitroimidazole treatment. http://purl.obolibrary.org/obo/ARO_3007111 nimI http://purl.obolibrary.org/obo/ARO_3007103 nitroimidazole reductase nimI is a nitroimidazole reductase discovered in the Prevotella baroniae that is associated with the deactivation of nitroimidazole antibiotics such as metronidazole. Although not found in Bacteroids fragilis, the source organism of most nim genes, nimI shares significant similarity with other nitroimidazole reductases. nimI is chromosomally encoded in P. baroniae, suggesting that it is intrinsic to this species. http://purl.obolibrary.org/obo/ARO_3007112 nimJ http://purl.obolibrary.org/obo/ARO_3007103 nitroimidazole reductase nimJ is a nitroimidazole reductase mainly found in Bacteroides fragilis that is associated with the deactivation of nitroimidazole antibiotics such as metronidazole. Minimum inhibitory concentrations observed in isolates vary greatly depending on species, strain, and nitroimidazole treatment. http://purl.obolibrary.org/obo/ARO_3007113 nimK http://purl.obolibrary.org/obo/ARO_3007103 nitroimidazole reductase nimK is a nitroimidazole reductase mainly found in Bacteroides fragilis that is associated with the deactivation of nitroimidazole antibiotics such as metronidazole. Minimum inhibitory concentrations observed in isolates vary greatly depending on species, strain, and nitroimidazole treatment. http://purl.obolibrary.org/obo/ARO_3007114 ornidazole http://purl.obolibrary.org/obo/ARO_3004115 nitroimidazole antibiotic Ornidazole is a synthetic nitroimidazole derivative mainly used to treat parasitic infections but has also demonstrated antibiotic activity against anaerobic bacteria. http://purl.obolibrary.org/obo/ARO_3007115 modification to cell morphology http://purl.obolibrary.org/obo/ARO_1000002 mechanism of antibiotic resistance Antibiotic-induced changes to cell morphology, including shape, volume and surface area, which decrease antibiotic susceptibility. http://purl.obolibrary.org/obo/ARO_3007116 Reduction in surface-to-volume ratio of cell http://purl.obolibrary.org/obo/ARO_3007115 modification to cell morphology Changes to cell morphology by activated growth response in the presence of an antibiotic, leading to a decreased surface-to-volume ratio. Such changes decrease antibiotic influx and increase antibiotic dilution in the cell, thereby increasing survivability, particularly in nutrient-poor environments. http://purl.obolibrary.org/obo/ARO_3007117 subclass B1 Bacteroides xylanisolvens crx beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase Subclass B1 Bacteroides xylanisolvens crx beta-lactamases are zinc metallo-beta-lactamases that hydrolyze carbapenems. http://purl.obolibrary.org/obo/ARO_3007118 crxA http://purl.obolibrary.org/obo/ARO_3007117 subclass B1 Bacteroides xylanisolvens crx beta-lactamase crxA is a subclass B1 metallo-betal-lactamase from Bacteroides xylanisolvens that hydrolyzes carbapenems such as imipenem and meropenem. http://purl.obolibrary.org/obo/ARO_3007119 tet(O/32/O) http://purl.obolibrary.org/obo/ARO_0000002 tetracycline-resistant ribosomal protection protein Tet(O/32/O) is a mosaic tetracycline resistance gene and ribosomal protection protein. http://purl.obolibrary.org/obo/ARO_3007120 tet(O/M/O) http://purl.obolibrary.org/obo/ARO_0000002 tetracycline-resistant ribosomal protection protein Tet(O/M/O) is a mosaic tetracycline resistance gene and ribosomal protection protein. http://purl.obolibrary.org/obo/ARO_3007121 tet(O/W) http://purl.obolibrary.org/obo/ARO_0000002 tetracycline-resistant ribosomal protection protein Tet(O/W) is a mosaic tetracycline resistance gene and ribosomal protection protein. http://purl.obolibrary.org/obo/ARO_3007122 tet(O/W/32/O) http://purl.obolibrary.org/obo/ARO_0000002 tetracycline-resistant ribosomal protection protein Tet(O/W/32/O) is a mosaic tetracycline resistance gene and ribosomal protection protein. http://purl.obolibrary.org/obo/ARO_3007123 tet(O/W/O) http://purl.obolibrary.org/obo/ARO_0000002 tetracycline-resistant ribosomal protection protein Tet(O/W/O) is a mosaic tetracycline resistance gene and ribosomal protection protein. http://purl.obolibrary.org/obo/ARO_3007124 tet(W/32/O) http://purl.obolibrary.org/obo/ARO_0000002 tetracycline-resistant ribosomal protection protein Tet(W/32/O) is a mosaic tetracycline resistance gene and ribosomal protection protein. http://purl.obolibrary.org/obo/ARO_3007125 ROB-11 http://purl.obolibrary.org/obo/ARO_3002994 ROB beta-lactamase ROB-11 is a class A beta-lactamase from the blaROB AMR gene family. http://purl.obolibrary.org/obo/ARO_3007126 ROB-12 http://purl.obolibrary.org/obo/ARO_3002994 ROB beta-lactamase ROB-12 is a class A beta-lactamase from the blaROB AMR gene family. http://purl.obolibrary.org/obo/ARO_3007127 Streptomyces lividans otr(A) http://purl.obolibrary.org/obo/ARO_0000002 tetracycline-resistant ribosomal protection protein Streptomyces lividans otr(A) is an oxytetracycline resistance ribosomal protection protein found in Streptomyces lividans. http://purl.obolibrary.org/obo/UBERON_0001003 skin epidermis http://purl.obolibrary.org/obo/ARO_3004430 antimicrobial resistance tissue specificity The outer epithelial layer of the skin that is superficial to the dermis. http://purl.obolibrary.org/obo/ARO_2000001 confers_resistance_to_drug_class A relationship ontology term in which the subject (e.g., a gene family) confers or contributes to antibiotic resistance to some or all of the object (e.g. a drug class). It is a qualitative measure of antibiotic resistance, based on an experiment illustrating elevated MIC even outside of a clinical setting. A family of AMR genes confers resistance to a class of antibiotics if and only if all instances of that family confer resistance to some instances of that class in an organism. http://purl.obolibrary.org/obo/ARO_2000002 inner_membrane_protein_of A component of tripartite efflux systems that resides in the inner membrane of Gram-negative bacteria that actively transports substrates out of the cell. http://purl.obolibrary.org/obo/ARO_3009147 MexGHI http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MexGHI is a multidrug efflux pump complex consisting of MexG, MexH, and MexI as its key components. Together, they form a central transport system that interfaces with outer membrane proteins to remove antibiotics and toxic substances, playing a role in multidrug resistance. http://purl.obolibrary.org/obo/DOID_0050161 lower respiratory tract disease http://purl.obolibrary.org/obo/DOID_1579 respiratory system disease A respiratory system disease which involves the lower respiratory tract. http://purl.obolibrary.org/obo/DOID_11162 respiratory failure http://purl.obolibrary.org/obo/DOID_850 lung disease A lung disease characterized by inadequate gas exchange by the respiratory system. http://purl.obolibrary.org/obo/DOID_11394 adult respiratory distress sydrome http://purl.obolibrary.org/obo/DOID_11162 respiratory failure A respiratory failure that results from diffuse injury to the endothelium of the lung (as in sepsis, chest trauma, massive blood transfusion, aspiration of the gastric contents, or pneumonia) and is characterized by pulmonary edema with an abnormally high amount of protein in the edematous fluid and by difficult rapid breathing and hypoxemia. http://purl.obolibrary.org/obo/DOID_12716 newborn respiratory distress syndrome http://purl.obolibrary.org/obo/DOID_11162 respiratory failure A respiratory failure that is characterized by deficiency of the surfactant coating the inner surface of the lungs, by failure of the lungs to expand and contract properly during breathing with resulting collapse, and by the accumulation of a protein-containing film lining the alveoli and their ducts. http://purl.obolibrary.org/obo/DOID_13148 acute cystitis http://purl.obolibrary.org/obo/ARO_3004430 antimicrobial resistance tissue specificity A cystitis characterized by a sudden onset or severe symptoms. http://purl.obolibrary.org/obo/DOID_1579 respiratory system disease http://purl.obolibrary.org/obo/ARO_3004430 antimicrobial resistance tissue specificity A disease of anatomical entity that located_in the respiratory system which extends from the nasal sinuses to the diaphragm. http://purl.obolibrary.org/obo/DOID_37 skin disease http://purl.obolibrary.org/obo/ARO_3004430 antimicrobial resistance tissue specificity An integumentary system disease that is located in the skin. http://purl.obolibrary.org/obo/DOID_850 lung disease http://purl.obolibrary.org/obo/DOID_0050161 lower respiratory tract disease A lower respiratory tract disease in which the function of the lungs is adversely affected by narrowing or blockage of the airways resulting in poor air flow, a loss of elasticity in the lungs that produces a decrease in the total volume of air that the lungs are able to hold, and clotting, scarring, or inflammation of the blood vessels that affect the ability of the lungs to take up oxygen and to release carbon dioxide. http://purl.obolibrary.org/obo/UBERON_0003134 female reproductive organ http://purl.obolibrary.org/obo/ARO_3004430 antimicrobial resistance tissue specificity A female organ involved in reproduction. http://purl.obolibrary.org/obo/UBERON_0003135 male reproductive organ http://purl.obolibrary.org/obo/ARO_3004430 antimicrobial resistance tissue specificity A male organ involved in reproduction. http://purl.obolibrary.org/obo/ARO_3000045 component of AMR genotypic or phenotypic terminology http://purl.obolibrary.org/obo/ARO_1000001 process or component of antibiotic biology or chemistry A collection of curated phenotypic terms relating to antibiotic resistance and the Comprehensive Antibiotic Resistance Database. http://purl.obolibrary.org/obo/ARO_3004266 antibiotic resistant katG http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Point mutations in katG confer antibiotic resistance by preventing katG from catalyzing the activation of antibiotics. http://purl.obolibrary.org/obo/ARO_3004267 antibiotic resistant pncA http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Point mutations in pncA prevent the enzyme from activating antibiotics, such as pyrazinamide. http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase http://purl.obolibrary.org/obo/ARO_3004112 phosphoethanolamine transferase conferring colistin resistance A group of mobile colistin resistance genes encode the MCR family of phosphoethanolamine transferases, which catalyze the addition of phosphoethanolamine onto lipid A, thus interfering with the binding of colistin to the cell membrane. http://purl.obolibrary.org/obo/ARO_3004269 pmr phosphoethanolamine transferase http://purl.obolibrary.org/obo/ARO_3004112 phosphoethanolamine transferase conferring colistin resistance This family of phosphoethanolamine transferase catalyze the addition of 4-amino-4-deoxy-L-arabinose (L-Ara4N) and phosphoethanolamine to lipid A, which impedes the binding of colistin to the cell membrane. http://purl.obolibrary.org/obo/ARO_3004270 antibiotic resistant fabI http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant fabI is a enoyl-acyl carrier reductase used in lipid metabolism and fatty acid biosynthesis. The bacterial biocide Triclosan blocks the final reduction step in fatty acid elongation, inhibiting biosynthesis. Point mutations in fabI can confer resistance to Triclosan and Isoniazid. http://purl.obolibrary.org/obo/ARO_3004271 16S rRNA methyltransferase (G1405) http://purl.obolibrary.org/obo/ARO_3000857 16S ribosomal RNA methyltransferase Methyltransferases that methylate the G1405 position of 16S rRNA, which is part of an aminoglycoside binding site. http://purl.obolibrary.org/obo/ARO_3004272 16S rRNA methyltransferase (A1408) http://purl.obolibrary.org/obo/ARO_3000857 16S ribosomal RNA methyltransferase Methyltransferases that methylate the A1408 position of 16S rRNA, which is part of an aminoglycoside binding site. http://purl.obolibrary.org/obo/ARO_3004273 Llm 23S ribosomal RNA methyltransferase http://purl.obolibrary.org/obo/ARO_3004274 23S ribosomal RNA methyltransferase A family of lincosamide resistant 23S rRNA methyltransferases. The only member of the family discovered so far was isolated from Paenibacillus sp. LC231, a strain found in Lechuguilla Cave, NM, USA. http://purl.obolibrary.org/obo/ARO_3004274 23S ribosomal RNA methyltransferase http://purl.obolibrary.org/obo/ARO_3000164 rRNA methyltransferase conferring antibiotic resistance Methyltransferases that modify the 23S rRNA of the 50S subunit of bacterial ribosomes, conferring resistance to drugs that target 23S rRNA. http://purl.obolibrary.org/obo/ARO_3004275 ANT(3'') http://purl.obolibrary.org/obo/ARO_3000218 aminoglycoside nucleotidyltransferase (ANT) A category of aminoglycoside O-nucleotidyltransferase enzymes with modification regiospecificity based at the 3''-hydroxyl group of the respective antibiotic. These enzymes inactivate aminoglycoside antibiotics by transfer of an AMP group from an ATP substrate to the 3''-hydroxyl group of the compound. http://purl.obolibrary.org/obo/ARO_3004276 ANT(2'') http://purl.obolibrary.org/obo/ARO_3000218 aminoglycoside nucleotidyltransferase (ANT) A category of aminoglycoside O-nucleotidyltransferase enzymes with modification regiospecificity based at the 2''-hydroxyl group of the respective antibiotic. These enzymes inactivate aminoglycoside antibiotics by transfer of an AMP group from an ATP substrate to the 2''-hydroxyl group of the compound. http://purl.obolibrary.org/obo/ARO_3004277 General Bacterial Porin (GBP) http://purl.obolibrary.org/obo/ARO_3000270 protein modulating permeability to antibiotic General bacterial porins are a family of porins found in the outer membrane of Gram-negative bacteria. They catalyze the energy-independent transport of small molecules across the outer membranes of bacteria. Most of the porins of these family are homotrimeric and have variable selectivity, ranging from being cation-selective, anion-selective or selective for different compounds. The most well characterized members of this family are the OmpF and OmpC porins of Escherichia coli. This family is also known as the classical porins. http://purl.obolibrary.org/obo/ARO_3004278 Outer Membrane Porin (Opr) http://purl.obolibrary.org/obo/ARO_3000270 protein modulating permeability to antibiotic The Opr family consists of porins in Pseudomonas species, and other Gram-negative bacteria, that exhibit a variety of substrate selectivities. http://purl.obolibrary.org/obo/ARO_3004279 Sugar Porin (SP) http://purl.obolibrary.org/obo/ARO_3000270 protein modulating permeability to antibiotic Members of the Sugar Porin family tend to facilitate the transport of maltodextrins and other sugars across the outer membrane of Gram-negative bacteria. These porins form a homotrimeric structure. http://purl.obolibrary.org/obo/ARO_3004280 MipA-interacting Protein http://purl.obolibrary.org/obo/ARO_3000270 protein modulating permeability to antibiotic The MltA-interacting Protein (MipA) family consists mainly of homologs to MipA and OmpV proteins. Proteins of this family, are predicted to form a beta-barrel. http://purl.obolibrary.org/obo/ARO_3004281 General Bacterial Porin with reduced permeability to beta-lactams http://purl.obolibrary.org/obo/ARO_3004277 General Bacterial Porin (GBP) These are GBPs that are associated with decreased susceptibility to beta-lactams either through mutations in the porin protein, absence of the porin protein, or expression of the porin protein. http://purl.obolibrary.org/obo/ARO_3004282 General Bacterial Porin with reduced permeability to peptide antibiotics http://purl.obolibrary.org/obo/ARO_3004277 General Bacterial Porin (GBP) These are GBPs that are associated with decreased susceptibility to peptide antibiotics either through mutations in the porin protein, absence of the porin protein, or expression of the porin protein. http://purl.obolibrary.org/obo/ARO_3004283 CarO porin http://purl.obolibrary.org/obo/ARO_3000270 protein modulating permeability to antibiotic The imipenum resistance-associated CarO porin family is composed of the CarO porin originally identified in Acinetobacter baumannii. The loss of these porins is associated with imipenem and meropenem multi-drug resistance. The channels formed by CarO porins show slight cation selectivity. http://purl.obolibrary.org/obo/ARO_3004284 antibiotic resistant fabG http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant fabG is a 3-oxoacyl-acyl carrier protein reductase involved in lipid metabolism and fatty acid biosynthesis. The bacterial biocide Triclosan blocks the final reduction step in fatty acid elongation, inhibiting biosynthesis. Point mutations in fabG can confer resistance to Triclosan. http://purl.obolibrary.org/obo/ARO_3004285 tunicamycin resistance protein http://purl.obolibrary.org/obo/ARO_3000270 protein modulating permeability to antibiotic A grouping of tunicamycin resistance proteins that are homologous to tmrB found in Bacillus subtilis. http://purl.obolibrary.org/obo/ARO_3004286 phenotypic variant regulator http://purl.obolibrary.org/obo/ARO_3003768 gene conferring resistance via absence Phenotypic variant regulator proteins play a role in controlling the switch between antibiotic-susceptible and antibiotic-resistant forms of bacteria. The characterized member of this family is the PvrR protein in Pseudomonas aeruginosa, which when absent, confers antibiotic resistance. http://purl.obolibrary.org/obo/ARO_3004287 lipid A phosphatase http://purl.obolibrary.org/obo/ARO_3003580 gene altering cell wall charge The antimicrobial activity of certain antibiotics, such as peptide antibiotics, is proposed to be initiated through binding to the lipid A moiety of lipopolysaccharides. Thus, covalent modification of Gram-negative bacterial lipid A by phosphatases is a mechanism to reduce the susceptibility of the bacteria to antibiotics. http://purl.obolibrary.org/obo/ARO_3004288 Subclass B1 Vibrio cholerae varG beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase varG is an Ambler class B metallo-beta-lactamase found on the antibiotic resistance var regulon in Vibrio cholerae, along with an antibiotic efflux pump varABCDEF. These genes are organized as a regulon under the control of VarR transcriptional activator. VarG was shown to have beta-lactamase activity against penicillins, carbapenems and cephalosporins in-vitro. http://purl.obolibrary.org/obo/ARO_3004289 Vibrio cholerae varG http://purl.obolibrary.org/obo/ARO_3004288 Subclass B1 Vibrio cholerae varG beta-lactamase varG is an Ambler class B metallo-beta-lactamase found on the antibiotic resistance var regulon in Vibrio cholerae, along with an antibiotic efflux pump varABCDEF. These genes are organized as a regulon under the control of VarR transcriptional activator. VarG was shown to have beta-lactamase activity against penicillins, carbapenems and cephalosporins in-vitro. Described by Lin HV et al. 2017. http://purl.obolibrary.org/obo/ARO_3004290 Escherichia coli ampC beta-lactamase http://purl.obolibrary.org/obo/ARO_3004232 ampC-type beta-lactamase A class C ampC beta-lactamase (cephalosporinase) enzyme described in Escherichia coli shown clinically to confer resistance to penicillin-like and cephalosporin-class antibiotics. http://purl.obolibrary.org/obo/ARO_3004291 Rhodobacter sphaeroides ampC beta-lactamase http://purl.obolibrary.org/obo/ARO_3004232 ampC-type beta-lactamase A periplasmic cephalosporinase described in Rhodobacter sphaeroides shown to contribute to resistance of beta-lactam antibiotics. http://purl.obolibrary.org/obo/ARO_3004293 BUT beta-lactamase http://purl.obolibrary.org/obo/ARO_3000076 class C beta-lactamase A class C beta-lactamase family of chromosome-encoded antibiotic resistance genes originally described from Buttiauxella spp. http://purl.obolibrary.org/obo/ARO_3004294 BUT-1 http://purl.obolibrary.org/obo/ARO_3004293 BUT beta-lactamase A chromosome-encoded class C cephalosporinase and penicillinase from Buttiauxella spp. shown clinically to confer resistance to beta-lactam antibiotics. Described by Fihman et al. 2002. http://purl.obolibrary.org/obo/ARO_3004295 lassomycin http://purl.obolibrary.org/obo/ARO_3000157 rifamycin antibiotic A ribosomally synthesized cyclic peptide antibiotic. Lassomycin has been shown to be effective against drug-resistant mycobacteria but shows little activity against other bacteria. Lassomycin targets and binds to a region of the ClpC1 ATPase complex and uncouples ATPase from proteolytic activity, an essential function for mycobacterial viability, causing cell death. http://purl.obolibrary.org/obo/ARO_3004296 bulgecin A http://purl.obolibrary.org/obo/ARO_3004564 unclassified resistance-modifying agents Bulgecin A is a lytic transglycosylase inhibitor and antibiotic potentiator produced from Pseudomonas mesoacidophila. In the presence of some beta-lactam antibiotics, including ampicillin and meropenem, bulgecin A has been shown to restore susceptibility to carbapenems in carbapenem-resistant pathogens. http://purl.obolibrary.org/obo/ARO_3004299 antimicrobial phenotype http://purl.obolibrary.org/obo/ARO_3000045 component of AMR genotypic or phenotypic terminology Qualitative description of a microbial response to antimicrobial agents and the expected clinical outcome. Bacteria may be susceptible or resistant to a broad range of antibiotic drugs or drug classes, with several intermediate states or phases. http://purl.obolibrary.org/obo/ARO_3004300 intermediate antimicrobial phenotype http://purl.obolibrary.org/obo/ARO_3004440 CLSI antimicrobial phenotype Intermediate sensitivity of a bacterial strain to a given antibiotic occurs when it is inhibited by a concentration of the drug that is associated with uncertain therapeutic effect. The elimination of intermediate phenotype bacteria may depend on the site of infection and/or the concentration of the administered drug. Definition from https://clsi.org. http://purl.obolibrary.org/obo/ARO_3004301 resistant antimicrobial phenotype http://purl.obolibrary.org/obo/ARO_3004440 CLSI antimicrobial phenotype A bacterial strain is said to be resistant to a given antibiotic when it is inhibited in vitro by a concentration of this drug that is associated with a high likelihood of therapeutic failure. http://purl.obolibrary.org/obo/ARO_3004302 susceptible antimicrobial phenotype http://purl.obolibrary.org/obo/ARO_3004440 CLSI antimicrobial phenotype A bacterial strain is said to be susceptible to a given antibiotic when it is inhibited in vitro by a concentration of a drug that is associated with a high likelihood of therapeutic success. http://purl.obolibrary.org/obo/ARO_3004303 nonsusceptible antimicrobial phenotype http://purl.obolibrary.org/obo/ARO_3004440 CLSI antimicrobial phenotype A bacterial strain is said to be nonsusceptible to a given antibiotic drug if it demonstrates either an intermediate or resistant phenotype when exposed to a concentration of a drug that is associated with a high likelihood of therapeutic failure, i.e. if the bacterial strain is not susceptible to the antibiotic drug but not necessarily totally resistant under all conditions. Definition from https://clsi.org. http://purl.obolibrary.org/obo/ARO_3004304 susceptible dose dependent antimicrobial phenotype http://purl.obolibrary.org/obo/ARO_3004440 CLSI antimicrobial phenotype A bacterial strain is said to be susceptible-dose dependent (SDD) to a given antibiotic when growth is inhibited with a high likelihood of therapeutic success, but when multiple approved dosing options exist. When a higher or more frequent dose is used, the predicted therapeutic result is the same as for susceptible individuals. http://purl.obolibrary.org/obo/ARO_3004305 multidrug resistance antimicrobial phenotype http://purl.obolibrary.org/obo/ARO_3004299 antimicrobial phenotype Multidrug-resistant organisms are defined as bacterial strains that have become resistant to multiple classes of antibacterial drugs or other agents. The phenotype of these organisms is defined by the spectrum of antibiotic drug classes to which that organism is resistant. Often, these organisms are susceptible to a narrow range of available drugs, making treatment difficult and urgent. http://purl.obolibrary.org/obo/ARO_3004306 methicillin-resistant Staphylococcus aureus http://purl.obolibrary.org/obo/ARO_3004305 multidrug resistance antimicrobial phenotype Any strain of Staphylococcus aureus that has tested resistant (R) to at least one of methicillin, oxacillin or cefoxitin by standard susceptibility testing methods. http://purl.obolibrary.org/obo/ARO_3004307 Linezolid-resistant MRSA http://purl.obolibrary.org/obo/ARO_3004306 methicillin-resistant Staphylococcus aureus Methicillin-resistant Staphylococcus aureus that has additionally tested resistant to the antibiotic drug linezolid. http://purl.obolibrary.org/obo/ARO_3004308 Fluoroquinolone-resistant MRSA http://purl.obolibrary.org/obo/ARO_3004306 methicillin-resistant Staphylococcus aureus Methicillin-resistant Staphylococcus aureus that has additionally tested resistant to the fluoroquinolone antibiotics ciprofloxacin and/or levofloxacin. http://purl.obolibrary.org/obo/ARO_3004309 Vancomycin-intermediate MRSA http://purl.obolibrary.org/obo/ARO_3004306 methicillin-resistant Staphylococcus aureus Methicillin-resistant Staphylococcus aureus that has additionally tested intermediate to vancomycin antibiotics. http://purl.obolibrary.org/obo/ARO_3004310 Daptomycin-resistant MRSA http://purl.obolibrary.org/obo/ARO_3004306 methicillin-resistant Staphylococcus aureus Methicillin-resistant Staphylococcus aureus that has additionally tested non-susceptible (NS, resistant or intermediate) to daptomycin antibiotics. http://purl.obolibrary.org/obo/ARO_3004311 carbapenem-resistant Acinetobacter http://purl.obolibrary.org/obo/ARO_3004305 multidrug resistance antimicrobial phenotype Any strain of Acinetobacter spp. that has tested either Intermediate or Resistant to at least one of the following carbapenem-class antibiotics by standard testing using approved breakpoints: imipenem, meropenem, doripenem. http://purl.obolibrary.org/obo/ARO_3004312 multidrug-resistant Acinetobacter http://purl.obolibrary.org/obo/ARO_3004305 multidrug resistance antimicrobial phenotype Any strain of an Acinetobacter spp. that has either tested Intermediate or Resistant to at least one antibiotic drug in at least 3 of the 6 following categories: 1) Extended-spectrum cephalosporins, 2) Fluoroquinolone, 3) Aminoglycosides, 4) Carbapenems, 5) Piperacillin group, and 6) Ampicillin/sulbactam. http://purl.obolibrary.org/obo/ARO_3004313 carbapenem-resistant Escherichia coli http://purl.obolibrary.org/obo/ARO_3004305 multidrug resistance antimicrobial phenotype Any strain of E. coli that has tested resistant to one of the following carbapenem antibiotics: imipenem, meropenem, doripenem, ertapenem. http://purl.obolibrary.org/obo/ARO_3004314 extended-spectrum cephalosporin-resistant Escherichia coli http://purl.obolibrary.org/obo/ARO_3004305 multidrug resistance antimicrobial phenotype Any E.coli that has tested resistant (R) to at least one of the following: ceftriaxone, ceftazidime, cefepime, and cefotaxime. http://purl.obolibrary.org/obo/ARO_3004315 fluoroquinolone-resistant Escherichia coli http://purl.obolibrary.org/obo/ARO_3004305 multidrug resistance antimicrobial phenotype Any E.coli that has tested resistant (R) to at least one of the following: ciprofloxacin, levofloxacin, and moxifloxacin. http://purl.obolibrary.org/obo/ARO_3004316 multidrug-resistant Escherichia coli http://purl.obolibrary.org/obo/ARO_3004305 multidrug resistance antimicrobial phenotype Any E.coli that has tested either intermediate (I) or resistant (R) to at least one drug in at least 3 of the following 5 categories: 1) Extended-spectrum cephalosporins, 2) Fluoroquinolones (ciprofloxacin, levofloxacin, moxifloxacin), 3) Aminoglycosides (amikacin, gentamicin, tobramycin), 4) Carbapenems (imipenem, meropenem, doripenem, ertapenem), 5) Piperacillin Group (piperacillin, piperacillin/tazobactam). http://purl.obolibrary.org/obo/ARO_3004317 carbapenem-resistant Enterobacter http://purl.obolibrary.org/obo/ARO_3004305 multidrug resistance antimicrobial phenotype Any Enterobacter spp. that has tested resistant to at least one of the following antibiotic drugs: imipenem, meropenem, doripenem, ertapenem. http://purl.obolibrary.org/obo/ARO_3004318 extended-spectrum cephalosporin-resistant Enterobacter http://purl.obolibrary.org/obo/ARO_3004305 multidrug resistance antimicrobial phenotype Any Enterobacter spp. that has tested resistant to at least one of the following antibiotics: ceftriaxone, ceftazidime, cefepime, and/or cefotaxime. http://purl.obolibrary.org/obo/ARO_3004319 multidrug-resistant Enterobacter http://purl.obolibrary.org/obo/ARO_3004305 multidrug resistance antimicrobial phenotype Any Enterobacter spp. that has tested either Intermediate or Resistant to at least one drug in at least 3 of the following categories: extended-spectrum cephalosporins, fluoroquinolones, aminoglycosides, carbapenems, and/or pipericillin/tazobactam. http://purl.obolibrary.org/obo/ARO_3004320 carbapenem-resistant Klebsiella http://purl.obolibrary.org/obo/ARO_3004305 multidrug resistance antimicrobial phenotype Any Klebsiella oxytoca or Klebsiella pneumoniae that has tested resistant to at least one of the following antibiotics: imipenem, meropenem, doripenem, ertapenem. http://purl.obolibrary.org/obo/ARO_3004321 extended-spectrum cephalosporin-resistant Klebsiella http://purl.obolibrary.org/obo/ARO_3004305 multidrug resistance antimicrobial phenotype Any Klebsiella oxytoca or Klebsiella pneumoniae that has tested resistant to at least one of the following antibiotics: ceftriaxone, ceftazidime, cefepime, and/or cefotaxime. http://purl.obolibrary.org/obo/ARO_3004322 multidrug-resistant Klebsiella http://purl.obolibrary.org/obo/ARO_3004305 multidrug resistance antimicrobial phenotype Any Klebsiella oxytoca or Klebsiella pneumoniae that has tested Intermediate or Resistant in at least 3 of the following categories: extended-spectrum cephalosporins, fluoroquinolones, aminoglycosides, carbapenems, or pipericillin/tazobactam. http://purl.obolibrary.org/obo/ARO_3004323 carbapenem-resistant Pseudomonas aeruginosa http://purl.obolibrary.org/obo/ARO_3004305 multidrug resistance antimicrobial phenotype Any strain of Pseudomonas aeruginosa that has tested either Intermediate or Resistant to at least one of the following antibiotics: imipenem, meropenem and/or doripenem. http://purl.obolibrary.org/obo/ARO_3004324 extended-spectrum cephalosporin-resistant Pseudomonas aeruginosa http://purl.obolibrary.org/obo/ARO_3004305 multidrug resistance antimicrobial phenotype Any strain of Pseudomonas aeruginosa that has tested Resistant to at least one of the following antibiotics: cefepime and/or ceftazidime. http://purl.obolibrary.org/obo/ARO_3004325 MCR-4.1 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase MCR-4 is a plasmid-borne phosphoethanolamine transferase variant of MCR-1, isolated from Salmonella enterica serovar Typhimurium of porcine origin in Italy, Spain and Belgium through 2013 and 2015-2016. MCR-4 confers resistance to collistin via addition of a phosphoethanolamine group to lipid A, reducing the negative charge of the cell membrane. Described by Carattoli et al. 2017. http://purl.obolibrary.org/obo/ARO_3004326 fluoroquinolone-resistant Pseudomonas aeruginosa http://purl.obolibrary.org/obo/ARO_3004305 multidrug resistance antimicrobial phenotype Any Pseudomonas aeruginosa that has tested resistant (R) to at least one of the following: ciprofloxacin, levofloxacin. http://purl.obolibrary.org/obo/ARO_3004327 aminoglycoside-resistant Pseudomonas aeruginosa http://purl.obolibrary.org/obo/ARO_3004305 multidrug resistance antimicrobial phenotype Any Pseudomonas aeruginosa that has tested resistant (R) to at least one of the following: amikacin, gentamicin, tobramycin. http://purl.obolibrary.org/obo/ARO_3004328 pipericillin-resistant Pseudomonas aeruginosa http://purl.obolibrary.org/obo/ARO_3004305 multidrug resistance antimicrobial phenotype Any Pseudomonas aeruginosa that has tested resistant (R) to at least one of the following: piperacillin, piperacillin/tazobactam. http://purl.obolibrary.org/obo/ARO_3004329 vancomycin-resistant Enterococcus http://purl.obolibrary.org/obo/ARO_3004305 multidrug resistance antimicrobial phenotype Any Enterococcus faecium or Enterococcus faecalis that has tested resistant (R) to vancomycin. http://purl.obolibrary.org/obo/ARO_3004330 daptomycin-resistant Enterococcus http://purl.obolibrary.org/obo/ARO_3004305 multidrug resistance antimicrobial phenotype Any Enterococcus faecium or Enterococcus faecalis that has tested non-susceptible (NS) to daptomycin. http://purl.obolibrary.org/obo/ARO_3004331 vancomycin-resistant coagulase-negative Staphylococci http://purl.obolibrary.org/obo/ARO_3004305 multidrug resistance antimicrobial phenotype Coagulase-Negative Staphylococci that has tested resistant(R) or intermediate(I) to vancomycin. http://purl.obolibrary.org/obo/ARO_3004332 MCR-5.1 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase MCR-5 is a transposon-associated phosphoethanolamine transferase gene, identified in Salmonella Paratyphi B dTa+ (d-tartrate fermenting Salmonella enterica subsp. enterica serovar Paratyphi B) isolates from food-producing animals. The isolates were collected between 2011 and 2013, and retrieved from the German National Reference Laboratory for Salmonella. MCR-5 confers resistance to collistin through the addition of a phosphoethanolamine group to lipid A, causing a reduction in negative charge of the cell membrane. Described by Borowiak et al, 2017. http://purl.obolibrary.org/obo/ARO_3004333 triclosan resistant gyrA http://purl.obolibrary.org/obo/ARO_3000273 antibiotic resistant DNA topoisomerase subunit gyrA DNA gyrase is responsible for DNA supercoiling and consists of two alpha and two beta subunits. Point mutations in gyrA have been shown to decrease susceptibility to the antibiotic triclosan. Although the mechanism is unclear, it is hypothesized that changes in supercoiling activity of mutant DNA gyrase proteins alters expression of stress response pathways thereby indirectly decreasing triclosan susceptibility. It has been shown that triclosan does not interact directly with gyrA. http://purl.obolibrary.org/obo/ARO_3004334 Salmonella enterica gyrA with mutation conferring resistance to triclosan http://purl.obolibrary.org/obo/ARO_3004333 triclosan resistant gyrA Point mutations in Salmonella enterica serovar Typhimurium which have been shown to increase the minimum inhibitory concentration of the antibiotic triclosan. It is hypothesized that decreased susceptibility to triclosan in Salmonella gyrA mutants occurs indirectly due to alterations in the stress response pathways. http://purl.obolibrary.org/obo/ARO_3004335 Escherichia coli gyrA with mutation conferring resistance to triclosan http://purl.obolibrary.org/obo/ARO_3004333 triclosan resistant gyrA Point mutations in Escherichia coli which have been shown to increase the minimum inhibitory concentration of the antibiotic triclosan. It is hypothesized that decreased susceptibility to triclosan in E. coli gyrA mutants occurs indirectly due to alterations in the stress response pathways. http://purl.obolibrary.org/obo/ARO_3004336 PDC-73 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase An AmpC-like beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3004337 PDC-74 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase An AmpC-like beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3004338 PDC-75 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase An AmpC-like beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3004339 PDC-76 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase An AmpC-like beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3004340 PDC-77 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase An AmpC-like beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3004341 PDC-78 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase An AmpC-like beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3004342 PDC-79 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase An AmpC-like beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3004343 PDC-80 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase An AmpC-like beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3004344 PDC-81 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase An AmpC-like beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3004345 PDC-82 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase An AmpC-like beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3004346 PDC-83 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase An AmpC-like beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3004347 PDC-84 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase An AmpC-like beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3004348 PDC-85 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase An AmpC-like beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3004349 PDC-86 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase An AmpC-like beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3004350 PDC-87 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase An AmpC-like beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3004351 PDC-88 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase An AmpC-like beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3004352 PDC-89 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase An AmpC-like beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3004353 PDC-90 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase An AmpC-like beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3004354 PDC-91 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase An AmpC-like beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3004355 PDC-92 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase An AmpC-like beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3004356 PDC-93 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase An AmpC-like beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3009158 Human Genome Variation Society (HGVS) Nomenclature http://purl.obolibrary.org/obo/ARO_3000045 component of AMR genotypic or phenotypic terminology The HGVS Nomenclature is an internationally-recognized standard for the description of DNA, RNA, and protein sequence variants. It is used to convey variants in clinical reports and to share variants in publications and databases (https://hgvs-nomenclature.org/stable). http://purl.obolibrary.org/obo/ARO_3003855 ADC-10 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-10 is a beta-lactamase found in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3004094 Erm(48) http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase Erm(48) is a macrolide-lincosamide-streptogramin resistance gene identified on resistance plasmid pJW2311. http://purl.obolibrary.org/obo/ARO_3004572 Staphylococcus aureus LmrS http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump MFS transporters are secondary active transporters with single-polypeptide chains containing 400-600 amino acids that transport small solutes across the membrane by using electrochemical gradients. LmrS has 14 transmembrane helices and, when expressed in E. coli, is capable of extruding a variety of antibiotics inclinding linezolid, trimethoprim, florfenicol, chlorampheniocol, erythromycin, streptomycin, kanamycin, and fusidic acid. http://purl.obolibrary.org/obo/ARO_3004573 Acinetobacter baumannii AbaF http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump Expression of abaF in E. coli resulted in increased resistance to fosfomycin. http://purl.obolibrary.org/obo/ARO_3004574 Acinetobacter baumannii AbaQ http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump AbaQ is an MFS transporter mainly involved in the extrusion of quinolone-type drugs in A. baumannii. http://purl.obolibrary.org/obo/ARO_3004575 S-adenosylmethionine (SAM) superfamily http://purl.obolibrary.org/obo/ARO_3004274 23S ribosomal RNA methyltransferase Members of the radical SAM superfamily are involved in a wide variety of reactions, including unusual methylations, isomerization, sulfur insertion, ring formation, anaerobic oxidation, and protein radical formation. http://purl.obolibrary.org/obo/ARO_3004576 tet(61) http://purl.obolibrary.org/obo/ARO_0000002 tetracycline-resistant ribosomal protection protein A tetracycline-resistance ribosomal protection protein. http://purl.obolibrary.org/obo/ARO_3004577 Acinetobacter baumannii AmvA http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump AmvA has 14 alpha-helical transmembrane segments, qualifying it as a member of the DHA2 transporter family of the major facilitator superfamily (MFS). When AmvA was expressed in E. coli, the cells had at least four-fold decreased susceptibility to erythromycin, acridine orange, acriflavine, deoxycholate and methyl viologen. AmvA from the AC0037 strain of A. baumannii was tested. http://purl.obolibrary.org/obo/ARO_3004578 Acinetobacter baumannii AbuO http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance AbuO is akin to the TolC outer membrane efflux protein. Deletion in A. baumannii results in increased susceptibility to antibiotics including amikacin, carbenicillin, ceftriaxone, meropenem, streptomycin, and tigecycline as well as disinfectants benzyalkonium chloride and chlorhexidine. http://purl.obolibrary.org/obo/ARO_3004580 Klebsiella pneumoniae KpnE http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance KpnE subunit of KpnEF resembles EbrAB from E. coli. Mutation in KpnEF resulted in increased susceptibility to cefepime, ceftriaxon, colistin, erythromycin, rifampin, tetracycline, and streptomycin as well as enhanced sensitivity toward sodium dodecyl sulfate, deoxycholate, dyes, benzalkonium chloride, chlorhexidine, and triclosan. http://purl.obolibrary.org/obo/ARO_3004581 tet(48) http://purl.obolibrary.org/obo/ARO_3000036 tetracycline inactivation enzyme A tetracycline inactivating enzyme. A flavoenzyme capable of degrading tetracycline antibiotics. http://purl.obolibrary.org/obo/ARO_3004582 tet(49) http://purl.obolibrary.org/obo/ARO_3000036 tetracycline inactivation enzyme A tetracycline inactivating enzyme. A flavoenzyme capable of degrading tetracycline antibiotics. http://purl.obolibrary.org/obo/ARO_3004583 Klebsiella pneumoniae KpnF http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance KpnF subunit of KpnEF resembles EbrAB from E. coli. Mutation in KpnEF resulted in increased susceptibility to cefepime, ceftriaxon, colistin, erythromycin, rifampin, tetracycline, and streptomycin as well as enhanced sensitivity toward sodium dodecyl sulfate, deoxycholate, dyes, benzalkonium chloride, chlorhexidine, and triclosan. http://purl.obolibrary.org/obo/ARO_3004584 tet(50) http://purl.obolibrary.org/obo/ARO_3000036 tetracycline inactivation enzyme A tetracycline inactivating enzyme. A flavoenzyme capable of degrading tetracycline antibiotics. http://purl.obolibrary.org/obo/ARO_3004585 Klebsiella pneumoniae KpnEF http://purl.obolibrary.org/obo/ARO_0010003 small multidrug resistance (SMR) antibiotic efflux pump KpnEF resembles EbrAB from E. coli. Mutation in KpnEF resulted in increased susceptibility to cefepime, ceftriaxon, colistin, erythromycin, rifampin, tetracycline, and streptomycin as well as enhanced sensitivity toward sodium dodecyl sulfate, deoxycholate, dyes, benzalkonium chloride, chlorhexidine, and triclosan. http://purl.obolibrary.org/obo/ARO_3004586 tet(51) http://purl.obolibrary.org/obo/ARO_3000036 tetracycline inactivation enzyme A tetracycline inactivating enzyme. A flavoenzyme capable of degrading tetracycline antibiotics. http://purl.obolibrary.org/obo/ARO_3004587 tet(52) http://purl.obolibrary.org/obo/ARO_3000036 tetracycline inactivation enzyme A tetracycline inactivating enzyme. A flavoenzyme capable of degrading tetracycline antibiotics. http://purl.obolibrary.org/obo/ARO_3004588 Klebsiella pneumoniae KpnG http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance KpnG consists of ~390 residues and resembles EmrA of E. coli. Disruption of the pump components KpnG-KpnH signficantly decrease resistance to azithromycin, ceftazidime, ciprofloxacin, ertapenem, erythromycin, gentamicin, imipenem, ticarcillin, norfloxacin, polymyxin-B, piperacillin, spectinomycin, tobramycin, and streptomycin. http://purl.obolibrary.org/obo/ARO_3004589 tet(53) http://purl.obolibrary.org/obo/ARO_3000036 tetracycline inactivation enzyme A tetracycline inactivating enzyme. A flavoenzyme capable of degrading tetracycline antibiotics. http://purl.obolibrary.org/obo/ARO_3004590 tet(54) http://purl.obolibrary.org/obo/ARO_3000036 tetracycline inactivation enzyme A tetracycline inactivating enzyme. A flavoenzyme capable of degrading tetracycline antibiotics. http://purl.obolibrary.org/obo/ARO_3004591 tet(55) http://purl.obolibrary.org/obo/ARO_3000036 tetracycline inactivation enzyme A tetracycline inactivating enzyme. A flavoenzyme capable of degrading tetracycline antibiotics. http://purl.obolibrary.org/obo/ARO_3004592 erm(32) http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase erm(32) is a rRNA methyltransferase. Encodes methyltransferases that modify 23S rRNA. http://purl.obolibrary.org/obo/ARO_3004595 erm(45) http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase Erm45 is an rRNA methylase that confers resistances to macrolide, lincosamide, and streptogramin B. http://purl.obolibrary.org/obo/ARO_3004596 erm(46) http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase erm(46) is transferable determinant that confers resistance to macrolides. http://purl.obolibrary.org/obo/ARO_3004597 Klebsiella pneumoniae KpnH http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance KpnH consists of ~511 residues, resembles EmrB of E. coli, and is probably a translocase in the KpnGH-TolC efflux protein in K. pneumoniae. Disruption of the pump components KpnG-KpnH signficantly decrease resistance to azithromycin, ceftazidime, ciprofloxacin, ertapenem, erythromycin, gentamicin, imipenem, ticarcillin, norfloxacin, polymyxin-B, piperacillin, spectinomycin, tobramycin, and streptomycin. http://purl.obolibrary.org/obo/ARO_3004598 Klebsiella pneumoniae KpnGH-TolC http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump Disruption of the pump components KpnGH signficantly decrease resistance to azithromycin, ceftazidime, ciprofloxacin, ertapenem, erythromycin, gentamicin, imipenem, ticarcillin, norfloxacin, polymyxin-B, piperacillin, spectinomycin, tobramycin, and streptomycin. http://purl.obolibrary.org/obo/ARO_3004599 clcD http://purl.obolibrary.org/obo/ARO_3004607 Cfr Group clcD gene can provide resistance to representatives of five of the six antibiotic groups previously shown to be affected by Cfr. clcD was originally found in Clostridioides difficile and is cfr-like. http://purl.obolibrary.org/obo/ARO_3004600 LnuH http://purl.obolibrary.org/obo/ARO_3000221 lincosamide nucleotidyltransferase (LNU) LnuH is a lincosamide nucleotidyltransferase transferase. http://purl.obolibrary.org/obo/ARO_3004601 LnuP http://purl.obolibrary.org/obo/ARO_3000221 lincosamide nucleotidyltransferase (LNU) LnuP is a lincosamide nucleotidyltransferase major efflux facilitator. http://purl.obolibrary.org/obo/ARO_3004603 tet(56) http://purl.obolibrary.org/obo/ARO_3000036 tetracycline inactivation enzyme A tetracycline inactivating enzyme. A flavoenzyme capable of degrading tetracycline antibiotics. http://purl.obolibrary.org/obo/ARO_3004605 ermZ http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase ermZ is an methyltransferase modifying 23S rRNA conferring resistance to Spiramycin. http://purl.obolibrary.org/obo/ARO_3004606 erm(40) http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase erm(40) is an adenine RNA methylase and confers intrinsic resistance in Mycobacteria. http://purl.obolibrary.org/obo/ARO_3004607 Cfr Group http://purl.obolibrary.org/obo/ARO_3000202 Cfr 23S ribosomal RNA methyltransferase The cfr groups were determined by Candela et al (2017) by determining the phylogenetic relationship using the neighbour-joining method to compare the cfr-like proteins to cfr. http://purl.obolibrary.org/obo/ARO_3004608 EreD http://purl.obolibrary.org/obo/ARO_3000320 macrolide esterase EreD is an erythromycin esterase protein. http://purl.obolibrary.org/obo/ARO_3004609 cfr(B) Group http://purl.obolibrary.org/obo/ARO_3000202 Cfr 23S ribosomal RNA methyltransferase The cfr groups were determined by Candela et al (2017) by determining the phylogenetic relationship using the neighbour-joining method to compare the cfr-like proteins to cfr. http://purl.obolibrary.org/obo/ARO_3004610 cfr(C) Group http://purl.obolibrary.org/obo/ARO_3000202 Cfr 23S ribosomal RNA methyltransferase The cfr groups were determined by Candela et al (2017) by determining the phylogenetic relationship using the neighbour-joining method to compare the cfr-like proteins to cfr. http://purl.obolibrary.org/obo/ARO_3004613 tet(47) http://purl.obolibrary.org/obo/ARO_3000036 tetracycline inactivation enzyme A tetracycline inactivating enzyme. A flavoenzyme capable of degrading tetracycline antibiotics. http://purl.obolibrary.org/obo/ARO_3004615 ADC-11 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-11 is a class C beta-lactamase found in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3004616 Mycoplasma genitalium 23S rRNA mutations confers resistance to fluoroquinolone and macrolide antibiotics http://purl.obolibrary.org/obo/ARO_3004125 23S rRNA with mutation conferring resistance to macrolide antibiotics Mycoplasma genitalium strain M6320 contains mutations that lead to resistance to fluoroquinolone and macrolide antibiotics. http://purl.obolibrary.org/obo/ARO_3004617 ADC-30 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity An ADC beta-lactamase and cephalosporinase from Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3004618 ADC-58 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity An ADC beta-lactamase and cephalosporinase from Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3004619 ADC-59 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity An ADC beta-lactamase and cephalosporinase from Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3004620 ADC-60 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity An ADC beta-lactamase and cephalosporinase from Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3004621 AAC(3)-IIe http://purl.obolibrary.org/obo/ARO_3007385 AAC(3)-II AAC(3)-IIe is a plasmid-encoded aminoglycoside acetyltransferase in E. coli. http://purl.obolibrary.org/obo/ARO_3004622 QnrS10 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrS10 is a plasmid-mediated quinolone resistance protein. http://purl.obolibrary.org/obo/ARO_3004623 AAC(3)-IId http://purl.obolibrary.org/obo/ARO_3007385 AAC(3)-II AAC(3)-IId is a plasmid-encoded aminoglycoside acetyltransferase in E. coli. http://purl.obolibrary.org/obo/ARO_3004624 QnrS11 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrS11 is a plasmid-mediated quinolone resistance protein. http://purl.obolibrary.org/obo/ARO_3004625 QnrS12 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrS12 is a plasmid-mediated quinolone resistance protein. http://purl.obolibrary.org/obo/ARO_3004626 Erm(49) http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase Erm(49) is an rRNA methylase gene. http://purl.obolibrary.org/obo/ARO_3004627 QnrS15 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrS15 is a plasmid-mediated quinolone resistance protein. http://purl.obolibrary.org/obo/ARO_3004628 AAC(2')-IIa http://purl.obolibrary.org/obo/ARO_3007394 AAC(2')-II AAC(2')-IIa is a kasugamycin 2' N-acetyltransferase protein found in Burkholderia glumae and Acidovorax avenae isolates. http://purl.obolibrary.org/obo/ARO_3004629 AAC(6')-Im http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Im is an aminoglycoside acetyltransferase encoded by plasmids in E. coli, and E. faecium. http://purl.obolibrary.org/obo/ARO_3004630 Mycoplasma genitalium parC mutations confers resistance to Moxifloxacin http://purl.obolibrary.org/obo/ARO_3000619 fluoroquinolone resistant parC Mycoplasma genitalium exhibits multiple mutations in parC which confers resistance to Moxifloxacin. http://purl.obolibrary.org/obo/ARO_3004631 Mycoplasma genitalium gyrA mutation confers resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3003292 fluoroquinolone resistant gyrA Mycoplasma Genitalium GyrA mutations confers resistance to fluoroquinolones such as Moxifloxacin. http://purl.obolibrary.org/obo/ARO_3004632 ADC-62 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity A class ADC beta-lactamase and cephalosporinase from Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3004633 ADC-67 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity A class C beta-lactamase and cephalosporinase from Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3004634 ADC-73 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity A class C ADC beta-lactamase and cephalosporinase found in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3004635 AAC(6')-Il http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Il is an aminoglycoside acetyltransferase encoded by plasmids and integrons in Enterobacter cloaecae and Klebsiella aerogenes. http://purl.obolibrary.org/obo/ARO_3004636 qnrE1 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) qnrE1 is a member of the qnrE family of plasmid-borne (fluoro)quinolone-resistance genes, with chromosomal origins from Enterobacter spp. http://purl.obolibrary.org/obo/ARO_3004637 qnrE2 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) qnrE2 is a qnrE-member of plasmid-borne (fluoro)quinolone-resistance genes. http://purl.obolibrary.org/obo/ARO_3004638 AAC(6')-I-48 http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-I-48 (AAC(6')-Iag) is an aminoglycoside acetyltransferase encoded by integrons in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3004639 Corynebacterium striatum tetA http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump The tetAB genes of the Corynebacterium striatum R-plasmid encode an ABC transporter and confer tetracycline, oxytetracycline, and oxalic resistance. http://purl.obolibrary.org/obo/ARO_3004640 dfrA15b http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr A dihydrofolate reductase found in Salmonella Enterica. http://purl.obolibrary.org/obo/ARO_3004641 AAC(6')-I-43 http://purl.obolibrary.org/obo/ARO_3000345 AAC(6') AAC(6')-I-43 (aacA43) is an aminoglycoside acetyltransferase encoded by integrons found in Klebsiella pneumoniae, Escherichia coli, and Enterobacter cloaecae. http://purl.obolibrary.org/obo/ARO_3004642 dfrA3b http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr A dihydrofolate reductase that confers resistance to trimethoprim. http://purl.obolibrary.org/obo/ARO_3004643 Erm(K) http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase A 23S rRNA (adenine(2058)-N(6))-methyltransferase Erm(K) [Alkalihalobacillus halodurans]. http://purl.obolibrary.org/obo/ARO_3004644 dfrA6 from Proteus mirabilis http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr dfrA6 is a dihydrofolate reductase that confers resistance to trimethoprim. Found in Proteus mirabilis. http://purl.obolibrary.org/obo/ARO_3004645 dfrI http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr dfrI is a dihydrofolate reductase that is resistant to trimethoprim. http://purl.obolibrary.org/obo/ARO_3004647 AQU-2 http://purl.obolibrary.org/obo/ARO_3002992 AQU beta-lactamase AQU-2 is a chromosomally-encoded AQU class C beta-lactamase and cephalosporinase from Aeromonas. http://purl.obolibrary.org/obo/ARO_3004648 AQU-3 http://purl.obolibrary.org/obo/ARO_3002992 AQU beta-lactamase AQU-3 is a chromosomally-encoded AQU class C beta-lactamase and cephalosporinase from. http://purl.obolibrary.org/obo/ARO_3004649 cfr(B) http://purl.obolibrary.org/obo/ARO_3004609 cfr(B) Group cfr(B) has been observed in mobile genetic elements in E. faecium and Clostridioides difficile and confers resistance to linezolid, clindamycin, erythromycin, chloramphenicol, and retapamulin. http://purl.obolibrary.org/obo/ARO_3004650 tet(U) http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump Initially reported as a tetracycline-resistant determinant encoded on the plasmid pKQ10 in Enterococcus faecium, tet(U) has since been determined to be a misannotation of a gene product not involved in tetracycline resistance. http://purl.obolibrary.org/obo/ARO_3004651 lin http://purl.obolibrary.org/obo/ARO_3000221 lincosamide nucleotidyltransferase (LNU) Listeria monocytogenes EGD-e lin gene for lincomycin resistance ABC-F type ribosomal protection protein, complete CDS. http://purl.obolibrary.org/obo/ARO_3004652 Erm(O)-lrm http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase ErmO (gene lrm) lincomycin resistance methylase [Streptomyces lividans]. http://purl.obolibrary.org/obo/ARO_3004653 tetR(G) http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump Class G tetracycline resistance determinant from Vibrio anguillarum. http://purl.obolibrary.org/obo/ARO_3004654 Clostridioides difficile 23S rRNA with mutation conferring resistance to erythromycin and clindamycin http://purl.obolibrary.org/obo/ARO_3004125 23S rRNA with mutation conferring resistance to macrolide antibiotics SNP causing high-level ERY resistance and low-level CLI resistance. http://purl.obolibrary.org/obo/ARO_3004656 catII from Escherichia coli K-12 http://purl.obolibrary.org/obo/ARO_3000122 chloramphenicol acetyltransferase (CAT) catII is a chloramphenicol acetyltransferase. This particular catII is found in E.coli K-12. Confers resistance to chloramphenicol. http://purl.obolibrary.org/obo/ARO_3004657 catA4 http://purl.obolibrary.org/obo/ARO_3000122 chloramphenicol acetyltransferase (CAT) catA4 is a chloramphenicol acetyltransferase that confers resistance to chloramphenicol. http://purl.obolibrary.org/obo/ARO_3004658 catA8 http://purl.obolibrary.org/obo/ARO_3000122 chloramphenicol acetyltransferase (CAT) catA8 is a chloramphenicol acetyltransferase that confers resistance to chloramphenicol. http://purl.obolibrary.org/obo/ARO_3004659 Mef(En2) http://purl.obolibrary.org/obo/ARO_3000747 mef NBU2-encoded resistance gene. An MefE homolog in Bacteroides species. Macrolide efflux MFS transporter. http://purl.obolibrary.org/obo/ARO_3004660 catB11 http://purl.obolibrary.org/obo/ARO_3000122 chloramphenicol acetyltransferase (CAT) catB11 is a chloramphenicol acetyltransferase that confers resistance to chloramphenicol. http://purl.obolibrary.org/obo/ARO_3004661 Staphylococcus aureus FosB http://purl.obolibrary.org/obo/ARO_3000133 fosfomycin thiol transferase The Bacillus subtilis fosB gene encodes a fosfomycin resistance protein. http://purl.obolibrary.org/obo/ARO_3004662 MCR-3.3 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase MCR-3.3 is a colistin resistance gene variant in the chromosome of an Aeromonas veronii. Conferred polymyxin resistance in both E. Coli and Aeromonas salmonicida. http://purl.obolibrary.org/obo/ARO_3004663 FusF http://purl.obolibrary.org/obo/ARO_3005086 Target protecting FusB-type protein conferring resistance to Fusidic acid A fusidic acid resistance determinant in Staphylococcus cohnii. This protein behaves akin to FusB as it is a FusB-type protein. It mediates dissociation of EF-G from the ribosome thus counteracting the action of Fusidic acid. http://purl.obolibrary.org/obo/ARO_3004665 cmlA8 http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump cmlA8 is a plasmid that confers resistance to chloramphenicol. http://purl.obolibrary.org/obo/ARO_3004666 pexA http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump pexA is a florfenicol and chloramphenicol resistance gene discovered in Alaskan soil. http://purl.obolibrary.org/obo/ARO_3004667 Staphylococcus aureus norA http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump NorA gene cloned from Staphylococcus aureus conferred relatively high resistance to hydrophilic quinolones such as norfloxacin, enoxacin, ofloxacin, and ciprofloxacin in S. aureus and Escherichia coli. Had low or no resistance at all to hydrophobic ones such as nalidixic acid, oxolinic acid, and sparfloxacin in S. aureus and Escherichia coli. http://purl.obolibrary.org/obo/ARO_3004668 QnrAS http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) Located on the chromosome of Aliivibrio salmonicida. Provides low-level resistance to quinolones. http://purl.obolibrary.org/obo/ARO_3004669 emtA http://purl.obolibrary.org/obo/ARO_3001298 non-erm 23S ribosomal RNA methyltransferase (G748) A rRNA methyltransferase conferring high-level evernimicin resistance. http://purl.obolibrary.org/obo/ARO_3004670 FosB1 http://purl.obolibrary.org/obo/ARO_3000133 fosfomycin thiol transferase Subtype of FosB, fosfomycin resistant. S.aureus SA1129 carried a FosB1 identical to S. haemolyticus. http://purl.obolibrary.org/obo/ARO_3004671 FosB4 http://purl.obolibrary.org/obo/ARO_3000133 fosfomycin thiol transferase Fosfomycin resistance gene. Shares a high homology with FosB1 and FosB3. http://purl.obolibrary.org/obo/ARO_3004672 FosB5 http://purl.obolibrary.org/obo/ARO_3000133 fosfomycin thiol transferase Fosfomycin resistance gene. High homology with FosB1 and FosB3. http://purl.obolibrary.org/obo/ARO_3004673 FosB6 http://purl.obolibrary.org/obo/ARO_3000133 fosfomycin thiol transferase Fosfomycin resistance gene. High homology with FosB1 and FosB3. http://purl.obolibrary.org/obo/ARO_3004674 FosD http://purl.obolibrary.org/obo/ARO_3000133 fosfomycin thiol transferase A fosfomycin resistance gene. http://purl.obolibrary.org/obo/ARO_3004675 aphA15 http://purl.obolibrary.org/obo/ARO_3007406 APH(3')-I Expression of cloned aphA15 gene in Escherichia coli reduced the susceptibility to kanamycin and neomycin, as well as to amikacin, netilmicin, and streptomycin. http://purl.obolibrary.org/obo/ARO_3004677 rmtD2 http://purl.obolibrary.org/obo/ARO_3004271 16S rRNA methyltransferase (G1405) The first allele of a 16S rRNA methyltransferase gene, rmtD2, confers a high resistance to all clinically available aminoglycosides. http://purl.obolibrary.org/obo/ARO_3004678 rmtE http://purl.obolibrary.org/obo/ARO_3004271 16S rRNA methyltransferase (G1405) Aminoglycoside-resistance gene. http://purl.obolibrary.org/obo/ARO_3004679 rmtE2 http://purl.obolibrary.org/obo/ARO_3004271 16S rRNA methyltransferase (G1405) A 16S rRNA mathyltransferase gene with a single nucleotide mutation compared to rmtE. http://purl.obolibrary.org/obo/ARO_3004680 APH(3')-VIIIa http://purl.obolibrary.org/obo/ARO_3000126 APH(3') APH(3')-VIIIa is an aminoglycoside phosphoryltransferase that acts on the 3-OH target of aminoglycosides found in Streptomyces rimosus. http://purl.obolibrary.org/obo/ARO_3004681 Clostridioides difficile rpoC with mutation conferring resistance to vancomycin http://purl.obolibrary.org/obo/ARO_3004725 vancomycin-resistant beta prime subunit of RNA polymerase (rpoC) Point mutations in the rpoC region of Clostridioides difficile which confer resistance to vancomycin. http://purl.obolibrary.org/obo/ARO_3004682 aadA27 http://purl.obolibrary.org/obo/ARO_3000232 ANT(3'')-Ia Small mobilizable plasmid pALWED1.8 containing a novel variant of the streptomycin/spectinomycin resistance gene. http://purl.obolibrary.org/obo/ARO_3004683 aadS http://purl.obolibrary.org/obo/ARO_3007399 ANT(6)-I A novel Tn4551 streptomycin-resistance gene that was phenotypically silent in wild-type Bacteroides; expression could be activated by a trans-acting chromosomal mutation. http://purl.obolibrary.org/obo/ARO_3004684 MCR-9.1 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase A mobilized and plasmid-mediated colistin resistance gene and phosphoethanolamine transferase identified from a Salmonella enterica isolate. http://purl.obolibrary.org/obo/ARO_3004685 MCR-1.5 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase A plasmid-mediated MCR-1 variant identified from polyclonal clinical Escherichia coli. http://purl.obolibrary.org/obo/ARO_3004686 MCR-1.7 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase A plasmid-mediated MCR-1 variant identified from Escherichia coli. http://purl.obolibrary.org/obo/ARO_3004687 MCR-1.8 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An unpublished MCR-1 variant. http://purl.obolibrary.org/obo/ARO_3004688 MCR-1.11 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase A plasmid-mediated phosphoethanolamine transferase and MCR-1 variant identified from Escherichia coli as conferring resistance to colistin antibiotics. http://purl.obolibrary.org/obo/ARO_3004689 MCR-1.12 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase A plasmid-mediated phosphoethanolamine transferase and MCR-1 variant identified from Escherichia coli and conferring resistance to colistin antibiotics. http://purl.obolibrary.org/obo/ARO_3004690 MCR-1.13 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase A plasmid-mediated phosphoethanolamine transferase and MCR-1 variant identified from Escherichia coli. http://purl.obolibrary.org/obo/ARO_3004691 MCR-3.4 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase A plasmid-mediated MCR-3.1 variant. http://purl.obolibrary.org/obo/ARO_3004692 aadA10 http://purl.obolibrary.org/obo/ARO_3000232 ANT(3'')-Ia aadA10 is a aminoglycoside nucleotidyltransferase gene encoded by plasmids in P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3004693 MCR-3.12 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase A plasmid-mediated phosphoethanolamine transferase and MCR-3 variant conferring resistance to colistin antibiotics. http://purl.obolibrary.org/obo/ARO_3004694 MCR-4.2 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase A plasmid-mediated MCR-4 variant which confers resistance to colistin antibiotics. http://purl.obolibrary.org/obo/ARO_3004695 MCR-4.3 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase A plasmid-mediated MCR-4 variant and colistin resistance gene from clinical Enterobacteriaceae. http://purl.obolibrary.org/obo/ARO_3004696 MCR-4.4 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase A plasmid-mediated MCR-4 variant and colistin resistance gene. http://purl.obolibrary.org/obo/ARO_3004697 MCR-4.5 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase A plasmid-mediated MCR-4 variant and colistin resistance gene. http://purl.obolibrary.org/obo/ARO_3004698 MCR-5.2 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase A plasmid-mediated MCR-5 variant from Escheichia coli which confers resistance to colistin antibiotics. http://purl.obolibrary.org/obo/ARO_3004699 sta http://purl.obolibrary.org/obo/ARO_3000869 streptothricin acetyltransferase (SAT) Streptothricin acetyltransferase gene (STAT gene) that confers streptothricin resistance on Escherichia coli and Bacillus subtilis. http://purl.obolibrary.org/obo/ARO_3004700 mutation in resistance determinant http://purl.obolibrary.org/obo/ARO_3004524 strain type Mutation in a resistance determinant rendering it non-functional. http://purl.obolibrary.org/obo/ARO_3004701 ceftazidime-cloxacillin http://purl.obolibrary.org/obo/ARO_3000707 antibiotic mixture An antibiotic cocktail containing beta-lactam penam antibiotic cloxacillin and the cephalosporin ceftazidime. http://purl.obolibrary.org/obo/ARO_3004702 cefepime-cloxacillin http://purl.obolibrary.org/obo/ARO_3000707 antibiotic mixture An antibiotic cocktail containing the cephalosporin cefepime and the penicillin cloxacillin. http://purl.obolibrary.org/obo/ARO_3004703 imipenem-cloxacillin http://purl.obolibrary.org/obo/ARO_3000707 antibiotic mixture An antibiotic cocktail containing beta-lactam penam antibiotic cloxacillin and the beta-lactam carbapenam antibiotic imipenam. http://purl.obolibrary.org/obo/ARO_3004704 aadA8b http://purl.obolibrary.org/obo/ARO_3000232 ANT(3'')-Ia aadA8b is an aminoglycoside nucleotidyltransferase gene encoded by plasmids in E. coli; can be created by a recombination event between aadA1 and aadA2. http://purl.obolibrary.org/obo/ARO_3004705 ceftazidime-clavulanic acid http://purl.obolibrary.org/obo/ARO_3000707 antibiotic mixture An antibiotic cocktail containing the cephalosporin antibiotic ceftazidime and the beta-lactamase inhibitor clavulanic acid. http://purl.obolibrary.org/obo/ARO_3004706 mutation in resistance determinant with plasmid harbouring resistance determinant http://purl.obolibrary.org/obo/ARO_3004524 strain type Experimental protocol where there is a mutation of resistance determinant and the transformation of a plasmid harbouring resistance determinant into the same strain. http://purl.obolibrary.org/obo/ARO_3004707 cefoxitin-clavulanate http://purl.obolibrary.org/obo/ARO_3000707 antibiotic mixture An antibiotic cocktail containing the cephamycin antibiotic cefoxitin and the beta-lactamase inhibitor clavulanate. http://purl.obolibrary.org/obo/ARO_3004708 cefoxitin-sulbactam http://purl.obolibrary.org/obo/ARO_3000707 antibiotic mixture An antibiotic cocktail containing the cephamycin antibiotic cefoxitin and the beta-lactamase inhibitor sulbactam. http://purl.obolibrary.org/obo/ARO_3004709 cefoxitin-tazobactam http://purl.obolibrary.org/obo/ARO_3000707 antibiotic mixture An antibiotic cocktail containing the cephamycin antibiotic cefoxitin and the beta-lactamase inhibitor tazobactam. http://purl.obolibrary.org/obo/ARO_3004710 cefotaxime-clavulanic acid http://purl.obolibrary.org/obo/ARO_3000707 antibiotic mixture An antibiotic cocktail containing the cephalosporin antibiotic cefotaxime and the beta-lactamase inhibitor clavulanic acid. http://purl.obolibrary.org/obo/ARO_3004711 cefotaxime-tazobactam http://purl.obolibrary.org/obo/ARO_3000707 antibiotic mixture An antibiotic cocktail containing the cephalosporin antibiotic cefotaxime and the beta-lactamase inhibitor Tazobactam. http://purl.obolibrary.org/obo/ARO_3004712 ceftazidime-tazobactam http://purl.obolibrary.org/obo/ARO_3000707 antibiotic mixture An antibiotic cocktail containing the cephalosporin antibiotic ceftazidime and the beta-lactamase inhibitor tazobactam. http://purl.obolibrary.org/obo/ARO_3004713 aztreonam-clavulanate http://purl.obolibrary.org/obo/ARO_3000707 antibiotic mixture An antibiotic cocktail containing the beta-lactam antibiotic aztreonam and the conjugate base of the beta-lactamase inhibitor clavulanic acid (clavulanate). http://purl.obolibrary.org/obo/ARO_3004714 aztreonam-tazobactam http://purl.obolibrary.org/obo/ARO_3000707 antibiotic mixture An antibiotic cocktail containing the beta-lactam antibiotic aztreonam and the beta-lactamase inhibitor tazobactam. http://purl.obolibrary.org/obo/ARO_3004715 vga(E) Staphylococcus cohnii http://purl.obolibrary.org/obo/ARO_3000113 vga-type ABC-F protein vga(E) gene variant that confers resistance to pleuromutilins, lincosamides and streptogramin A antibiotics in staphylococci. http://purl.obolibrary.org/obo/ARO_3004716 Vanillobiocin http://purl.obolibrary.org/obo/ARO_3000103 aminocoumarin antibiotic Antibiotic similar to clorobiocin, but with vanillic acid as the acyl component instead of crenelated 4-hydroxybenzoic acid. http://purl.obolibrary.org/obo/ARO_3004717 Isovanillobiocin http://purl.obolibrary.org/obo/ARO_3000103 aminocoumarin antibiotic Antibiotic similar to clorobiocin, but with vanillic acid as the acyl component instead of crenelated 4-hydroxybenzoic acid. different from vanillobiocin by the [psition of the pyrrole unit attached to the sugar moiety of the antibiotic. http://purl.obolibrary.org/obo/ARO_3004718 Declovanillobiocin http://purl.obolibrary.org/obo/ARO_3000103 aminocoumarin antibiotic Antibiotic similar to clorobiocin, but with vanillic acid as the acyl component instead of crenelated 4-hydroxybenzoic acid. Declovanillobiocin lacks the chlorine atom at the aminocoumarin ring compared to vanillobiocin. http://purl.obolibrary.org/obo/ARO_3004719 tet(X3) http://purl.obolibrary.org/obo/ARO_3000036 tetracycline inactivation enzyme A tetracyline resistance gene located on an approximately 300-kb plasmid, designated p47AB. It inactivates all tetracyclines, including tigecycline, eravacycline, and omadacycline.Adjacent to insertion sequence ISVsa3 on the conjugative plasmid. http://purl.obolibrary.org/obo/ARO_3004720 tet(X4) http://purl.obolibrary.org/obo/ARO_3000036 tetracycline inactivation enzyme A tetracyline resistance gene located on an approximately 180-kb plasmid, designated p47EC. It inactivates all tetracyclines, including tigecycline, eravacycline, and omadacycline.Adjacent to insertion sequence ISVsa3 on the conjugative plasmid. http://purl.obolibrary.org/obo/ARO_3004721 Mycobacterium tuberculosis rpsA mutations conferring resistance to pyrazinamide http://purl.obolibrary.org/obo/ARO_3004722 pyrazinamide resistant rpsA RpsA, the 30S ribosomal protein S1 of Mycobacterium tuberculosis, is involved in trans-translation and is targeted by pyrazinonic acid, the active form of the antibiotic pyrazinamide, which disrupts the initiation of mRNA translation. Mutations in the amino acid sequence of rpsA can confer resistance to pyrazinamide maintaining rpsA function. http://purl.obolibrary.org/obo/ARO_3004722 pyrazinamide resistant rpsA http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant The 30S ribosomal protein S1 of Mycobacterium tuberculosis is required for mRNA translation initiation, playing a particular role in trans-translation. Mutations to rpsA prevent pyrazinoic acid, the active form of pyrazinamide catalyzed by pncA, from targeting RpsA to inhibit translation. http://purl.obolibrary.org/obo/ARO_3004723 gradient plate method http://purl.obolibrary.org/obo/ARO_3004388 in-vitro microbial susceptibility test A method to determine microbial susceptibility to antibiotics in which test bacteria is inoculated onto an agar plate that contains a concentration gradient of antibiotic. The minimum inhibitory concentration of antibiotic is assessed. http://purl.obolibrary.org/obo/ARO_3004724 ceftolozane-tazobactam http://purl.obolibrary.org/obo/ARO_3000707 antibiotic mixture An antibiotic cocktail containing the cephalosporin antibiotic ceftolozane and the beta-lactamase inhibitor tazobactam. http://purl.obolibrary.org/obo/ARO_3004725 vancomycin-resistant beta prime subunit of RNA polymerase (rpoC) http://purl.obolibrary.org/obo/ARO_3003289 antibiotic resistant rpoC Point mutations in rpoC, an RNA polymerase subunit, which confer resistance to vancomycin. http://purl.obolibrary.org/obo/ARO_3004823 IMP-52 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-52 is a class B metallo-beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3004824 LAP beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase LAP is a Ambler Class A beta-lactamase gene family that confers resistance to beta-lactams. http://purl.obolibrary.org/obo/ARO_3004825 LAP-1 http://purl.obolibrary.org/obo/ARO_3004824 LAP beta-lactamase LAP-1 is an Ambler Class A beta-lactamase gene. http://purl.obolibrary.org/obo/ARO_3004826 LAP-2 http://purl.obolibrary.org/obo/ARO_3004824 LAP beta-lactamase LAP-2 is an Ambler Class A beta-lactamase gene. http://purl.obolibrary.org/obo/ARO_3004827 LEN-35 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase LEN-35 is a Class A beta-lactamase gene found in Klebsiella variicola. http://purl.obolibrary.org/obo/ARO_3004828 LEN-36 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase LEN-36 is a class A beta-lactamase gene found in Klebsiella variicola. http://purl.obolibrary.org/obo/ARO_3004829 LEN-37 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase LEN-37 is a Class A beta-lactamase gene found in Klebsiella variicola. http://purl.obolibrary.org/obo/ARO_3004832 Neisseria gonorrhoeae PBP2 conferring resistance to beta-lactam antibiotics http://purl.obolibrary.org/obo/ARO_3003938 Penicillin-binding protein mutations conferring resistance to beta-lactam antibiotics PBP2 is a penicillin-binding protein and beta-lactam resistance enzyme encoded by the penA gene, due to mutations can cause resistance to various drugs such as Penicillin and Ceftriaxone. http://purl.obolibrary.org/obo/ARO_3005387 AAK beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase AAK beta-lactamases are a group of class A beta-lactamases found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3005388 AFM beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase AFM beta-lactamases are class B1 beta-lactamases found in proteobacteria like Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005389 ALG11 beta-lactamase http://purl.obolibrary.org/obo/ARO_3000571 subclass B3 (metallo-) beta-lactamase ALG11 beta-lactamases are class B3 beta-lactamases. http://purl.obolibrary.org/obo/ARO_3005390 ALG6 beta-lactamases http://purl.obolibrary.org/obo/ARO_3000571 subclass B3 (metallo-) beta-lactamase ALG6 beta-lactamases are class B3 beta-lactamases. http://purl.obolibrary.org/obo/ARO_3005391 ALI beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase ALI beta-lactamases are class B1 beta-lactamases found in species of the Aliivibrio genus. http://purl.obolibrary.org/obo/ARO_3005392 ANA beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase ANA beta-lactamases are class B1 beta-lactamases found in Anaeromyxobacter. http://purl.obolibrary.org/obo/ARO_3005393 AXC beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase AXC beta-lactamases are class A beta-lactamase found in the Anaeromyxobacter genus. http://purl.obolibrary.org/obo/ARO_3005394 BSU beta-lactamase http://purl.obolibrary.org/obo/ARO_3000075 class D beta-lactamase BSU beta-lactamases are class D beta-lactamases found in Bacillus inaquosorum. http://purl.obolibrary.org/obo/ARO_3005395 CAR beta-lactamase http://purl.obolibrary.org/obo/ARO_3000571 subclass B3 (metallo-) beta-lactamase CAR beta-lactamases are class B3 beta-lactamases found in Pectobacterium atrosepticum. http://purl.obolibrary.org/obo/ARO_3005396 CDD beta-lactamase http://purl.obolibrary.org/obo/ARO_3000075 class D beta-lactamase CDD beta-lactamases are class D beta-lactamases found in Clostridioides difficile. http://purl.obolibrary.org/obo/ARO_3005397 CMA beta-lactamase http://purl.obolibrary.org/obo/ARO_3000076 class C beta-lactamase CMA beta-lactamases are class C beta-lactamases found in Cronobacter malonaticus. http://purl.obolibrary.org/obo/ARO_3005398 CRD3 beta-lactamase http://purl.obolibrary.org/obo/ARO_3000571 subclass B3 (metallo-) beta-lactamase CRD3 beta-lactamases are class B3 beta-lactamases. http://purl.obolibrary.org/obo/ARO_3005399 CRH beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase CRH beta-lactamases are class A beta-lactamases found in Chromobacterium haemolyticum. http://purl.obolibrary.org/obo/ARO_3005400 CRP beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase CRP beta-lactamases are class A beta-lactamase found in Chromobacterium piscinae. http://purl.obolibrary.org/obo/ARO_3005401 CSA beta-lactamase http://purl.obolibrary.org/obo/ARO_3000076 class C beta-lactamase CSA beta-lactamases are class C beta-lactamases found in Cronobacter sakazakii. http://purl.obolibrary.org/obo/ARO_3005402 CSP beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase CSP beta-lactamases are class A beta-lactamases found in Capnocytophaga sputigena. http://purl.obolibrary.org/obo/ARO_3005403 CVI beta-lactamase http://purl.obolibrary.org/obo/ARO_3000570 subclass B2 (metallo-) beta-lactamase CVI beta-lactamases are a class B2 beta-lactamase found in Chromobacterium violaceum. http://purl.obolibrary.org/obo/ARO_3005404 DHT2 beta-lactamase http://purl.obolibrary.org/obo/ARO_3000571 subclass B3 (metallo-) beta-lactamase DHT2 beta-lactamases are class B3 beta-lactamases. http://purl.obolibrary.org/obo/ARO_3005405 EAM beta-lactamase http://purl.obolibrary.org/obo/ARO_3000571 subclass B3 (metallo-) beta-lactamase EAM beta-lactamase are class B3 beta-lactamases found in Qipengyuania aquimaris. http://purl.obolibrary.org/obo/ARO_3005406 EC beta-lactamase http://purl.obolibrary.org/obo/ARO_3000076 class C beta-lactamase EC beta-lactamases are class C beta-lactamases found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3005407 ECM beta-lactamase http://purl.obolibrary.org/obo/ARO_3000571 subclass B3 (metallo-) beta-lactamase ECM beta-lactamases are class B3 beta-lactamases found in Qipengyuania citrea. http://purl.obolibrary.org/obo/ARO_3005408 ECV beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase ECV beta-lactamases are class B1 beta-lactamases found in Echinicola vietnamensis. http://purl.obolibrary.org/obo/ARO_3005409 EFM beta-lactamase http://purl.obolibrary.org/obo/ARO_3000571 subclass B3 (metallo-) beta-lactamase EFM beta-lactamases are class B3 beta-lactamase found in Qipengyuania flava. http://purl.obolibrary.org/obo/ARO_3005410 ELM beta-lactamase http://purl.obolibrary.org/obo/ARO_3000571 subclass B3 (metallo-) beta-lactamase ELM beta-lactamases are class B3 beta-lactamases found in Erythrobacter longus. http://purl.obolibrary.org/obo/ARO_3005411 EVM beta-lactamase http://purl.obolibrary.org/obo/ARO_3000571 subclass B3 (metallo-) beta-lactamase EVM beta-lactamases are class B3 beta-lactamases found in Qipengyuania vulgaris. http://purl.obolibrary.org/obo/ARO_3005412 FIA beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase FIA beta-lactamases are class B1 beta-lactamases found in Fibrella aestuarina. http://purl.obolibrary.org/obo/ARO_3005413 GIL beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase GIL-beta-lactamases are class A beta-lactamases found in Citrobacter gillenii. http://purl.obolibrary.org/obo/ARO_3005414 GMB beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase GMB beta-lactamases are class B1 beta-lactamases found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3005415 GRD23 beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase GRD23 beta-lactamases are class B1 beta-lactamases. http://purl.obolibrary.org/obo/ARO_3005416 GRD33 beta-lactamase http://purl.obolibrary.org/obo/ARO_3000571 subclass B3 (metallo-) beta-lactamase GRD33 beta-lactamases are class B3 beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005417 KLUC beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase KLUC beta-lactamases are class A beta-lactamases found in Kluyvera cryocrescens, Escherichia coli and Enterobacteriaceae. http://purl.obolibrary.org/obo/ARO_3005418 LHK beta-lactamase http://purl.obolibrary.org/obo/ARO_3000076 class C beta-lactamase LHK beta-lactamases are class C beta-lactamases found in Laribacter hongkongensis. http://purl.obolibrary.org/obo/ARO_3005419 LRG beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase LRG beta-lactamases are class A beta-lactamases. http://purl.obolibrary.org/obo/ARO_3005420 LUS beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase LUS beta-lactamases are class A beta-lactamases found in Pedobacter lusitanus. http://purl.obolibrary.org/obo/ARO_3005421 LUT beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase LUT beta-lactamases are class A beta lactamases found in Pseudomonas luteola. http://purl.obolibrary.org/obo/ARO_3005422 MAL beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase MAL beta-lactamase are class A beta-lactamases found in Citrobacter koseri. http://purl.obolibrary.org/obo/ARO_3005423 MBL beta-lactamase http://purl.obolibrary.org/obo/ARO_3000571 subclass B3 (metallo-) beta-lactamase MBL beta-lactamases are class B3 beta-lactamases found in Caulobacter vibrioides. http://purl.obolibrary.org/obo/ARO_3005424 MOC beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase MOC beta-lactamases are class B1 beta-lactamase found in Myroides odoratus. http://purl.obolibrary.org/obo/ARO_3005425 MOR beta-lactamase http://purl.obolibrary.org/obo/ARO_3000076 class C beta-lactamase MOR beta-lactamases are class C beta-lactamases found in Morganella morganii. http://purl.obolibrary.org/obo/ARO_3005426 MYO beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase MYO beta-lactamases are class B1 beta-lactamases found in Myroides odoratimimus. http://purl.obolibrary.org/obo/ARO_3005427 MYX beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase MYX beta-lactamases are class B1 beta-lactamases found in Myxococcus. http://purl.obolibrary.org/obo/ARO_3005428 OHIO beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase OHIO beta-lactamases are class A beta-lactamases. http://purl.obolibrary.org/obo/ARO_3005429 ORN beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase ORN beta-lactamases are class A beta-lactamases found in Raoultella ornithinolytica. http://purl.obolibrary.org/obo/ARO_3005430 ORR beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase ORR beta-lactamases are class B1 beta-lactamases found in Ornithobacterium rhinotracheale. http://purl.obolibrary.org/obo/ARO_3005431 PAU beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase PAU beta-lactamases are class A beta-lactamases found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005432 PFM beta-lactamase http://purl.obolibrary.org/obo/ARO_3000570 subclass B2 (metallo-) beta-lactamase PFM beta-lactamases are class B2 beta-lactamases found in Pseudomonas fluorescens. http://purl.obolibrary.org/obo/ARO_3005433 PLA beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase PLA beta-lactamases are class A beta-lactamase found in Raoultella planticola. http://purl.obolibrary.org/obo/ARO_3005434 PLN beta-lactamase http://purl.obolibrary.org/obo/ARO_3000571 subclass B3 (metallo-) beta-lactamase PLN beta-lactamases are class B3 beta-lactamases found in Pedobacter lusitanus. http://purl.obolibrary.org/obo/ARO_3005435 PME beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase PME beta-lactamases are class A beta-lactamases found in Gammaproteobacteria. http://purl.obolibrary.org/obo/ARO_3005436 POM beta-lactamase http://purl.obolibrary.org/obo/ARO_3000571 subclass B3 (metallo-) beta-lactamase POM beta-lactamases are class B3 beta-lactamases found in Pseudomonas otitidis. http://purl.obolibrary.org/obo/ARO_3005437 PST beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase PST bea-lactamases are class B1 beta-lactamases found in Pseudomonas stutzeri. http://purl.obolibrary.org/obo/ARO_3005438 PSV beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase PSV beta-lactamases are class A beta-lactamases found in Pseudovibrio. http://purl.obolibrary.org/obo/ARO_3005439 RAHN beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase RAHN beta-lactamases are class A beta-lactamases found in Rahnella aquatilis. http://purl.obolibrary.org/obo/ARO_3005440 RSA2 beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase RSA2 beta-lactamases are class A beta-lactamases. http://purl.obolibrary.org/obo/ARO_3005441 RSD2 beta-lactamase http://purl.obolibrary.org/obo/ARO_3000075 class D beta-lactamase RSD2 beta-lactamases are class D beta-lactamases. http://purl.obolibrary.org/obo/ARO_3005442 RUB beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase RUB beta-lactamases are class A beta-lactamases found in Serratia rubidaea. http://purl.obolibrary.org/obo/ARO_3005443 SFC beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase SFC beta-lactamases are class A beta-lactamases found in Serratia fonticola. http://purl.obolibrary.org/obo/ARO_3005444 SFO beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase SFO beta-lactamases are class A beta-lactamases found in Gammaproteobacteria. http://purl.obolibrary.org/obo/ARO_3005445 SGM beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase SGM beta-lactamases are class A beta-lactamases found in members of the Sphingobium genus. http://purl.obolibrary.org/obo/ARO_3005446 SHN beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase SHN beta-lactamases are class B1 beta-lactamases found in Shewanella denitrificans. http://purl.obolibrary.org/obo/ARO_3005447 SPN79 beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase SPN beta-lactamases are class B1 beta-lactamases. http://purl.obolibrary.org/obo/ARO_3005448 SPR beta-lactamase http://purl.obolibrary.org/obo/ARO_3000004 class B (metallo-) beta-lactamase SPR beta-lactamases are class B beta-lactamases found in Serratia proteamaculans. http://purl.obolibrary.org/obo/ARO_3005449 SPS beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase SPS beta-lactamases are class B1 beta lactamases found in Sediminispirochaeta smaragdinae. http://purl.obolibrary.org/obo/ARO_3005450 SPU beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase SPU beta-lactamases are class A beta-lactamases found in Capnocytophaga sputigena. http://purl.obolibrary.org/obo/ARO_3005451 SST beta-lactamase http://purl.obolibrary.org/obo/ARO_3000076 class C beta-lactamase SST beta-lactamases are class C beta-lactamases found in Serratia marcescens. http://purl.obolibrary.org/obo/ARO_3005452 STA beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase STA beta-lactamases are class B1 beta-lactamases found in Stigmatella aurantiaca. http://purl.obolibrary.org/obo/ARO_3005453 TER beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase TER beta-lactamases are class A beta-lactamases found in Raoultella terrigena. http://purl.obolibrary.org/obo/ARO_3005454 TTU beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase TTU beta-lactamases are class B1 beta-lactamases found in Teredinibacter turnerae. http://purl.obolibrary.org/obo/ARO_3005455 VHH beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase VHH beta-lactamases are class A beta-lactamases found in Vibrio harveyi. http://purl.obolibrary.org/obo/ARO_3005456 VHW beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase VHW beta-lactamases are class A beta-lactamases found Vibrio harveyi. http://purl.obolibrary.org/obo/ARO_3005457 YEM beta-lactamase http://purl.obolibrary.org/obo/ARO_3000570 subclass B2 (metallo-) beta-lactamase YEM beta-lactamases are class B2 beta-lactamases found in Yersinia mollaretii. http://purl.obolibrary.org/obo/ARO_3005458 ZOG beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase ZOG beta-lactamases are class B1 beta-lactamases found in Zobellia galactanivorans. http://purl.obolibrary.org/obo/ARO_3005459 ADC beta-lactamase http://purl.obolibrary.org/obo/ARO_3000076 class C beta-lactamase ADC beta-lactamases, also known as AmpC beta-lactamases, are cephalosporinases with extended-spectrum resistance to cephalosporins and may or may not cause resistance to carbapenems. ADC beta-lactamases are found in Acinetobacter sp. and Oligella urethralis. http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity http://purl.obolibrary.org/obo/ARO_3005459 ADC beta-lactamase ADC beta-lactamases with undetermined carbapenemase activity. http://purl.obolibrary.org/obo/ARO_3005461 EBR-3 http://purl.obolibrary.org/obo/ARO_3004204 EBR beta-lactamase EBR-3 is a EBR beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005462 EBR-4 http://purl.obolibrary.org/obo/ARO_3004204 EBR beta-lactamase EBR-4 is a EBR beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005463 IMP-53 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-53 is a IMP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005464 IMP-54 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-54 is a IMP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005465 IMP-58 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-58 is a IMP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005466 IMP-59 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-59 is a IMP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005467 IMP-60 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-60 is a IMP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005468 IMP-61 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-61 is a IMP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005469 IMP-62 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-62 is a IMP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005470 IMP-63 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-63 is a IMP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005471 IMP-64 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-64 is a IMP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005472 IMP-65 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-65 is a IMP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005473 IMP-66 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-66 is a IMP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005474 IMP-67 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-67 is a IMP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005475 IMP-69 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-69 is a IMP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005476 IMP-70 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-70 is a IMP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005477 IMP-71 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-71 is a IMP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005478 IMP-73 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-73 is a IMP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005479 IMP-74 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-74 is a IMP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005480 IMP-75 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-75 is a IMP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005481 IMP-76 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-76 is a IMP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005482 IMP-77 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-77 is a IMP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005483 IMP-78 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-78 is a IMP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005484 IMP-79 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-79 is a IMP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005485 IMP-80 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-80 is a IMP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005486 IMP-81 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-81 is a IMP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005487 IMP-82 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-82 is a IMP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005488 IMP-83 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-83 is a IMP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005489 IMP-84 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-84 is a IMP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005490 IMP-85 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-85 is a IMP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005491 IMP-88 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-88 is a IMP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005492 IMP-89 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-89 is a IMP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005493 IND-16 http://purl.obolibrary.org/obo/ARO_3000060 IND beta-lactamase IND-16 is a IND beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005494 SIM-2 http://purl.obolibrary.org/obo/ARO_3004206 SIM beta-lactamase SIM-2 is a SIM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005495 VIM-47 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-47 is a VIM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005496 VIM-48 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-48 is a VIM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005497 VIM-49 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-49 is a VIM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005498 VIM-50 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-50 is a VIM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005499 VIM-51 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-51 is a VIM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005500 VIM-52 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-52 is a VIM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005501 VIM-53 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-53 is a VIM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005502 VIM-54 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-54 is a VIM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005503 VIM-55 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-55 is a VIM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005504 VIM-56 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-56 is a VIM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005505 VIM-57 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-57 is a VIM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005506 VIM-58 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-58 is a VIM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005507 VIM-59 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-59 is a VIM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005508 VIM-60 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-60 is a VIM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005509 VIM-61 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-61 is a VIM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005510 VIM-62 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-62 is a VIM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005511 VIM-63 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-63 is a VIM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005512 VIM-64 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-64 is a VIM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005513 VIM-65 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-65 is a VIM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005514 VIM-66 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-66 is a VIM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005515 VIM-67 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-67 is a VIM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005516 VIM-68 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-68 is a VIM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005517 VIM-69 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-69 is a VIM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005518 VIM-70 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-70 is a VIM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005519 VIM-71 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-71 is a VIM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005520 VIM-72 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-72 is a VIM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005521 VIM-73 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-73 is a VIM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005522 BlaB-1 http://purl.obolibrary.org/obo/ARO_3004201 BlaB beta-lactamase BlaB-1 is a BlaB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005523 BlaB-10 http://purl.obolibrary.org/obo/ARO_3004201 BlaB beta-lactamase BlaB-10 is a BlaB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005524 BlaB-11 http://purl.obolibrary.org/obo/ARO_3004201 BlaB beta-lactamase BlaB-11 is a BlaB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005525 BlaB-12 http://purl.obolibrary.org/obo/ARO_3004201 BlaB beta-lactamase BlaB-12 is a BlaB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005526 BlaB-13 http://purl.obolibrary.org/obo/ARO_3004201 BlaB beta-lactamase BlaB-13 is a BlaB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005527 BlaB-14 http://purl.obolibrary.org/obo/ARO_3004201 BlaB beta-lactamase BlaB-14 is a BlaB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005528 BlaB-15 http://purl.obolibrary.org/obo/ARO_3004201 BlaB beta-lactamase BlaB-15 is a BlaB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005529 BlaB-16 http://purl.obolibrary.org/obo/ARO_3004201 BlaB beta-lactamase BlaB-16 is a BlaB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005530 BlaB-17 http://purl.obolibrary.org/obo/ARO_3004201 BlaB beta-lactamase BlaB-17 is a BlaB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005531 BlaB-18 http://purl.obolibrary.org/obo/ARO_3004201 BlaB beta-lactamase BlaB-18 is a BlaB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005532 BlaB-19 http://purl.obolibrary.org/obo/ARO_3004201 BlaB beta-lactamase BlaB-19 is a BlaB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005533 BlaB-2 http://purl.obolibrary.org/obo/ARO_3004201 BlaB beta-lactamase BlaB-2 is a BlaB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005534 BlaB-20 http://purl.obolibrary.org/obo/ARO_3004201 BlaB beta-lactamase BlaB-20 is a BlaB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005535 BlaB-22 http://purl.obolibrary.org/obo/ARO_3004201 BlaB beta-lactamase BlaB-22 is a BlaB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005536 BlaB-23 http://purl.obolibrary.org/obo/ARO_3004201 BlaB beta-lactamase BlaB-23 is a BlaB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005537 BlaB-24 http://purl.obolibrary.org/obo/ARO_3004201 BlaB beta-lactamase BlaB-24 is a BlaB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005538 BlaB-25 http://purl.obolibrary.org/obo/ARO_3004201 BlaB beta-lactamase BlaB-25 is a BlaB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005539 BlaB-26 http://purl.obolibrary.org/obo/ARO_3004201 BlaB beta-lactamase BlaB-26 is a BlaB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005540 BlaB-27 http://purl.obolibrary.org/obo/ARO_3004201 BlaB beta-lactamase BlaB-27 is a BlaB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005541 BlaB-28 http://purl.obolibrary.org/obo/ARO_3004201 BlaB beta-lactamase BlaB-28 is a BlaB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005542 BlaB-29 http://purl.obolibrary.org/obo/ARO_3004201 BlaB beta-lactamase BlaB-29 is a BlaB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005543 BlaB-3 http://purl.obolibrary.org/obo/ARO_3004201 BlaB beta-lactamase BlaB-3 is a BlaB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005544 BlaB-30 http://purl.obolibrary.org/obo/ARO_3004201 BlaB beta-lactamase BlaB-30 is a BlaB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005545 BlaB-31 http://purl.obolibrary.org/obo/ARO_3004201 BlaB beta-lactamase BlaB-31 is a BlaB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005546 BlaB-32 http://purl.obolibrary.org/obo/ARO_3004201 BlaB beta-lactamase BlaB-32 is a BlaB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005547 BlaB-33 http://purl.obolibrary.org/obo/ARO_3004201 BlaB beta-lactamase BlaB-33 is a BlaB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005548 BlaB-34 http://purl.obolibrary.org/obo/ARO_3004201 BlaB beta-lactamase BlaB-34 is a BlaB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005549 BlaB-35 http://purl.obolibrary.org/obo/ARO_3004201 BlaB beta-lactamase BlaB-35 is a BlaB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005550 BlaB-36 http://purl.obolibrary.org/obo/ARO_3004201 BlaB beta-lactamase BlaB-36 is a BlaB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005551 BlaB-38 http://purl.obolibrary.org/obo/ARO_3004201 BlaB beta-lactamase BlaB-38 is a BlaB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005552 BlaB-39 http://purl.obolibrary.org/obo/ARO_3004201 BlaB beta-lactamase BlaB-39 is a BlaB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005553 BlaB-5 http://purl.obolibrary.org/obo/ARO_3004201 BlaB beta-lactamase BlaB-5 is a BlaB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005554 BlaB-6 http://purl.obolibrary.org/obo/ARO_3004201 BlaB beta-lactamase BlaB-6 is a BlaB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005555 BlaB-7 http://purl.obolibrary.org/obo/ARO_3004201 BlaB beta-lactamase BlaB-7 is a BlaB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005556 BlaB-8 http://purl.obolibrary.org/obo/ARO_3004201 BlaB beta-lactamase BlaB-8 is a BlaB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005557 BlaB-9 http://purl.obolibrary.org/obo/ARO_3004201 BlaB beta-lactamase BlaB-9 is a BlaB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005558 BUT-2 http://purl.obolibrary.org/obo/ARO_3004293 BUT beta-lactamase BUT-2 is a BUT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005559 CARB-11 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-11 is a CARB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005560 CARB-24 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-24 is a CARB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005561 CARB-25 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-25 is a CARB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005562 CARB-26 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-26 is a CARB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005563 CARB-27 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-27 is a CARB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005564 CARB-28 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-28 is a CARB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005565 CARB-29 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-29 is a CARB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005566 CARB-30 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-30 is a CARB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005567 CARB-31 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-31 is a CARB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005568 CARB-32 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-32 is a CARB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005569 CARB-33 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-33 is a CARB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005570 CARB-34 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-34 is a CARB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005571 CARB-35 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-35 is a CARB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005572 CARB-36 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-36 is a CARB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005573 CARB-38 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-38 is a CARB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005574 CARB-40 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-40 is a CARB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005575 CARB-41 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-41 is a CARB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005576 CARB-42 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-42 is a CARB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005577 CARB-43 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-43 is a CARB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005578 CARB-44 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-44 is a CARB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005579 CARB-45 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-45 is a CARB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005580 CARB-46 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-46 is a CARB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005581 CARB-47 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-47 is a CARB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005582 CARB-48 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-48 is a CARB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005583 CARB-49 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-49 is a CARB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005584 CARB-50 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-50 is a CARB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005585 CARB-51 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-51 is a CARB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005586 CARB-52 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-52 is a CARB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005587 CARB-53 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-53 is a CARB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005588 CARB-54 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-54 is a CARB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005589 CARB-55 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-55 is a CARB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005590 CTX-M-167 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-167 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005591 CTX-M-168 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-168 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005592 CTX-M-169 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-169 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005593 CTX-M-170 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-170 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005594 CTX-M-171 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-171 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005595 CTX-M-172 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-172 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005596 CTX-M-173 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-173 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005597 CTX-M-174 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-174 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005598 CTX-M-175 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-175 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005599 CTX-M-176 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-176 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005600 CTX-M-177 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-177 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005601 CTX-M-178 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-178 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005602 CTX-M-179 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-179 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005603 CTX-M-180 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-180 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005604 CTX-M-181 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-181 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005605 CTX-M-182 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-182 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005606 CTX-M-183 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-183 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005607 CTX-M-184 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-184 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005608 CTX-M-185 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-185 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005609 CTX-M-186 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-186 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005610 CTX-M-187 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-187 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005611 CTX-M-188 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-188 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005612 CTX-M-189 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-189 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005613 CTX-M-190 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-190 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005614 CTX-M-191 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-191 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005615 CTX-M-192 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-192 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005616 CTX-M-193 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-193 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005617 CTX-M-194 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-194 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005618 CTX-M-195 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-195 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005619 CTX-M-196 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-196 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005620 CTX-M-197 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-197 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005621 CTX-M-198 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-198 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005622 CTX-M-199 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-199 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005623 CTX-M-200 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-200 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005624 CTX-M-201 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-201 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005625 CTX-M-202 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-202 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005626 CTX-M-203 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-203 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005627 CTX-M-204 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-204 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005628 CTX-M-205 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-205 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005629 CTX-M-206 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-206 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005630 CTX-M-207 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-207 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005631 CTX-M-208 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-208 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005632 CTX-M-209 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-209 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005633 CTX-M-210 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-210 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005634 CTX-M-211 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-211 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005635 CTX-M-212 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-212 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005636 CTX-M-213 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-213 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005637 CTX-M-214 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-214 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005638 CTX-M-215 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-215 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005639 CTX-M-216 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-216 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005640 CTX-M-217 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-217 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005641 CTX-M-218 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-218 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005642 CTX-M-219 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-219 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005643 CTX-M-220 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-220 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005644 CTX-M-221 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-221 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005645 CTX-M-222 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-222 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005646 CTX-M-223 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-223 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005647 CTX-M-224 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-224 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005648 CTX-M-225 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-225 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005649 CTX-M-226 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-226 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005650 CTX-M-227 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-227 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005651 CTX-M-228 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-228 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005652 CTX-M-229 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-229 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005653 CTX-M-230 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-230 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005654 CTX-M-231 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-231 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005655 CTX-M-232 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-232 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005656 CTX-M-233 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-233 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005657 CTX-M-234 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-234 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005658 CTX-M-235 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-235 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005659 CTX-M-236 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-236 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005660 CTX-M-237 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-237 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005661 CTX-M-238 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-238 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005662 CTX-M-239 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-239 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005663 CTX-M-240 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-240 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005664 CTX-M-241 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-241 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005665 CTX-M-242 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-242 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005666 CTX-M-244 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-244 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005667 CTX-M-97 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-97 is a CTX-M beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005668 GOB-19 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-19 is a GOB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005669 GOB-20 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-20 is a GOB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005670 GOB-21 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-21 is a GOB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005671 GOB-22 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-22 is a GOB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005672 GOB-23 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-23 is a GOB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005673 GOB-24 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-24 is a GOB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005674 GOB-25 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-25 is a GOB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005675 GOB-26 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-26 is a GOB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005676 GOB-27 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-27 is a GOB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005677 GOB-28 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-28 is a GOB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005678 GOB-29 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-29 is a GOB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005679 GOB-30 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-30 is a GOB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005680 GOB-31 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-31 is a GOB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005681 GOB-32 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-32 is a GOB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005682 GOB-33 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-33 is a GOB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005683 GOB-34 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-34 is a GOB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005684 GOB-35 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-35 is a GOB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005685 GOB-36 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-36 is a GOB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005686 GOB-37 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-37 is a GOB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005687 GOB-38 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-38 is a GOB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005688 GOB-39 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-39 is a GOB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005689 GOB-40 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-40 is a GOB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005690 GOB-41 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-41 is a GOB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005691 GOB-42 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-42 is a GOB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005692 GOB-43 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-43 is a GOB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005693 GOB-44 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-44 is a GOB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005694 GOB-45 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-45 is a GOB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005695 GOB-46 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-46 is a GOB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005696 GOB-48 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-48 is a GOB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005697 GOB-49 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-49 is a GOB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005698 GOB-50 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-50 is a GOB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005699 GOB-51 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-51 is a GOB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005700 NDM-30 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase NDM-30 is a NDM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005701 NDM-31 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase NDM-31 is a NDM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005702 OXA-114b http://purl.obolibrary.org/obo/ARO_3007698 OXA-114-like beta-lactamase OXA-114b is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005703 OXA-114c http://purl.obolibrary.org/obo/ARO_3007698 OXA-114-like beta-lactamase OXA-114c is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005704 OXA-114d http://purl.obolibrary.org/obo/ARO_3007698 OXA-114-like beta-lactamase OXA-114d is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005705 OXA-114e http://purl.obolibrary.org/obo/ARO_3007698 OXA-114-like beta-lactamase OXA-114e is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005706 OXA-114f http://purl.obolibrary.org/obo/ARO_3007698 OXA-114-like beta-lactamase OXA-114f is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005707 OXA-114g http://purl.obolibrary.org/obo/ARO_3007698 OXA-114-like beta-lactamase OXA-114g is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005708 OXA-114h http://purl.obolibrary.org/obo/ARO_3007698 OXA-114-like beta-lactamase OXA-114h is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005709 OXA-114i http://purl.obolibrary.org/obo/ARO_3007698 OXA-114-like beta-lactamase OXA-114i is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005710 OXA-114j http://purl.obolibrary.org/obo/ARO_3007698 OXA-114-like beta-lactamase OXA-114j is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005711 OXA-114k http://purl.obolibrary.org/obo/ARO_3007698 OXA-114-like beta-lactamase OXA-114k is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005712 OXA-114l http://purl.obolibrary.org/obo/ARO_3007698 OXA-114-like beta-lactamase OXA-114l is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005713 OXA-114m http://purl.obolibrary.org/obo/ARO_3007698 OXA-114-like beta-lactamase OXA-114m is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005714 OXA-114n http://purl.obolibrary.org/obo/ARO_3007698 OXA-114-like beta-lactamase OXA-114n is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005715 OXA-114p http://purl.obolibrary.org/obo/ARO_3007698 OXA-114-like beta-lactamase OXA-114p is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005716 OXA-114q http://purl.obolibrary.org/obo/ARO_3007698 OXA-114-like beta-lactamase OXA-114q is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005717 OXA-114r http://purl.obolibrary.org/obo/ARO_3007698 OXA-114-like beta-lactamase OXA-114r is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005718 OXA-114s http://purl.obolibrary.org/obo/ARO_3007698 OXA-114-like beta-lactamase OXA-114s is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005719 OXA-114t http://purl.obolibrary.org/obo/ARO_3007698 OXA-114-like beta-lactamase OXA-114t is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005720 OXA-114u http://purl.obolibrary.org/obo/ARO_3007698 OXA-114-like beta-lactamase OXA-114u is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005721 OXA-114v http://purl.obolibrary.org/obo/ARO_3007698 OXA-114-like beta-lactamase OXA-114v is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005722 OXA-114w http://purl.obolibrary.org/obo/ARO_3007698 OXA-114-like beta-lactamase OXA-114w is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005723 OXA-114x http://purl.obolibrary.org/obo/ARO_3007698 OXA-114-like beta-lactamase OXA-114x is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005724 OXA-489 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-489 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005725 OXA-491 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-491 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005726 OXA-493 http://purl.obolibrary.org/obo/ARO_3007722 OXA-493-like beta-lactamase OXA-493 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005727 OXA-494 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-494 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005728 OXA-497 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-497 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005729 OXA-498 http://purl.obolibrary.org/obo/ARO_3007705 OXA-211-like beta-lactamase OXA-498 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005730 OXA-500 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-500 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005731 OXA-501 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-501 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005732 OXA-502 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-502 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005733 OXA-503 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-503 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005734 OXA-504 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-504 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005735 OXA-505 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-505 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005736 OXA-506 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-506 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005737 OXA-507 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-507 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005738 OXA-508 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-508 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005739 OXA-509 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-509 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005740 OXA-510 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-510 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005741 OXA-511 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-511 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005742 OXA-512 http://purl.obolibrary.org/obo/ARO_3007728 OXA-58-like beta-lactamase OXA-512 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005743 OXA-513 http://purl.obolibrary.org/obo/ARO_3007716 OXA-364-like beta-lactamase OXA-513 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005744 OXA-514 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-514 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005745 OXA-515 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-515 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005746 OXA-516 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-516 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005747 OXA-517 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-517 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005748 OXA-518 http://purl.obolibrary.org/obo/ARO_3007722 OXA-493-like beta-lactamase OXA-518 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005749 OXA-519 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-519 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005750 OXA-520 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-520 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005751 OXA-521 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-521 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005752 OXA-522 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-522 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005753 OXA-523 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-523 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005754 OXA-524 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-524 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005755 OXA-525 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-525 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005756 OXA-526 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-526 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005757 OXA-527 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-527 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005758 OXA-528 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-528 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005759 OXA-529 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-529 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005760 OXA-530 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-530 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005761 OXA-531 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-531 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005762 OXA-532 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-532 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005763 OXA-533 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-533 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005764 OXA-534 http://purl.obolibrary.org/obo/ARO_3007696 OXA-1-like beta-lactamase OXA-534 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005765 OXA-536 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-536 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005766 OXA-537 http://purl.obolibrary.org/obo/ARO_3007700 OXA-134-like beta-lactamase OXA-537 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005767 OXA-538 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-538 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005768 OXA-542 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-542 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005769 OXA-545 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-545 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005770 OXA-546 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-546 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005771 OXA-547 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-547 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005772 OXA-548 http://purl.obolibrary.org/obo/ARO_3007726 OXA-548-like beta-lactamase OXA-548 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005773 OXA-549 http://purl.obolibrary.org/obo/ARO_3007726 OXA-548-like beta-lactamase OXA-549 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005774 OXA-550 http://purl.obolibrary.org/obo/ARO_3007726 OXA-548-like beta-lactamase OXA-550 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005775 OXA-551 http://purl.obolibrary.org/obo/ARO_3007726 OXA-548-like beta-lactamase OXA-551 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005776 OXA-552 http://purl.obolibrary.org/obo/ARO_3007726 OXA-548-like beta-lactamase OXA-552 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005777 OXA-553 http://purl.obolibrary.org/obo/ARO_3007726 OXA-548-like beta-lactamase OXA-553 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005778 OXA-554 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-554 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005779 OXA-555 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-555 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005780 OXA-556 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-556 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005781 OXA-557 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-557 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005782 OXA-558 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-558 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005783 OXA-559 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-559 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005784 OXA-560 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-560 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005785 OXA-561 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-561 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005786 OXA-562 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-562 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005787 OXA-563 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-563 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005788 OXA-564 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-564 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005789 OXA-565 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-565 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005790 OXA-566 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-566 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005791 OXA-567 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-567 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005792 OXA-568 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-568 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005793 OXA-569 http://purl.obolibrary.org/obo/ARO_3007708 OXA-22-like beta-lactamase OXA-569 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005794 OXA-572 http://purl.obolibrary.org/obo/ARO_3007708 OXA-22-like beta-lactamase OXA-572 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005795 OXA-574 http://purl.obolibrary.org/obo/ARO_3007708 OXA-22-like beta-lactamase OXA-574 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005796 OXA-575 http://purl.obolibrary.org/obo/ARO_3007707 OXA-214-like beta-lactamase OXA-575 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005797 OXA-576 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-576 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005798 OXA-577 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-577 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005799 OXA-578 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-578 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005800 OXA-579 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-579 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005801 OXA-580 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-580 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005802 OXA-581 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-581 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005803 OXA-582 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-582 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005804 OXA-583 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-583 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005805 OXA-584 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-584 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005806 OXA-585 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-585 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005807 OXA-586 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-586 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005808 OXA-587 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-587 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005809 OXA-588 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-588 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005810 OXA-589 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-589 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005811 OXA-590 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-590 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005812 OXA-591 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-591 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005813 OXA-592 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-592 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005814 OXA-593 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-593 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005815 OXA-594 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-594 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005816 OXA-595 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-595 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005817 OXA-596 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-596 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005818 OXA-597 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-597 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005819 OXA-598 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-598 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005820 OXA-599 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-599 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005821 OXA-600 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-600 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005822 OXA-601 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-601 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005823 OXA-602 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-602 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005824 OXA-603 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-603 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005825 OXA-604 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-604 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005826 OXA-605 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-605 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005827 OXA-606 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-606 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005828 OXA-607 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-607 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005829 OXA-608 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-608 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005830 OXA-609 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-609 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005831 OXA-610 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-610 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005832 OXA-611 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-611 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005833 OXA-612 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-612 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005834 OXA-613 http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase OXA-613 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005835 OXA-614 http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase OXA-614 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005836 OXA-615 http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase OXA-615 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005837 OXA-616 http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase OXA-616 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005838 OXA-617 http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase OXA-617 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005839 OXA-618 http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase OXA-618 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005840 OXA-619 http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase OXA-619 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005841 OXA-620 http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase OXA-620 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005842 OXA-621 http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase OXA-621 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005843 OXA-622 http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase OXA-622 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005844 OXA-623 http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase OXA-623 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005845 OXA-624 http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase OXA-624 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005846 OXA-625 http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase OXA-625 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005847 OXA-626 http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase OXA-626 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005848 OXA-627 http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase OXA-627 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005849 OXA-628 http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase OXA-628 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005850 OXA-629 http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase OXA-629 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005851 OXA-630 http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase OXA-630 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005852 OXA-631 http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase OXA-631 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005853 OXA-632 http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase OXA-632 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005854 OXA-633 http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase OXA-633 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005855 OXA-634 http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase OXA-634 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005856 OXA-635 http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase OXA-635 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005857 OXA-636 http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase OXA-636 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005858 OXA-637 http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase OXA-637 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005859 OXA-638 http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase OXA-638 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005860 OXA-639 http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase OXA-639 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005861 OXA-640 http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase OXA-640 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005862 OXA-642 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-642 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005863 OXA-643 http://purl.obolibrary.org/obo/ARO_3007705 OXA-211-like beta-lactamase OXA-643 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005864 OXA-644 http://purl.obolibrary.org/obo/ARO_3007705 OXA-211-like beta-lactamase OXA-644 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005865 OXA-645 http://purl.obolibrary.org/obo/ARO_3007705 OXA-211-like beta-lactamase OXA-645 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005866 OXA-650 http://purl.obolibrary.org/obo/ARO_3007705 OXA-211-like beta-lactamase OXA-650 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005867 OXA-651 http://purl.obolibrary.org/obo/ARO_3007705 OXA-211-like beta-lactamase OXA-651 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005868 OXA-652 http://purl.obolibrary.org/obo/ARO_3007705 OXA-211-like beta-lactamase OXA-652 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005869 OXA-654 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-654 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005870 OXA-655 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-655 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005871 OXA-656 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-656 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005872 OXA-657 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-657 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005873 OXA-658 http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase OXA-658 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005874 OXA-659 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-659 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005875 OXA-660 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-660 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005876 OXA-661 http://purl.obolibrary.org/obo/ARO_3007712 OXA-266-like beta-lactamase OXA-661 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005877 OXA-662 http://purl.obolibrary.org/obo/ARO_3007705 OXA-211-like beta-lactamase OXA-662 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005878 OXA-666 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-666 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005879 OXA-667 http://purl.obolibrary.org/obo/ARO_3007713 OXA-274-like beta-lactamase OXA-667 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005880 OXA-669 http://purl.obolibrary.org/obo/ARO_3007713 OXA-274-like beta-lactamase OXA-669 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005881 OXA-670 http://purl.obolibrary.org/obo/ARO_3007714 OXA-286-like beta-lactamase OXA-670 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005882 OXA-674 http://purl.obolibrary.org/obo/ARO_3007714 OXA-286-like beta-lactamase OXA-674 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005883 OXA-675 http://purl.obolibrary.org/obo/ARO_3007696 OXA-1-like beta-lactamase OXA-675 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005884 OXA-676 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-676 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005885 OXA-677 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-677 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005886 OXA-678 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-678 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005887 OXA-679 http://purl.obolibrary.org/obo/ARO_3007733 OXA-679-like beta-lactamase OXA-679 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005888 OXA-680 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-680 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005889 OXA-682 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-682 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005890 OXA-683 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-683 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005891 OXA-684 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-684 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005892 OXA-685 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-685 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005893 OXA-686 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-686 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005894 OXA-687 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-687 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005895 OXA-688 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-688 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005896 OXA-689 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-689 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005897 OXA-690 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-690 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005898 OXA-691 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-691 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005899 OXA-692 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-692 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005900 OXA-693 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-693 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005901 OXA-694 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-694 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005902 OXA-695 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-695 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005903 OXA-696 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-696 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005904 OXA-697 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-697 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005905 OXA-698 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-698 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005906 OXA-699 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-699 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005907 OXA-700 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-700 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005908 OXA-701 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-701 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005909 OXA-702 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-702 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005910 OXA-703 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-703 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005911 OXA-704 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-704 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005912 OXA-705 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-705 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005913 OXA-706 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-706 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005914 OXA-707 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-707 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005915 OXA-708 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-708 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005916 OXA-709 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-709 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005917 OXA-710 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-710 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005918 OXA-711 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-711 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005919 OXA-712 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-712 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005920 OXA-713 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-713 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005921 OXA-714 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-714 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005922 OXA-715 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-715 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005923 OXA-716 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-716 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005924 OXA-717 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-717 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005925 OXA-718 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-718 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005926 OXA-719 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-719 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005927 OXA-720 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-720 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005928 OXA-721 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-721 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005929 OXA-722 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-722 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005930 OXA-723 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-723 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005931 OXA-726 http://purl.obolibrary.org/obo/ARO_3007699 OXA-12-like beta-lactamase OXA-726 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005932 OXA-727 http://purl.obolibrary.org/obo/ARO_3007734 OXA-727-like beta-lactamase OXA-727 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005933 OXA-728 http://purl.obolibrary.org/obo/ARO_3007734 OXA-727-like beta-lactamase OXA-728 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005934 OXA-729 http://purl.obolibrary.org/obo/ARO_3007727 OXA-55-like beta-lactamase OXA-729 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005935 OXA-730 http://purl.obolibrary.org/obo/ARO_3007733 OXA-679-like beta-lactamase OXA-730 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005936 OXA-731 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-731 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005937 OXA-732 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-732 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005938 OXA-733 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-733 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005939 OXA-734 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-734 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005940 OXA-735 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-735 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005941 OXA-736 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-736 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005942 OXA-738 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-738 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005943 OXA-739 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-739 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005944 OXA-740 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-740 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005945 OXA-741 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-741 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005946 OXA-742 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-742 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005947 OXA-743 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-743 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005948 OXA-744 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-744 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005949 OXA-745 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-745 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005950 OXA-746 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-746 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005951 OXA-747 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-747 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005952 OXA-748 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-748 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005953 OXA-749 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-749 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005954 OXA-750 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-750 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005955 OXA-751 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-751 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005956 OXA-752 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-752 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005957 OXA-753 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-753 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005958 OXA-754 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-754 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005959 OXA-755 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-755 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005960 OXA-756 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-756 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005961 OXA-757 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-757 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005962 OXA-758 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-758 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005963 OXA-759 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-759 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005964 OXA-760 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-760 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005965 OXA-761 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-761 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005966 OXA-762 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-762 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005967 OXA-763 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-763 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005968 OXA-764 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-764 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005969 OXA-765 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-765 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005970 OXA-766 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-766 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005971 OXA-767 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-767 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005972 OXA-768 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-768 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005973 OXA-769 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-769 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005974 OXA-770 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-770 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005975 OXA-771 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-771 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005976 OXA-772 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-772 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005977 OXA-773 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-773 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005978 OXA-774 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-774 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005979 OXA-775 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-775 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005980 OXA-776 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-776 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005981 OXA-777 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-777 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005982 OXA-778 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-778 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005983 OXA-780 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-780 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005984 OXA-781 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-781 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005985 OXA-782 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-782 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005986 OXA-783 http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase OXA-783 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005987 OXA-784 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-784 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005988 OXA-785 http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase OXA-785 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005989 OXA-786 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-786 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005990 OXA-787 http://purl.obolibrary.org/obo/ARO_3007716 OXA-364-like beta-lactamase OXA-787 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005991 OXA-788 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-788 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005992 OXA-789 http://purl.obolibrary.org/obo/ARO_3007716 OXA-364-like beta-lactamase OXA-789 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005993 OXA-793 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-793 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005994 OXA-794 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-794 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005995 OXA-795 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-795 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005996 OXA-796 http://purl.obolibrary.org/obo/ARO_3007696 OXA-1-like beta-lactamase OXA-796 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005997 OXA-797 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-797 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005998 OXA-798 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-798 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005999 OXA-799 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-799 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006000 OXA-800 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-800 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006001 OXA-801 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-801 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006002 OXA-802 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-802 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006003 OXA-803 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-803 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006004 OXA-804 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-804 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006005 OXA-805 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-805 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006006 OXA-806 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-806 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006007 OXA-807 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-807 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006008 OXA-808 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-808 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006009 OXA-809 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-809 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006010 OXA-810 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-810 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006011 OXA-811 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-811 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006012 OXA-813 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-813 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006013 OXA-814 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-814 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006014 OXA-815 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-815 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006015 OXA-816 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-816 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006016 OXA-817 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-817 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006017 OXA-819 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-819 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006018 OXA-820 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-820 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006019 OXA-821 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-821 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006020 OXA-822 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-822 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006021 OXA-823 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-823 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006022 OXA-824 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-824 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006023 OXA-826 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-826 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006024 OXA-827 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-827 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006025 OXA-828 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-828 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006026 OXA-829 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-829 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006027 OXA-830 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-830 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006028 OXA-831 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-831 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006029 OXA-832 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-832 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006030 OXA-833 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-833 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006031 OXA-834 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-834 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006032 OXA-836 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-836 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006033 OXA-839 http://purl.obolibrary.org/obo/ARO_3007698 OXA-114-like beta-lactamase OXA-839 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006034 OXA-840 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-840 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006035 OXA-841 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-841 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006036 OXA-842 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-842 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006037 OXA-843 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-843 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006038 OXA-844 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-844 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006039 OXA-845 http://purl.obolibrary.org/obo/ARO_3007707 OXA-214-like beta-lactamase OXA-845 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006040 OXA-847 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-847 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006041 OXA-848 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-848 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006042 OXA-849 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-849 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006043 OXA-851 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-851 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006044 OXA-852 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-852 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006045 OXA-853 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-853 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006046 OXA-854 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-854 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006047 OXA-855 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-855 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006048 OXA-856 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-856 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006049 OXA-857 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-857 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006050 OXA-858 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-858 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006051 OXA-859 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-859 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006052 OXA-860 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-860 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006053 OXA-861 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-861 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006054 OXA-862 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-862 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006055 OXA-863 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-863 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006056 OXA-864 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-864 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006057 OXA-865 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-865 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006058 OXA-866 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-866 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006059 OXA-867 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-867 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006060 OXA-868 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-868 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006061 OXA-869 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-869 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006062 OXA-870 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-870 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006063 OXA-871 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-871 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006064 OXA-872 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-872 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006065 OXA-873 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-873 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006066 OXA-874 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-874 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006067 OXA-875 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-875 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006068 OXA-876 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-876 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006069 OXA-877 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-877 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006070 OXA-878 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-878 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006071 OXA-879 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-879 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006072 OXA-880 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-880 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006073 OXA-881 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-881 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006074 OXA-882 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-882 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006075 OXA-883 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-883 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006076 OXA-884 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-884 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006077 OXA-885 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-885 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006078 OXA-886 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-886 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006079 OXA-887 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-887 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006080 OXA-888 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-888 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006081 OXA-889 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-889 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006082 OXA-890 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-890 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006083 OXA-891 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-891 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006084 OXA-892 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-892 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006085 OXA-893 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-893 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006086 OXA-894 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-894 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006087 OXA-896 http://purl.obolibrary.org/obo/ARO_3007735 OXA-9-like beta-lactamase OXA-896 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006088 OXA-900 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-900 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006089 OXA-901 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-901 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006090 OXA-902 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-902 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006091 OXA-903 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-903 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006092 OXA-904 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-904 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006093 OXA-905 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-905 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006094 OXA-907 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-907 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006095 OXA-908 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-908 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006096 OXA-909 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-909 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006097 OXA-910 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-910 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006098 OXA-911 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-911 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006099 OXA-912 http://purl.obolibrary.org/obo/ARO_3007699 OXA-12-like beta-lactamase OXA-912 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006100 OXA-913 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-913 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006101 OXA-914 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-914 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006102 OXA-916 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-916 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006103 OXA-917 http://purl.obolibrary.org/obo/ARO_3007719 OXA-427-like beta-lactamase OXA-917 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006104 OXA-918 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-918 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006105 OXA-919 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-919 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006106 OXA-920 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-920 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006107 OXA-921 http://purl.obolibrary.org/obo/ARO_3007696 OXA-1-like beta-lactamase OXA-921 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006108 OXA-922 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-922 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006109 OXA-923 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-923 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006110 OXA-924 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-924 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006111 OXA-925 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-925 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006112 OXA-927 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-927 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006113 OXA-928 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-928 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006114 OXA-929 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-929 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006115 OXA-932 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-932 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006116 OXA-935 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-935 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006117 OXA-937 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-937 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006118 OXA-938 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-938 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006119 OXA-939 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-939 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006120 OXA-940 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-940 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006121 OXA-941 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-941 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006122 OXA-942 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-942 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006123 OXA-943 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-943 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006124 OXA-945 http://purl.obolibrary.org/obo/ARO_3007701 OXA-143-like beta-lactamase OXA-945 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006125 OXA-946 http://purl.obolibrary.org/obo/ARO_3007733 OXA-679-like beta-lactamase OXA-946 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006126 OXA-947 http://purl.obolibrary.org/obo/ARO_3007733 OXA-679-like beta-lactamase OXA-947 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006127 OXA-948 http://purl.obolibrary.org/obo/ARO_3007733 OXA-679-like beta-lactamase OXA-948 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006128 OXA-949 http://purl.obolibrary.org/obo/ARO_3007733 OXA-679-like beta-lactamase OXA-949 is a OXA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006129 OXY-2-14 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase OXY-2-14 is a OXY beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006130 OXY-2-15 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase OXY-2-15 is a OXY beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006131 PER-10 http://purl.obolibrary.org/obo/ARO_3000056 PER beta-lactamase PER-10 is a PER beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006132 PER-11 http://purl.obolibrary.org/obo/ARO_3000056 PER beta-lactamase PER-11 is a PER beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006133 PER-12 http://purl.obolibrary.org/obo/ARO_3000056 PER beta-lactamase PER-12 is a PER beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006134 PER-13 http://purl.obolibrary.org/obo/ARO_3000056 PER beta-lactamase PER-13 is a PER beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006135 PER-14 http://purl.obolibrary.org/obo/ARO_3000056 PER beta-lactamase PER-14 is a PER beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006136 PER-15 http://purl.obolibrary.org/obo/ARO_3000056 PER beta-lactamase PER-15 is a PER beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006137 PER-16 http://purl.obolibrary.org/obo/ARO_3000056 PER beta-lactamase PER-16 is a PER beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006138 PER-9 http://purl.obolibrary.org/obo/ARO_3000056 PER beta-lactamase PER-9 is a PER beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006139 TEM-98 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-98 is a TEM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006140 TEM-99 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-99 is a TEM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006141 OKP-A-17 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-A-17 is a OKP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006142 OKP-B-16 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-B-16 is a OKP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006143 OKP-B-21 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-B-21 is a OKP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006144 OKP-B-22 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-B-22 is a OKP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006145 OKP-B-23 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-B-23 is a OKP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006146 OKP-B-24 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-B-24 is a OKP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006147 OKP-B-34 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-B-34 is a OKP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006148 OKP-B-36 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-B-36 is a OKP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006149 OKP-B-40 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-B-40 is a OKP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006150 OKP-B-41 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-B-41 is a OKP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006151 OKP-B-45 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-B-45 is a OKP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006152 OKP-C-1 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-C-1 is a OKP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006153 OKP-D-1 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-D-1 is a OKP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006154 BEL-4 http://purl.obolibrary.org/obo/ARO_3002384 BEL beta-lactamase BEL-4 is a BEL beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006155 CME-2 http://purl.obolibrary.org/obo/ARO_3004774 CME beta-lactamase CME-2 is a CME beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006156 GES-27 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-27 is a GES beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006157 GES-28 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-28 is a GES beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006158 GES-29 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-29 is a GES beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006159 GES-30 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-30 is a GES beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006160 GES-31 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-31 is a GES beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006161 GES-32 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-32 is a GES beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006162 GES-33 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-33 is a GES beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006163 GES-34 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-34 is a GES beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006164 GES-35 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-35 is a GES beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006165 GES-36 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-36 is a GES beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006166 GES-37 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-37 is a GES beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006167 GES-38 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-38 is a GES beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006168 GES-39 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-39 is a GES beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006169 GES-40 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-40 is a GES beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006170 GES-41 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-41 is a GES beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006171 GES-42 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-42 is a GES beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006172 GES-43 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-43 is a GES beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006173 GES-44 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-44 is a GES beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006174 GES-45 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-45 is a GES beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006175 GES-46 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-46 is a GES beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006176 IMI-12 http://purl.obolibrary.org/obo/ARO_3000018 IMI beta-lactamase IMI-12 is a IMI beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006177 IMI-13 http://purl.obolibrary.org/obo/ARO_3000018 IMI beta-lactamase IMI-13 is a IMI beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006178 IMI-14 http://purl.obolibrary.org/obo/ARO_3000018 IMI beta-lactamase IMI-14 is a IMI beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006179 IMI-15 http://purl.obolibrary.org/obo/ARO_3000018 IMI beta-lactamase IMI-15 is a IMI beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006180 IMI-16 http://purl.obolibrary.org/obo/ARO_3000018 IMI beta-lactamase IMI-16 is a IMI beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006181 IMI-17 http://purl.obolibrary.org/obo/ARO_3000018 IMI beta-lactamase IMI-17 is a IMI beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006182 IMI-18 http://purl.obolibrary.org/obo/ARO_3000018 IMI beta-lactamase IMI-18 is a IMI beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006183 IMI-19 http://purl.obolibrary.org/obo/ARO_3000018 IMI beta-lactamase IMI-19 is a IMI beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006184 IMI-20 http://purl.obolibrary.org/obo/ARO_3000018 IMI beta-lactamase IMI-20 is a IMI beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006185 IMI-21 http://purl.obolibrary.org/obo/ARO_3000018 IMI beta-lactamase IMI-21 is a IMI beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006186 KPC-44 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-44 is a KPC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006187 KPC-58 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-58 is a KPC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006188 KPC-59 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-59 is a KPC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006189 KPC-60 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-60 is a KPC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006190 KPC-61 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-61 is a KPC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006191 KPC-62 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-62 is a KPC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006192 KPC-63 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-63 is a KPC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006193 KPC-64 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-64 is a KPC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006194 KPC-65 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-65 is a KPC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006195 KPC-66 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-66 is a KPC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006196 KPC-71 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-71 is a KPC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006197 KPC-72 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-72 is a KPC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006198 KPC-73 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-73 is a KPC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006199 KPC-74 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-74 is a KPC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006200 KPC-75 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-75 is a KPC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006201 KPC-76 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-76 is a KPC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006202 KPC-77 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-77 is a KPC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006203 KPC-78 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-78 is a KPC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006204 KPC-79 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-79 is a KPC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006205 KPC-80 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-80 is a KPC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006206 KPC-81 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-81 is a KPC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006207 KPC-82 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-82 is a KPC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006208 VEB-11 http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase VEB-11 is a VEB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006209 VEB-12 http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase VEB-12 is a VEB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006210 VEB-13 http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase VEB-13 is a VEB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006211 VEB-14 http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase VEB-14 is a VEB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006212 VEB-15 http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase VEB-15 is a VEB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006213 VEB-17 http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase VEB-17 is a VEB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006214 VEB-19 http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase VEB-19 is a VEB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006215 VEB-20 http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase VEB-20 is a VEB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006216 VEB-21 http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase VEB-21 is a VEB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006217 VEB-22 http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase VEB-22 is a VEB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006218 VEB-23 http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase VEB-23 is a VEB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006219 VEB-24 http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase VEB-24 is a VEB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006220 VEB-25 http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase VEB-25 is a VEB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006221 VEB-26 http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase VEB-26 is a VEB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006222 VEB-27 http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase VEB-27 is a VEB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006223 BKC-2 http://purl.obolibrary.org/obo/ARO_3004756 BKC Beta-lactamase BKC-2 is a BKC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006224 CepA-29 http://purl.obolibrary.org/obo/ARO_3004192 CepA beta-lactamase CepA-29 is a CepA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006225 CepA-44 http://purl.obolibrary.org/obo/ARO_3004192 CepA beta-lactamase CepA-44 is a CepA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006226 CepA-49 http://purl.obolibrary.org/obo/ARO_3004192 CepA beta-lactamase CepA-49 is a CepA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006227 FRI-10 http://purl.obolibrary.org/obo/ARO_3004796 FRI beta-lactamase FRI-10 is a FRI beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006228 ACC-1a http://purl.obolibrary.org/obo/ARO_3001815 ACC-1 ACC-1a is a ACC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006229 ACC-1b http://purl.obolibrary.org/obo/ARO_3001815 ACC-1 ACC-1b is a ACC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006230 ACC-1c http://purl.obolibrary.org/obo/ARO_3001815 ACC-1 ACC-1c is a ACC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006231 ACC-1d http://purl.obolibrary.org/obo/ARO_3001815 ACC-1 ACC-1d is a ACC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006232 ACC-7 http://purl.obolibrary.org/obo/ARO_3000073 ACC beta-lactamase ACC-7 is a ACC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006233 ACC-8 http://purl.obolibrary.org/obo/ARO_3000073 ACC beta-lactamase ACC-8 is a ACC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006234 ACT-39 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-39 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006235 ACT-40 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-40 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006236 ACT-41 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-41 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006237 ACT-42 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-42 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006238 ACT-43 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-43 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006239 ACT-44 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-44 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006240 ACT-45 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-45 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006241 ACT-46 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-46 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006242 ACT-47 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-47 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006243 ACT-48 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-48 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006244 ACT-49 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-49 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006245 ACT-50 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-50 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006246 ACT-51 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-51 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006247 ACT-52 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-52 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006248 ACT-53 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-53 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006249 ACT-54 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-54 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006250 ACT-55 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-55 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006251 ACT-56 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-56 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006252 ACT-57 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-57 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006253 ACT-58 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-58 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006254 ACT-59 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-59 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006255 ACT-60 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-60 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006256 ACT-61 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-61 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006257 ACT-62 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-62 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006258 ACT-63 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-63 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006259 ACT-64 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-64 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006260 ACT-65 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-65 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006261 ACT-66 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-66 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006262 ACT-67 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-67 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006263 ACT-68 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-68 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006264 ACT-69 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-69 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006265 ACT-70 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-70 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006266 ACT-72 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-72 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006267 ACT-73 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-73 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006268 ACT-74 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-74 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006269 ACT-75 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-75 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006270 ACT-76 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-76 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006271 ACT-77 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-77 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006272 ACT-78 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-78 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006273 ACT-79 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-79 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006274 ACT-80 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-80 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006275 ACT-81 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-81 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006276 ACT-82 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-82 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006277 ACT-83 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-83 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006278 ACT-84 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-84 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006279 ACT-87 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-87 is a ACT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006280 ADC-100 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-100 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006281 ADC-101 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-101 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006282 ADC-102 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-102 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006283 ADC-103 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-103 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006284 ADC-104 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-104 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006285 ADC-105 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-105 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006286 ADC-106 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-106 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006287 ADC-107 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-107 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006288 ADC-109 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-109 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006289 ADC-110 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-110 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006290 ADC-112 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-112 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006291 ADC-113 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-113 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006292 ADC-114 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-114 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006293 ADC-115 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-115 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006294 ADC-116 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-116 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006295 ADC-117 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-117 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006296 ADC-119 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-119 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006297 ADC-120 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-120 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006298 ADC-121 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-121 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006299 ADC-122 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-122 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006300 ADC-123 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-123 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006301 ADC-125 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-125 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006302 ADC-127 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-127 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006303 ADC-128 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-128 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006304 ADC-129 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-129 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006305 ADC-130 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-130 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006306 ADC-131 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-131 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006307 ADC-132 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-132 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006308 ADC-133 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-133 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006309 ADC-134 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-134 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006310 ADC-135 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-135 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006311 ADC-136 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-136 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006312 ADC-137 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-137 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006313 ADC-138 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-138 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006314 ADC-139 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-139 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006315 ADC-140 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-140 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006316 ADC-141 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-141 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006317 ADC-143 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-143 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006318 ADC-144 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-144 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006319 ADC-145 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-145 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006320 ADC-146 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-146 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006321 ADC-147 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-147 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006322 ADC-148 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-148 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006323 ADC-149 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-149 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006324 ADC-150 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-150 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006325 ADC-151 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-151 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006326 ADC-152 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-152 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006327 ADC-153 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-153 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006328 ADC-154 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-154 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006329 ADC-155 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-155 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006330 ADC-156 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-156 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006331 ADC-157 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-157 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006332 ADC-158 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-158 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006333 ADC-160 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-160 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006334 ADC-162 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-162 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006335 ADC-163 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-163 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006336 ADC-164 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-164 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006337 ADC-165 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-165 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006338 ADC-166 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-166 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006339 ADC-167 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-167 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006340 ADC-168 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-168 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006341 ADC-169 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-169 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006342 ADC-170 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-170 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006343 ADC-171 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-171 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006344 ADC-172 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-172 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006345 ADC-173 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-173 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006346 ADC-174 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-174 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006347 ADC-175 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-175 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006348 ADC-176 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-176 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006349 ADC-177 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-177 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006350 ADC-178 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-178 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006351 ADC-179 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-179 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006352 ADC-180 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-180 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006353 ADC-184 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-184 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006354 ADC-185 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-185 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006355 ADC-186 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-186 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006356 ADC-187 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-187 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006357 ADC-188 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-188 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006358 ADC-189 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-189 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006359 ADC-190 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-190 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006360 ADC-191 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-191 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006361 ADC-192 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-192 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006362 ADC-193 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-193 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006363 ADC-194 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-194 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006364 ADC-195 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-195 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006365 ADC-196 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-196 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006366 ADC-197 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-197 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006367 ADC-198 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-198 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006368 ADC-199 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-199 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006369 ADC-200 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-200 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006370 ADC-201 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-201 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006371 ADC-202 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-202 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006372 ADC-203 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-203 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006373 ADC-204 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-204 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006374 ADC-205 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-205 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006375 ADC-206 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-206 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006376 ADC-207 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-207 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006377 ADC-208 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-208 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006378 ADC-209 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-209 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006379 ADC-210 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-210 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006380 ADC-211 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-211 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006381 ADC-212 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-212 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006382 ADC-213 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-213 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006383 ADC-214 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-214 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006384 ADC-215 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-215 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006385 ADC-216 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-216 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006386 ADC-217 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-217 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006387 ADC-218 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-218 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006388 ADC-219 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-219 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006389 ADC-220 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-220 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006390 ADC-221 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-221 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006391 ADC-222 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-222 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006392 ADC-223 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-223 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006393 ADC-224 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-224 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006394 ADC-225 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-225 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006395 ADC-226 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-226 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006396 ADC-227 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-227 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006397 ADC-228 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-228 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006398 ADC-229 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-229 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006399 ADC-230 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-230 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006400 ADC-231 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-231 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006401 ADC-232 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-232 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006402 ADC-233 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-233 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006403 ADC-234 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-234 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006404 ADC-235 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-235 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006405 ADC-236 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-236 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006406 ADC-237 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-237 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006407 ADC-238 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-238 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006408 ADC-239 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-239 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006409 ADC-24 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-24 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006410 ADC-240 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-240 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006411 ADC-241 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-241 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006412 ADC-242 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-242 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006413 ADC-243 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-243 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006414 ADC-244 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-244 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006415 ADC-245 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-245 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006416 ADC-246 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-246 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006417 ADC-247 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-247 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006418 ADC-248 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-248 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006419 ADC-249 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-249 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006420 ADC-250 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-250 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006421 ADC-251 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-251 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006422 ADC-252 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-252 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006423 ADC-253 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-253 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006424 ADC-254 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-254 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006425 ADC-255 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-255 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006426 ADC-256 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-256 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006427 ADC-29 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-29 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006428 ADC-32 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-32 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006429 ADC-33 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-33 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006430 ADC-38 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-38 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006431 ADC-51 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-51 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006432 ADC-52 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-52 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006433 ADC-53 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-53 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006434 ADC-54 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-54 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006435 ADC-57 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-57 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006436 ADC-63 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-63 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006437 ADC-65 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-65 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006438 ADC-66 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-66 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006439 ADC-70 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-70 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006440 ADC-83 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-83 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006441 ADC-84 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-84 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006442 ADC-85 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-85 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006443 ADC-86 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-86 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006444 ADC-87 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-87 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006445 ADC-88 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-88 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006446 ADC-89 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-89 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006447 ADC-90 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-90 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006448 ADC-91 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-91 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006449 ADC-92 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-92 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006450 ADC-93 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-93 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006451 ADC-94 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-94 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006452 ADC-95 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-95 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006453 ADC-96 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-96 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006454 ADC-97 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-97 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006455 ADC-98 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-98 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006456 ADC-99 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity ADC-99 is a ADC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006457 CMY-137 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-137 is a CMY beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006458 CMY-159 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-159 is a CMY beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006459 CMY-167 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-167 is a CMY beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006460 CMY-168 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-168 is a CMY beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006461 CMY-169 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-169 is a CMY beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006462 CMY-170 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-170 is a CMY beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006463 CMY-174 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-174 is a CMY beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006464 CMY-8b http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-8b is a CMY beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006465 DHA-24 http://purl.obolibrary.org/obo/ARO_3000068 DHA beta-lactamase DHA-24 is a DHA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006466 DHA-25 http://purl.obolibrary.org/obo/ARO_3000068 DHA beta-lactamase DHA-25 is a DHA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006467 DHA-26 http://purl.obolibrary.org/obo/ARO_3000068 DHA beta-lactamase DHA-26 is a DHA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006468 DHA-27 http://purl.obolibrary.org/obo/ARO_3000068 DHA beta-lactamase DHA-27 is a DHA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006469 DHA-28 http://purl.obolibrary.org/obo/ARO_3000068 DHA beta-lactamase DHA-28 is a DHA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006470 DHA-29 http://purl.obolibrary.org/obo/ARO_3000068 DHA beta-lactamase DHA-29 is a DHA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006471 FOX-13 http://purl.obolibrary.org/obo/ARO_3000067 FOX beta-lactamase FOX-13 is a FOX beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006472 FOX-14 http://purl.obolibrary.org/obo/ARO_3000067 FOX beta-lactamase FOX-14 is a FOX beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006473 FOX-15 http://purl.obolibrary.org/obo/ARO_3000067 FOX beta-lactamase FOX-15 is a FOX beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006474 FOX-16 http://purl.obolibrary.org/obo/ARO_3000067 FOX beta-lactamase FOX-16 is a FOX beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006475 FOX-17 http://purl.obolibrary.org/obo/ARO_3000067 FOX beta-lactamase FOX-17 is a FOX beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006477 MOX-12 http://purl.obolibrary.org/obo/ARO_3000083 MOX beta-lactamase MOX-12 is a MOX beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006478 MOX-13 http://purl.obolibrary.org/obo/ARO_3000083 MOX beta-lactamase MOX-13 is a MOX beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006479 MOX-14 http://purl.obolibrary.org/obo/ARO_3000083 MOX beta-lactamase MOX-14 is a MOX beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006480 PDC-100 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-100 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006481 PDC-101 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-101 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006482 PDC-102 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-102 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006483 PDC-103 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-103 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006484 PDC-106 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-106 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006485 PDC-107 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-107 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006486 PDC-108 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-108 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006487 PDC-109 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-109 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006488 PDC-110 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-110 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006489 PDC-111 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-111 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006490 PDC-112 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-112 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006491 PDC-113 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-113 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006492 PDC-114 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-114 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006493 PDC-115 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-115 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006494 PDC-116 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-116 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006495 PDC-12 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-12 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006496 PDC-120 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-120 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006497 PDC-121 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-121 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006498 PDC-122 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-122 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006499 PDC-123 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-123 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006500 PDC-124 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-124 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006501 PDC-125 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-125 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006502 PDC-126 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-126 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006503 PDC-127 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-127 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006504 PDC-128 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-128 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006505 PDC-129 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-129 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006506 PDC-13 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-13 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006507 PDC-130 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-130 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006508 PDC-131 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-131 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006509 PDC-132 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-132 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006510 PDC-133 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-133 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006511 PDC-134 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-134 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006512 PDC-135 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-135 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006513 PDC-136 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-136 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006514 PDC-137 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-137 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006515 PDC-138 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-138 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006516 PDC-139 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-139 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006517 PDC-140 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-140 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006518 PDC-141 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-141 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006519 PDC-142 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-142 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006520 PDC-143 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-143 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006521 PDC-144 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-144 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006522 PDC-145 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-145 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006523 PDC-146 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-146 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006524 PDC-147 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-147 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006525 PDC-148 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-148 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006526 PDC-149 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-149 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006527 PDC-15 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-15 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006528 PDC-150 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-150 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006529 PDC-151 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-151 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006530 PDC-152 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-152 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006531 PDC-153 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-153 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006532 PDC-154 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-154 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006533 PDC-155 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-155 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006534 PDC-156 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-156 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006535 PDC-157 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-157 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006536 PDC-158 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-158 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006537 PDC-159 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-159 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006538 PDC-16 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-16 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006539 PDC-160 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-160 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006540 PDC-161 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-161 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006541 PDC-162 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-162 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006542 PDC-163 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-163 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006543 PDC-164 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-164 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006544 PDC-165 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-165 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006545 PDC-166 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-166 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006546 PDC-167 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-167 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006547 PDC-168 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-168 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006548 PDC-169 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-169 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006549 PDC-17 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-17 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006550 PDC-170 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-170 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006551 PDC-171 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-171 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006552 PDC-172 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-172 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006553 PDC-174 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-174 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006554 PDC-175 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-175 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006555 PDC-176 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-176 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006556 PDC-177 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-177 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006557 PDC-178 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-178 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006558 PDC-179 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-179 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006559 PDC-18 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-18 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006560 PDC-180 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-180 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006561 PDC-181 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-181 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006562 PDC-182 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-182 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006563 PDC-184 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-184 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006564 PDC-185 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-185 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006565 PDC-186 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-186 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006566 PDC-187 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-187 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006567 PDC-188 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-188 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006568 PDC-189 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-189 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006569 PDC-190 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-190 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006570 PDC-191 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-191 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006571 PDC-192 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-192 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006572 PDC-193 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-193 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006573 PDC-194 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-194 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006574 PDC-195 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-195 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006575 PDC-196 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-196 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006576 PDC-197 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-197 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006577 PDC-198 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-198 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006578 PDC-199 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-199 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006579 PDC-20 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-20 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006580 PDC-200 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-200 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006581 PDC-202 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-202 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006582 PDC-203 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-203 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006583 PDC-204 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-204 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006584 PDC-205 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-205 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006585 PDC-206 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-206 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006586 PDC-208 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-208 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006587 PDC-209 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-209 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006588 PDC-210 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-210 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006589 PDC-211 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-211 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006590 PDC-213 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-213 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006591 PDC-214 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-214 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006592 PDC-215 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-215 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006593 PDC-216 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-216 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006594 PDC-217 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-217 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006595 PDC-218 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-218 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006596 PDC-219 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-219 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006597 PDC-21a http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-21a is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006598 PDC-21b http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-21b is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006599 PDC-22 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-22 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006600 PDC-220 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-220 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006601 PDC-221 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-221 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006602 PDC-222 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-222 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006603 PDC-223 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-223 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006604 PDC-224 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-224 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006605 PDC-226 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-226 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006606 PDC-227 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-227 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006607 PDC-228 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-228 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006608 PDC-229 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-229 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006609 PDC-230 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-230 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006610 PDC-232 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-232 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006611 PDC-233 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-233 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006612 PDC-234 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-234 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006613 PDC-235 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-235 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006614 PDC-236 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-236 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006615 PDC-237 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-237 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006616 PDC-238 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-238 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006617 PDC-239 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-239 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006618 PDC-24 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-24 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006619 PDC-241 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-241 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006620 PDC-242 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-242 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006621 PDC-243 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-243 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006622 PDC-244 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-244 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006623 PDC-245 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-245 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006624 PDC-246 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-246 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006625 PDC-247 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-247 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006626 PDC-248 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-248 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006627 PDC-249 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-249 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006628 PDC-25 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-25 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006629 PDC-250 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-250 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006630 PDC-251 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-251 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006631 PDC-252 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-252 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006632 PDC-253 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-253 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006633 PDC-254 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-254 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006634 PDC-256 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-256 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006635 PDC-259 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-259 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006636 PDC-26 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-26 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006637 PDC-260 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-260 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006638 PDC-261 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-261 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006639 PDC-262 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-262 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006640 PDC-263 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-263 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006641 PDC-265 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-265 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006642 PDC-266 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-266 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006643 PDC-267 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-267 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006644 PDC-268 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-268 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006645 PDC-270 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-270 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006646 PDC-271 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-271 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006647 PDC-273 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-273 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006648 PDC-274 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-274 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006649 PDC-275 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-275 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006650 PDC-276 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-276 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006651 PDC-277 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-277 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006652 PDC-278 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-278 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006653 PDC-279 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-279 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006654 PDC-280 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-280 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006655 PDC-281 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-281 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006656 PDC-282 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-282 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006657 PDC-283 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-283 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006658 PDC-286 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-286 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006659 PDC-287 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-287 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006660 PDC-288 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-288 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006661 PDC-289 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-289 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006662 PDC-290 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-290 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006663 PDC-291 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-291 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006664 PDC-294 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-294 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006665 PDC-295 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-295 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006666 PDC-296 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-296 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006667 PDC-297 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-297 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006668 PDC-298 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-298 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006669 PDC-299 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-299 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006670 PDC-30 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-30 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006671 PDC-300 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-300 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006672 PDC-301 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-301 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006673 PDC-302 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-302 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006674 PDC-303 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-303 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006675 PDC-304 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-304 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006676 PDC-305 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-305 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006677 PDC-307 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-307 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006678 PDC-308 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-308 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006679 PDC-309 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-309 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006680 PDC-31 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-31 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006681 PDC-310 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-310 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006682 PDC-311 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-311 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006683 PDC-312 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-312 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006684 PDC-314 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-314 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006685 PDC-315 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-315 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006686 PDC-316 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-316 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006687 PDC-317 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-317 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006688 PDC-318 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-318 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006689 PDC-319 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-319 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006690 PDC-32 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-32 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006691 PDC-320 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-320 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006692 PDC-321 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-321 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006693 PDC-322 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-322 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006694 PDC-325 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-325 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006695 PDC-326 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-326 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006696 PDC-327 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-327 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006697 PDC-328 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-328 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006698 PDC-329 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-329 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006699 PDC-33 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-33 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006700 PDC-330 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-330 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006701 PDC-331 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-331 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006702 PDC-332 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-332 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006703 PDC-333 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-333 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006704 PDC-334 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-334 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006705 PDC-335 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-335 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006706 PDC-336 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-336 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006707 PDC-338 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-338 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006708 PDC-339 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-339 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006709 PDC-34 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-34 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006710 PDC-340 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-340 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006711 PDC-341 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-341 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006712 PDC-342 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-342 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006713 PDC-343 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-343 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006714 PDC-344 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-344 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006715 PDC-345 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-345 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006716 PDC-347 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-347 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006717 PDC-348 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-348 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006718 PDC-349 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-349 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006719 PDC-35 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-35 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006720 PDC-350 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-350 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006721 PDC-351 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-351 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006722 PDC-353 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-353 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006723 PDC-354 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-354 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006724 PDC-355 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-355 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006725 PDC-356 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-356 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006726 PDC-357 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-357 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006727 PDC-358 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-358 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006728 PDC-359 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-359 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006729 PDC-36 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-36 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006730 PDC-360 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-360 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006731 PDC-361 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-361 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006732 PDC-362 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-362 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006733 PDC-363 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-363 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006734 PDC-364 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-364 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006735 PDC-365 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-365 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006736 PDC-366 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-366 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006737 PDC-367 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-367 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006738 PDC-368 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-368 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006739 PDC-369 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-369 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006740 PDC-37 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-37 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006741 PDC-370 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-370 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006742 PDC-371 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-371 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006743 PDC-372 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-372 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006744 PDC-373 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-373 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006745 PDC-374 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-374 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006746 PDC-375 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-375 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006747 PDC-377 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-377 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006748 PDC-378 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-378 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006749 PDC-379 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-379 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006750 PDC-38 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-38 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006751 PDC-381 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-381 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006752 PDC-382 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-382 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006753 PDC-383 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-383 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006754 PDC-385 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-385 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006755 PDC-386 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-386 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006756 PDC-387 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-387 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006757 PDC-388 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-388 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006758 PDC-389 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-389 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006759 PDC-39 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-39 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006760 PDC-390 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-390 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006761 PDC-391 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-391 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006762 PDC-392 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-392 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006763 PDC-394 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-394 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006764 PDC-395 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-395 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006765 PDC-396 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-396 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006766 PDC-397 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-397 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006767 PDC-398 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-398 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006768 PDC-399 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-399 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006769 PDC-40 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-40 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006770 PDC-400 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-400 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006771 PDC-401 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-401 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006772 PDC-402 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-402 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006773 PDC-403 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-403 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006774 PDC-404 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-404 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006775 PDC-405 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-405 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006776 PDC-406 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-406 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006777 PDC-407 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-407 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006778 PDC-408 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-408 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006779 PDC-409 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-409 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006780 PDC-410 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-410 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006781 PDC-411 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-411 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006782 PDC-412 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-412 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006783 PDC-414 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-414 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006784 PDC-415 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-415 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006785 PDC-416 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-416 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006786 PDC-417 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-417 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006787 PDC-418 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-418 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006788 PDC-419 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-419 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006789 PDC-42 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-42 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006790 PDC-420 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-420 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006791 PDC-421 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-421 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006792 PDC-422 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-422 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006793 PDC-423 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-423 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006794 PDC-424 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-424 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006795 PDC-425 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-425 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006796 PDC-426 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-426 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006797 PDC-427 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-427 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006798 PDC-428 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-428 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006799 PDC-430 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-430 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006800 PDC-431 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-431 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006801 PDC-432 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-432 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006802 PDC-433 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-433 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006803 PDC-434 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-434 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006804 PDC-435 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-435 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006805 PDC-436 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-436 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006806 PDC-437 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-437 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006807 PDC-439 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-439 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006808 PDC-440 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-440 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006809 PDC-441 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-441 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006810 PDC-442 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-442 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006811 PDC-443 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-443 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006812 PDC-444 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-444 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006813 PDC-445 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-445 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006814 PDC-446 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-446 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006815 PDC-447 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-447 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006816 PDC-448 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-448 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006817 PDC-450 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-450 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006818 PDC-451 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-451 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006819 PDC-452 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-452 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006820 PDC-453 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-453 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006821 PDC-454 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-454 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006822 PDC-455 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-455 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006823 PDC-456 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-456 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006824 PDC-457 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-457 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006825 PDC-458 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-458 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006826 PDC-459 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-459 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006827 PDC-46 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-46 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006828 PDC-460 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-460 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006829 PDC-462 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-462 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006830 PDC-463 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-463 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006831 PDC-465 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-465 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006832 PDC-466 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-466 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006833 PDC-467 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-467 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006834 PDC-468 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-468 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006835 PDC-469 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-469 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006836 PDC-470 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-470 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006837 PDC-471 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-471 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006838 PDC-472 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-472 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006839 PDC-473 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-473 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006840 PDC-474 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-474 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006841 PDC-475 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-475 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006842 PDC-476 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-476 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006843 PDC-58 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-58 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006844 PDC-60 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-60 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006845 PDC-64 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-64 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006846 PDC-71 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-71 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006847 PDC-94 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-94 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006848 PDC-95 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-95 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006849 PDC-96 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-96 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006850 PDC-97 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-97 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006851 PDC-98 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-98 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006852 PDC-99 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-99 is a PDC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006853 SRT-3 http://purl.obolibrary.org/obo/ARO_3000095 SRT beta-lactamase SRT-3 is a SRT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006854 CMH-2 http://purl.obolibrary.org/obo/ARO_3004776 CMH beta-lactamase CMH-2 is a CMH beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006855 CMH-3 http://purl.obolibrary.org/obo/ARO_3004776 CMH beta-lactamase CMH-3 is a CMH beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006856 CMH-4 http://purl.obolibrary.org/obo/ARO_3004776 CMH beta-lactamase CMH-4 is a CMH beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006857 CMH-5 http://purl.obolibrary.org/obo/ARO_3004776 CMH beta-lactamase CMH-5 is a CMH beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006858 CMH-6 http://purl.obolibrary.org/obo/ARO_3004776 CMH beta-lactamase CMH-6 is a CMH beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006859 MIR-19 http://purl.obolibrary.org/obo/ARO_3000058 MIR beta-lactamase MIR-19 is a MIR beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006860 MIR-20 http://purl.obolibrary.org/obo/ARO_3000058 MIR beta-lactamase MIR-20 is a MIR beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006861 MIR-21 http://purl.obolibrary.org/obo/ARO_3000058 MIR beta-lactamase MIR-21 is a MIR beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006862 MIR-22 http://purl.obolibrary.org/obo/ARO_3000058 MIR beta-lactamase MIR-22 is a MIR beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006863 AAK-1 http://purl.obolibrary.org/obo/ARO_3005387 AAK beta-lactamase AAK-1 is a AAK beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006864 CRD3-1 http://purl.obolibrary.org/obo/ARO_3005398 CRD3 beta-lactamase CRD3-1 is a CRD3 beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006865 CRH-1 http://purl.obolibrary.org/obo/ARO_3005399 CRH beta-lactamase CRH-1 is a CRH beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006866 CRH-2 http://purl.obolibrary.org/obo/ARO_3005399 CRH beta-lactamase CRH-2 is a CRH beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006867 CRH-3 http://purl.obolibrary.org/obo/ARO_3005399 CRH beta-lactamase CRH-3 is a CRH beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006868 CRP-1 http://purl.obolibrary.org/obo/ARO_3005400 CRP beta-lactamase CRP-1 is a CRP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006869 CSA-1 http://purl.obolibrary.org/obo/ARO_3005401 CSA beta-lactamase CSA-1 is a CSA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006870 CSA-2 http://purl.obolibrary.org/obo/ARO_3005401 CSA beta-lactamase CSA-2 is a CSA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006871 CSP-1 http://purl.obolibrary.org/obo/ARO_3005402 CSP beta-lactamase CSP-1 is a CSP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006872 DHT2-1 http://purl.obolibrary.org/obo/ARO_3005404 DHT2 beta-lactamase DHT2-1 is a DHT2 beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006873 EAM-1 http://purl.obolibrary.org/obo/ARO_3005405 EAM beta-lactamase EAM-1 is a EAM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006874 EC-13 http://purl.obolibrary.org/obo/ARO_3005406 EC beta-lactamase EC-13 is a EC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006875 EC-14 http://purl.obolibrary.org/obo/ARO_3005406 EC beta-lactamase EC-14 is a EC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006876 EC-15 http://purl.obolibrary.org/obo/ARO_3005406 EC beta-lactamase EC-15 is a EC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006877 EC-16 http://purl.obolibrary.org/obo/ARO_3005406 EC beta-lactamase EC-16 is a EC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006878 EC-18 http://purl.obolibrary.org/obo/ARO_3005406 EC beta-lactamase EC-18 is a EC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006879 EC-19 http://purl.obolibrary.org/obo/ARO_3005406 EC beta-lactamase EC-19 is a EC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006880 EC-5 http://purl.obolibrary.org/obo/ARO_3005406 EC beta-lactamase EC-5 is a EC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006881 EC-8 http://purl.obolibrary.org/obo/ARO_3005406 EC beta-lactamase EC-8 is a EC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006882 ECM-1 http://purl.obolibrary.org/obo/ARO_3005407 ECM beta-lactamase ECM-1 is a ECM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006883 ECV-1 http://purl.obolibrary.org/obo/ARO_3005408 ECV beta-lactamase ECV-1 is a ECV beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006884 EFM-1 http://purl.obolibrary.org/obo/ARO_3005409 EFM beta-lactamase EFM-1 is a EFM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006885 ELM-1 http://purl.obolibrary.org/obo/ARO_3005410 ELM beta-lactamase ELM-1 is a ELM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006886 EVM-1 http://purl.obolibrary.org/obo/ARO_3005411 EVM beta-lactamase EVM-1 is a EVM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006887 FIA-1 http://purl.obolibrary.org/obo/ARO_3005412 FIA beta-lactamase FIA-1 is a FIA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006888 GIL-1 http://purl.obolibrary.org/obo/ARO_3005413 GIL beta-lactamase GIL-1 is a GIL beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006889 GMB-1 http://purl.obolibrary.org/obo/ARO_3005414 GMB beta-lactamase GMB-1 is a GMB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006890 AFM-1 http://purl.obolibrary.org/obo/ARO_3005388 AFM beta-lactamase AFM-1 is a AFM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006891 AFM-2 http://purl.obolibrary.org/obo/ARO_3005388 AFM beta-lactamase AFM-2 is a AFM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006892 ALG11-1 http://purl.obolibrary.org/obo/ARO_3005389 ALG11 beta-lactamase ALG11-1 is a ALG11 beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006893 ALG6-1 http://purl.obolibrary.org/obo/ARO_3005390 ALG6 beta-lactamases ALG6-1 is a ALG6 beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006894 ALI-1 http://purl.obolibrary.org/obo/ARO_3005391 ALI beta-lactamase ALI-1 is a ALI beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006895 ALI-2 http://purl.obolibrary.org/obo/ARO_3005391 ALI beta-lactamase ALI-2 is a ALI beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006896 ANA-1 http://purl.obolibrary.org/obo/ARO_3005392 ANA beta-lactamase ANA-1 is a ANA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006897 AXC-1 http://purl.obolibrary.org/obo/ARO_3005393 AXC beta-lactamase AXC-1 is a AXC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006898 AXC-2 http://purl.obolibrary.org/obo/ARO_3005393 AXC beta-lactamase AXC-2 is a AXC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006899 AXC-3 http://purl.obolibrary.org/obo/ARO_3005393 AXC beta-lactamase AXC-3 is a AXC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006900 AXC-4 http://purl.obolibrary.org/obo/ARO_3005393 AXC beta-lactamase AXC-4 is a AXC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006901 AXC-5 http://purl.obolibrary.org/obo/ARO_3005393 AXC beta-lactamase AXC-5 is a AXC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006902 BSU-1 http://purl.obolibrary.org/obo/ARO_3005394 BSU beta-lactamase BSU-1 is a BSU beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006903 CAR-1 http://purl.obolibrary.org/obo/ARO_3005395 CAR beta-lactamase CAR-1 is a CAR beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006904 CDD-1 http://purl.obolibrary.org/obo/ARO_3005396 CDD beta-lactamase CDD-1 is a CDD beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006905 CDD-2 http://purl.obolibrary.org/obo/ARO_3005396 CDD beta-lactamase CDD-2 is a CDD beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006906 CfiA10 http://purl.obolibrary.org/obo/ARO_3004200 CfiA beta-lactamase CfiA10 is a CfiA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006907 CfiA11 http://purl.obolibrary.org/obo/ARO_3004200 CfiA beta-lactamase CfiA11 is a CfiA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006908 CfiA14 http://purl.obolibrary.org/obo/ARO_3004200 CfiA beta-lactamase CfiA14 is a CfiA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006909 CfiA17 http://purl.obolibrary.org/obo/ARO_3004200 CfiA beta-lactamase CfiA17 is a CfiA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006910 CfiA18 http://purl.obolibrary.org/obo/ARO_3004200 CfiA beta-lactamase CfiA18 is a CfiA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006911 CfiA19 http://purl.obolibrary.org/obo/ARO_3004200 CfiA beta-lactamase CfiA19 is a CfiA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006912 CfiA2 http://purl.obolibrary.org/obo/ARO_3004200 CfiA beta-lactamase CfiA2 is a CfiA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006913 CfiA21 http://purl.obolibrary.org/obo/ARO_3004200 CfiA beta-lactamase CfiA21 is a CfiA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006914 CfiA22 http://purl.obolibrary.org/obo/ARO_3004200 CfiA beta-lactamase CfiA22 is a CfiA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006915 CfiA23 http://purl.obolibrary.org/obo/ARO_3004200 CfiA beta-lactamase CfiA23 is a CfiA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006916 CfiA24 http://purl.obolibrary.org/obo/ARO_3004200 CfiA beta-lactamase CfiA24 is a CfiA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006917 CfiA26 http://purl.obolibrary.org/obo/ARO_3004200 CfiA beta-lactamase CfiA26 is a CfiA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006918 CfiA27 http://purl.obolibrary.org/obo/ARO_3004200 CfiA beta-lactamase CfiA27 is a CfiA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006919 CfiA4 http://purl.obolibrary.org/obo/ARO_3004200 CfiA beta-lactamase CfiA4 is a CfiA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006920 CfiA8 http://purl.obolibrary.org/obo/ARO_3004200 CfiA beta-lactamase CfiA8 is a CfiA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006921 CfiA9 http://purl.obolibrary.org/obo/ARO_3004200 CfiA beta-lactamase CfiA9 is a CfiA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006922 CMA-1 http://purl.obolibrary.org/obo/ARO_3005397 CMA beta-lactamase CMA-1 is a CMA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006923 CMA-2 http://purl.obolibrary.org/obo/ARO_3005397 CMA beta-lactamase CMA-2 is a CMA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006924 CVI-1 http://purl.obolibrary.org/obo/ARO_3005403 CVI beta-lactamase CVI-1 is a CVI beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006925 GRD23-1 http://purl.obolibrary.org/obo/ARO_3005415 GRD23 beta-lactamase GRD23-1 is a GRD23 beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006926 GRD33-1 http://purl.obolibrary.org/obo/ARO_3005416 GRD33 beta-lactamase GRD33-1 is a GRD33 beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006927 KLUC-1 http://purl.obolibrary.org/obo/ARO_3005417 KLUC beta-lactamase KLUC-1 is a KLUC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006928 KLUC-2 http://purl.obolibrary.org/obo/ARO_3005417 KLUC beta-lactamase KLUC-2 is a KLUC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006929 KLUC-3 http://purl.obolibrary.org/obo/ARO_3005417 KLUC beta-lactamase KLUC-3 is a KLUC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006930 KLUC-4 http://purl.obolibrary.org/obo/ARO_3005417 KLUC beta-lactamase KLUC-4 is a KLUC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006931 KLUC-5 http://purl.obolibrary.org/obo/ARO_3005417 KLUC beta-lactamase KLUC-5 is a KLUC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006932 LEN-27 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase LEN-27 is a LEN beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006933 LEN-28 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase LEN-28 is a LEN beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006934 LEN-31 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase LEN-31 is a LEN beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006935 LHK-1 http://purl.obolibrary.org/obo/ARO_3005418 LHK beta-lactamase LHK-1 is a LHK beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006936 LHK-2 http://purl.obolibrary.org/obo/ARO_3005418 LHK beta-lactamase LHK-2 is a LHK beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006937 LHK-3 http://purl.obolibrary.org/obo/ARO_3005418 LHK beta-lactamase LHK-3 is a LHK beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006938 LHK-4 http://purl.obolibrary.org/obo/ARO_3005418 LHK beta-lactamase LHK-4 is a LHK beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006939 LHK-5 http://purl.obolibrary.org/obo/ARO_3005418 LHK beta-lactamase LHK-5 is a LHK beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006940 LHK-6 http://purl.obolibrary.org/obo/ARO_3005418 LHK beta-lactamase LHK-6 is a LHK beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006941 LRG-1 http://purl.obolibrary.org/obo/ARO_3005419 LRG beta-lactamase LRG-1 is a LRG beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006942 LUS-1 http://purl.obolibrary.org/obo/ARO_3005420 LUS beta-lactamase LUS-1 is a LUS beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006943 LUT-1 http://purl.obolibrary.org/obo/ARO_3005421 LUT beta-lactamase LUT-1 is a LUT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006944 LUT-2 http://purl.obolibrary.org/obo/ARO_3005421 LUT beta-lactamase LUT-2 is a LUT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006945 LUT-3 http://purl.obolibrary.org/obo/ARO_3005421 LUT beta-lactamase LUT-3 is a LUT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006946 LUT-4 http://purl.obolibrary.org/obo/ARO_3005421 LUT beta-lactamase LUT-4 is a LUT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006947 LUT-5 http://purl.obolibrary.org/obo/ARO_3005421 LUT beta-lactamase LUT-5 is a LUT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006948 LUT-6 http://purl.obolibrary.org/obo/ARO_3005421 LUT beta-lactamase LUT-6 is a LUT beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006949 MAL-1 http://purl.obolibrary.org/obo/ARO_3005422 MAL beta-lactamase MAL-1 is a MAL beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006950 MAL-2 http://purl.obolibrary.org/obo/ARO_3005422 MAL beta-lactamase MAL-2 is a MAL beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006951 MBL1b http://purl.obolibrary.org/obo/ARO_3005423 MBL beta-lactamase MBL1b is a MBL beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006952 MOC-1 http://purl.obolibrary.org/obo/ARO_3005424 MOC beta-lactamase MOC-1 is a MOC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006953 MOR-2 http://purl.obolibrary.org/obo/ARO_3005425 MOR beta-lactamase MOR-2 is a MOR beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006954 MYO-1 http://purl.obolibrary.org/obo/ARO_3005426 MYO beta-lactamase MYO-1 is a MYO beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006955 MYX-1 http://purl.obolibrary.org/obo/ARO_3005427 MYX beta-lactamase MYX-1 is a MYX beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006956 OHIO-1 http://purl.obolibrary.org/obo/ARO_3005428 OHIO beta-lactamase OHIO-1 is a OHIO beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006957 ORN-1 http://purl.obolibrary.org/obo/ARO_3005429 ORN beta-lactamase ORN-1 is a ORN beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006958 ORN-2 http://purl.obolibrary.org/obo/ARO_3005429 ORN beta-lactamase ORN-2 is a ORN beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006959 ORN-3 http://purl.obolibrary.org/obo/ARO_3005429 ORN beta-lactamase ORN-3 is a ORN beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006960 ORN-4 http://purl.obolibrary.org/obo/ARO_3005429 ORN beta-lactamase ORN-4 is a ORN beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006961 ORN-5 http://purl.obolibrary.org/obo/ARO_3005429 ORN beta-lactamase ORN-5 is a ORN beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006962 ORN-6 http://purl.obolibrary.org/obo/ARO_3005429 ORN beta-lactamase ORN-6 is a ORN beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006963 ORR-1 http://purl.obolibrary.org/obo/ARO_3005430 ORR beta-lactamase ORR-1 is a ORR beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006964 PAU-1 http://purl.obolibrary.org/obo/ARO_3005431 PAU beta-lactamase PAU-1 is a PAU beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006965 PFM-1 http://purl.obolibrary.org/obo/ARO_3005432 PFM beta-lactamase PFM-1 is a PFM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006966 PFM-2 http://purl.obolibrary.org/obo/ARO_3005432 PFM beta-lactamase PFM-2 is a PFM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006967 PFM-3 http://purl.obolibrary.org/obo/ARO_3005432 PFM beta-lactamase PFM-3 is a PFM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006968 PLA-1 http://purl.obolibrary.org/obo/ARO_3005433 PLA beta-lactamase PLA-1 is a PLA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006969 PLA-2a http://purl.obolibrary.org/obo/ARO_3005433 PLA beta-lactamase PLA-2a is a PLA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006970 PLA-3 http://purl.obolibrary.org/obo/ARO_3005433 PLA beta-lactamase PLA-3 is a PLA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006971 PLA-6 http://purl.obolibrary.org/obo/ARO_3005433 PLA beta-lactamase PLA-6 is a PLA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006972 PLN-1 http://purl.obolibrary.org/obo/ARO_3005434 PLN beta-lactamase PLN-1 is a PLN beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006973 PME-1 http://purl.obolibrary.org/obo/ARO_3005435 PME beta-lactamase PME-1 is a PME beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006974 POM-1 http://purl.obolibrary.org/obo/ARO_3005436 POM beta-lactamase POM-1 is a POM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006975 POM-2 http://purl.obolibrary.org/obo/ARO_3005436 POM beta-lactamase POM-2 is a POM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006976 PST-1 http://purl.obolibrary.org/obo/ARO_3005437 PST beta-lactamase PST-1 is a PST beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006977 PST-2 http://purl.obolibrary.org/obo/ARO_3005437 PST beta-lactamase PST-2 is a PST beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006978 PSV-1 http://purl.obolibrary.org/obo/ARO_3005438 PSV beta-lactamase PSV-1 is a PSV beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006979 RAHN-1 http://purl.obolibrary.org/obo/ARO_3005439 RAHN beta-lactamase RAHN-1 is a RAHN beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006980 RAHN-2 http://purl.obolibrary.org/obo/ARO_3005439 RAHN beta-lactamase RAHN-2 is a RAHN beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006981 RSA2-1 http://purl.obolibrary.org/obo/ARO_3005440 RSA2 beta-lactamase RSA2-1 is a RSA2 beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006982 RSD2-1 http://purl.obolibrary.org/obo/ARO_3005441 RSD2 beta-lactamase RSD2-1 is a RSD2 beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006983 RSD2-2 http://purl.obolibrary.org/obo/ARO_3005441 RSD2 beta-lactamase RSD2-2 is a RSD2 beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006984 RUB-1 http://purl.obolibrary.org/obo/ARO_3005442 RUB beta-lactamase RUB-1 is a RUB beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006985 SFC-1 http://purl.obolibrary.org/obo/ARO_3005443 SFC beta-lactamase SFC-1 is a SFC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006986 SFO-1 http://purl.obolibrary.org/obo/ARO_3005444 SFO beta-lactamase SFO-1 is a SFO beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006987 SGM-1 http://purl.obolibrary.org/obo/ARO_3005445 SGM beta-lactamase SGM-1 is a SGM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006988 SGM-2 http://purl.obolibrary.org/obo/ARO_3005445 SGM beta-lactamase SGM-2 is a SGM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006989 SGM-3 http://purl.obolibrary.org/obo/ARO_3005445 SGM beta-lactamase SGM-3 is a SGM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006990 SGM-4 http://purl.obolibrary.org/obo/ARO_3005445 SGM beta-lactamase SGM-4 is a SGM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006991 SGM-5 http://purl.obolibrary.org/obo/ARO_3005445 SGM beta-lactamase SGM-5 is a SGM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006992 SGM-6 http://purl.obolibrary.org/obo/ARO_3005445 SGM beta-lactamase SGM-6 is a SGM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006993 SGM-7 http://purl.obolibrary.org/obo/ARO_3005445 SGM beta-lactamase SGM-7 is a SGM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006994 SHN-1 http://purl.obolibrary.org/obo/ARO_3005446 SHN beta-lactamase SHN-1 is a SHN beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006995 SPN79-1 http://purl.obolibrary.org/obo/ARO_3005447 SPN79 beta-lactamase SPN79-1 is a SPN79 beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006996 SPR-1 http://purl.obolibrary.org/obo/ARO_3005448 SPR beta-lactamase SPR-1 is a SPR beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006997 SPS-1 http://purl.obolibrary.org/obo/ARO_3005449 SPS beta-lactamase SPS-1 is a SPS beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006998 SPU-1 http://purl.obolibrary.org/obo/ARO_3005450 SPU beta-lactamase SPU-1 is a SPU beta-lactamase. http://purl.obolibrary.org/obo/ARO_3006999 SST-1 http://purl.obolibrary.org/obo/ARO_3005451 SST beta-lactamase SST-1 is a SST beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007000 STA-1 http://purl.obolibrary.org/obo/ARO_3005452 STA beta-lactamase STA-1 is a STA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007001 TER-1 http://purl.obolibrary.org/obo/ARO_3005453 TER beta-lactamase TER-1 is a TER beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007002 TTU-1 http://purl.obolibrary.org/obo/ARO_3005454 TTU beta-lactamase TTU-1 is a TTU beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007003 VHH-1 http://purl.obolibrary.org/obo/ARO_3005455 VHH beta-lactamase VHH-1 is a VHH beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007004 VHW-1 http://purl.obolibrary.org/obo/ARO_3005456 VHW beta-lactamase VHW-1 is a VHW beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007005 YEM-1 http://purl.obolibrary.org/obo/ARO_3005457 YEM beta-lactamase YEM-1 is a YEM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007006 ZOG-1 http://purl.obolibrary.org/obo/ARO_3005458 ZOG beta-lactamase ZOG-1 is a ZOG beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007007 TER-2 http://purl.obolibrary.org/obo/ARO_3005453 TER beta-lactamase TER-2 is a TER beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007008 diazabicyclooctane http://purl.obolibrary.org/obo/ARO_3007128 serine beta-lactamase inhibitor A class of serine beta-lactamase inhibitors. http://purl.obolibrary.org/obo/ARO_3007009 ANT3310 http://purl.obolibrary.org/obo/ARO_3007008 diazabicyclooctane An experimental diazabicyclooctane beta-lactamase inhibitor that contains a fluorine atom in place of the carboxamide. http://purl.obolibrary.org/obo/ARO_2000005 stoichiometrically_homologous_to http://purl.obolibrary.org/obo/ARO_3009193 ARO relationship type Homology that is defined by similarity with regard to selected stoichiometrical parameters. http://purl.obolibrary.org/obo/ARO_2000006 structurally_homologous_to http://purl.obolibrary.org/obo/ARO_3009193 ARO relationship type Homology that is defined by similarity with regard to selected structural parameters. http://purl.obolibrary.org/obo/ARO_3009144 MexAB http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MexAB is a multidrug efflux pump complex consisting of Mex A and Mex B, two primary components. Forming the core transport machinery that can interface with various outer membrane proteins to expel antibiotics and toxic compounds, contributing to multidrug resistance. This component can be paired with OprM. http://purl.obolibrary.org/obo/ARO_3009145 MexCD http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MexCD is a multidrug efflux pump complex composed of Mex C and Mex D as its primary components. This system forms the central transport mechanism, capable of interacting with diverse outer membrane proteins to eject antibiotics and toxic substances, thus playing a significant role in multidrug resistance. http://purl.obolibrary.org/obo/ARO_3009146 MexEF http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MexEF is a multidrug efflux pump complex comprising MexE and MexF as its core components. This system functions as the primary transport mechanism, interacting with various outer membrane proteins to expel antibiotics and harmful compounds, thus contributing to multidrug resistance. http://purl.obolibrary.org/obo/ARO_3009153 MexHI-OpmD http://purl.obolibrary.org/obo/ARO_0010004 resistance-nodulation-cell division (RND) antibiotic efflux pump MexHI-OpmD is a multidrug efflux protein expressed in the Gram-negative Pseudomonas aeruginosa. MexH is the membrane fusion protein, MexI is the inner membrane resistance-nodulation-cell division (RND) transporter, and OpmD is the outer membrane factor protein. http://purl.obolibrary.org/obo/ARO_3009151 MexVW http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MexVW is a multidrug efflux pump complex composed of MexV and MexW as its main components. This system operates as a central transport mechanism, associating with outer membrane proteins to expel antibiotics and toxic compounds, thereby playing a role in multidrug resistance. http://purl.obolibrary.org/obo/ARO_3009152 MexXY http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MexXY is a multidrug efflux pump complex consisting of MexX and MexY as its core components. This system serves as a key transport mechanism, interacting with outer membrane proteins to expel antibiotics and toxic compounds, contributing to multidrug resistance. http://purl.obolibrary.org/obo/ARO_3009148 MexJK http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance The MexJK efflux pump system in Pseudomonas aeruginosa is unique in that it can function independently of an outer membrane protein (OMP), distinguishing it from many other efflux systems. MexJK is a multidrug efflux pump complex composed of MexJ and MexK as its primary components. This system serves as a core transport mechanism, working with outer membrane proteins to expel antibiotics and harmful compounds, thereby contributing to multidrug resistance. http://purl.obolibrary.org/obo/ARO_3009150 MexPQ http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MexPQ is a multidrug efflux pump complex comprising MexP and MexQ as its primary components. This system functions as a core transport mechanism, interacting with outer membrane proteins to expel antibiotics and toxic substances, contributing to multidrug resistance. http://purl.obolibrary.org/obo/ARO_3009149 MexMN http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MexMN is a multidrug efflux pump complex consisting of MexM and MexN as its main components. This system acts as a central transport mechanism, partnering with outer membrane proteins to expel antibiotics and toxic compounds, thereby playing a significant role in multidrug resistance. http://purl.obolibrary.org/obo/ARO_3009134 antifungal resistance-associated MSH2 http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant MSH2 is a mismatch repair gene in fungi. Strains with alterations in this gene exhibit the resistance to Polyenes (Amphotericin B), Echinocandins (Caspofungin, Micafungin), and Azoles (Fluconazole, Voriconazole). http://purl.obolibrary.org/obo/ARO_3009138 5-Fluorouracil http://purl.obolibrary.org/obo/ARO_3007560 pyrimidine antifungal drug 5-Fluorouracil (5FU) is an antimetabolite typically used as a cancer treatment and is cytotoxic. It is a pyrimidine analogue inhibits thymidylate synthase which halts the DNA synthesis. Its cytotoxic effects on eukaryotic cells have also allowed the drug to be explored for fungal infection treatment as well. http://purl.obolibrary.org/obo/ARO_3009154 napthoquinone antibiotics http://purl.obolibrary.org/obo/ARO_3005167 quinone with antibiotic activity Naphthoquinones constitute a class of organic compounds structurally related to naphthalene. http://purl.obolibrary.org/obo/ARO_3009155 atovaquone http://purl.obolibrary.org/obo/ARO_3009154 napthoquinone antibiotics Atovaquone is an antimicrobial medication for the prevention and treatment of Pneumocystis jirovecii pneumonia (PCP). It is a naphthoquinone compound having a 4-(4-chlorophenyl)cyclohexyl group at the 2-position and a hydroxy substituent at the 3-position. http://purl.obolibrary.org/obo/ARO_3009156 neutramycin http://purl.obolibrary.org/obo/ARO_0000000 macrolide antibiotic Neutramycin is a macrolide first identified from S. rimosus and S. luteoverticillatus. http://purl.obolibrary.org/obo/ARO_3009159 Bifonazole http://purl.obolibrary.org/obo/ARO_3007500 imidazole antibiotic Antifungal compound typically used to treat skin infections. http://purl.obolibrary.org/obo/ARO_3009160 5-fluorocytosine http://purl.obolibrary.org/obo/ARO_3000034 nucleoside antibiotic An antifungal compound that is converted into fluorouracil inside cells, thereby impairing the synthesis of proteins and DNA. This drug should almost always be used in combination with amphotericin B for systemic fungal infections, but the ratio is important since flucytosine can increase the toxicity of amphotericin B and vice versa. Flucytosine is typically indicated for Candida and Cryptococcus infections. http://purl.obolibrary.org/obo/ARO_3009162 Ravuconazole http://purl.obolibrary.org/obo/ARO_3007499 triazole antibiotic This compound is a small molecule antifungal drug with a maximum clinical trial phase of II. The compound inhibits 14a demethylase, an enzyme involved in sterol synthesis, resulting in lysis of the fungal cell wall and fungal cell death. http://purl.obolibrary.org/obo/ARO_3009169 triflumizole http://purl.obolibrary.org/obo/ARO_3007500 imidazole antibiotic This compound inhibits sterol 14alpha-demethylase and is used as a fungicide for the control of powdery mildew, scab and other diseases on a variety of crops. It is a member of the following groups: monochlorobenzenes, imidazoles, (trifluoromethyl)benzenes, carboxamidine, ether and conazoles. http://purl.obolibrary.org/obo/ARO_3009171 oxpoconazole http://purl.obolibrary.org/obo/ARO_3007500 imidazole antibiotic An agricultural fungicide that inhibits the pathway leading to the synthesis of ergosterol. http://purl.obolibrary.org/obo/ARO_3009172 arborcandin C http://purl.obolibrary.org/obo/ARO_3009165 antifungal without defined classification This compound inhibits 1,3-beta-glucan synthase in fungi (primarily yeasts), which is a major compound of cell wall synthesis. http://purl.obolibrary.org/obo/ARO_3009174 tolnaftate http://purl.obolibrary.org/obo/ARO_3009165 antifungal without defined classification Tolnaftate is a synthetic over-the-counter antifungal which may come as a cream, powder, spray or liquid aerosol typically used to treat jock itch, athlete's foot and ringworm. It is a monothiocarbamic ester that is the methyl(3-tolyl)carbamothioate ester of 2-naphthol. http://purl.obolibrary.org/obo/ARO_3009175 carbendazim http://purl.obolibrary.org/obo/ARO_3007500 imidazole antibiotic As a fungicide, carbendazim controls Ascomycetes, Fungi Imperfecti, and Basidiomycetes on a wide variety of crops. It also has a role as an antinematodal drug, a metabolite, a microtubule-destabilising agent. Carbendazim is a member of the class of benzimidazoles that is 2-aminobenzimidazole in which the primary amino group is substituted by a methoxycarbonyl group. It is a carbamate ester and a benzimidazolylcarbamate fungicide. It is functionally related to a 2-aminobenzimidazole. Additionally, Carbendazim has been used in cancer trials studying the treatment of Lymphoma and Unspecified Adult Solid Tumor, Protocol Specific. http://purl.obolibrary.org/obo/ARO_3009176 brefeldin A http://purl.obolibrary.org/obo/ARO_0000000 macrolide antibiotic A metabolite from Penicillium brefeldianum that exhibits a wide range of antibiotic activity, including antifungal functionality. It also has a role as a Penicillium metabolite. http://purl.obolibrary.org/obo/ARO_3009180 hexaconazole http://purl.obolibrary.org/obo/ARO_3007500 imidazole antibiotic An agricultural fungicide that is a systemic conazole (imidazole) fungicide used for the control of many seed-borne and soil-borne diseases and fungi particularly Ascomycetes and Basidiomycetes. It has a broad spectrum of action, being systemic with protective and curative action, but is known to disrupt membrane function. It also has a role as a chelator. It is a tertiary alcohol, a member of triazoles and a dichlorobenzene. In FungAMR, it was listed as having effects against Aspergillus fumigatus. It is commonly used in the control of apple, coffee and peanut diseases, but is also used for various other fruits and vegetables. Major consumption is in Asian countries and it is used mainly for the control of rice sheath blight in China, India, Vietnam, and parts of East Asia. It was introduced in the 1980s, it is not approved for use within the European Union. http://purl.obolibrary.org/obo/ARO_3009181 tebuconazole http://purl.obolibrary.org/obo/ARO_3007499 triazole antibiotic An agricultural fungicide that is a member of the triazole antifungal class. http://purl.obolibrary.org/obo/ARO_3009182 propiconazole http://purl.obolibrary.org/obo/ARO_3007499 triazole antibiotic A fungicide that is used commercially for agriculture. It is also used in combination with permethrin in formulations of wood preserver. The compound is known as a DMI, or demethylation inhibiting fungicide, due to its binding with and inhibition of the 14-alpha demethylase enzyme from demethylating a precursor to ergosterol. Without this demethylation step, the ergosterols are not incorporated into the growing fungal cell membranes, and cellular growth is stopped. http://purl.obolibrary.org/obo/ARO_3009183 tricyclazole http://purl.obolibrary.org/obo/ARO_3009165 antifungal without defined classification A fungicide used for the control of rice blast, it is not approved for use within the European Union. It has a role as a melanin synthesis inhibitor and an antifungal agrochemical. According to CHEBI, this compound is not a member of the azole group of antifungals, but is instead part of a group called the triazobenzothiazoles. http://purl.obolibrary.org/obo/ARO_3009184 mebendazole http://purl.obolibrary.org/obo/ARO_3009165 antifungal without defined classification Mebendazole has a role as an antinematodal drug, a tubulin modulator, and a fungal microtubule-destabilising agent. http://purl.obolibrary.org/obo/ARO_3009187 bromuconazole http://purl.obolibrary.org/obo/ARO_3007499 triazole antibiotic Bromuconazole is a member of the class of oxolanes and is a foliar applied conazole fungicide for a range of crops. It is a dichlorobenzene, an organobromine compound, a member of oxolanes, a member of triazoles, a conazole fungicide and a triazole fungicide. http://purl.obolibrary.org/obo/ARO_3009188 cyclohexamide http://purl.obolibrary.org/obo/ARO_3009165 antifungal without defined classification Cycloheximide appears as colorless crystals that can be used as a fungicide and as a anticancer drug. It is produced by the bacterium Streptomyces griseus and has a role as a bacterial metabolite, a protein synthesis inhibitor, a neuroprotective agent, an anticoronaviral agent and a ferroptosis inhibitor. It is a member of piperidones, a piperidine antibiotic, a fungicide, a dicarboximide, a secondary alcohol and a cyclic ketone. It is functionally related to a piperidine-2,6-dione. Cycloheximide can cause developmental toxicity. http://purl.obolibrary.org/obo/ARO_3009189 cyproconazole http://purl.obolibrary.org/obo/ARO_3007499 triazole antibiotic Cyproconazole is a fungicide that prevents wood decay from fungi in above-ground applications, but is not intended to protect trees in the ground. http://purl.obolibrary.org/obo/ARO_3009190 difenoconazole http://purl.obolibrary.org/obo/ARO_3007499 triazole antibiotic Difenoconazole is a broad spectrum fungicide with efficacy against some members of the Aschomycetes, Basidomycetes and Deuteromycetes families. It acts as a seed treatment, foliar spray and systemic fungicide. It is taken up through the surface of the infected plant and is translocated to all parts of the plant. It has a curative effect and a preventative effect. The mode of action of difenoconazole is that it is a sterol demethylation inhibitor which prevents the development of the fungus by inhibiting cell membrane ergosterol biosynthesis. http://purl.obolibrary.org/obo/ARO_3009191 epoxiconazole http://purl.obolibrary.org/obo/ARO_3007499 triazole antibiotic Epoxiconazole was introduced in 1990 as a broad-spectrum fungicide with long-lasting activity. Even though epoxiconazole is produced and commercialized as a racemic compound, not surprisingly, a recent publication indicates that the optically pure (2S,3R) enantiomer of epoxiconazole is much more active against pathogenic fungi than its (2R,3S)-enantiomer, whereas the plant growth regulatory activity mainly rests in the (2R,3S)-enantiomer. http://purl.obolibrary.org/obo/ARO_3009192 OXY-1-7 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase OXY-1-7 is a OXY family class A extended-spectrum beta-lactamase identified from Klebsiella oxytoca. http://purl.obolibrary.org/obo/ARO_3004851 Neisseria gonorrhoeae mtrR with mutation conferring resistance http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux MtrR is a repressor of mtrCDE efflux pump expression, point mutations in mtrR confer resistance to azithromycin and other drugs. http://purl.obolibrary.org/obo/ARO_3004852 SYN-1012 http://purl.obolibrary.org/obo/ARO_3007130 beta-lactam derived beta-lactamase inhibitor An experimental serine beta-lactamase inhibitor comparable to clavulanic acid, tazobactam and sulbactam. http://purl.obolibrary.org/obo/ARO_3004853 Mycobacterium tuberculosis 16S rRNA mutation conferring resistance to capreomycin http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in the 3' domain of 16S rRNA of Mycobacterium tuberculosis can confer resistance to capreomycin. http://purl.obolibrary.org/obo/ARO_3004854 CMY-136 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase A CMY-2-like beta-lactamase which confers resistance to cephalosporin antibiotics, and is also capable of hydrolyzing the CMY-2 inhibitors ticarcillin and cloxacillin. http://purl.obolibrary.org/obo/ARO_3004855 SCO beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase SCOs are Class A beta-lactamases that confer resistance to a narrow range of penams, with some minor activity on cephalosporins and carbapenems. http://purl.obolibrary.org/obo/ARO_3004856 SCO-1 http://purl.obolibrary.org/obo/ARO_3004855 SCO beta-lactamase Narrow-spectrum beta-lactamase isolated from several Acinetobacter spp. isolates from Argentina, as well as E. Coli. Hydrolyzes penicillins at a high level and cephalosporins and carbapenems at a very low level. http://purl.obolibrary.org/obo/ARO_3004858 Zoliflodacin http://purl.obolibrary.org/obo/ARO_3007160 zoliflodacin-like antibiotic Experimental antibiotic in phase two trial for Neisseria gonorrhoeae treatment. http://purl.obolibrary.org/obo/ARO_3004859 Neisseria gonorrhoeae gyrB conferring resistance to zoliflodacin http://purl.obolibrary.org/obo/ARO_3005000 Zoliflodacin resistant gyrB Point mutation in Neisseria gonorrhoea gyrase B decreases affinity to zoliflodacin antibiotic. http://purl.obolibrary.org/obo/ARO_3004860 Burkholderia dolosa gyrA conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3003292 fluoroquinolone resistant gyrA Point mutations in Burkholderia gyrA that confer resistance to ciprofloxacin, a fluoroquinolone antibiotic. http://purl.obolibrary.org/obo/ARO_3004861 NDM-18 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase A class B New Delhi metallo-beta-lactamase and NDM-1 variant. http://purl.obolibrary.org/obo/ARO_3004862 NDM-19 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase A class B New Delhi metallo-beta-lactamase and NDM-1 variant. http://purl.obolibrary.org/obo/ARO_3004863 NDM-20 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase A class B New Delhi metallo-beta-lactamase. http://purl.obolibrary.org/obo/ARO_3004864 NDM-21 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase A class B New Delhi metallo-beta-lactamase and NDM-1 variant. http://purl.obolibrary.org/obo/ARO_3004865 NDM-22 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase A class B New Delhi metallo-beta-lactamase and NDM-1 variant. http://purl.obolibrary.org/obo/ARO_3004866 NDM-23 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase A class B New Delhi metallo-beta-lactamase. http://purl.obolibrary.org/obo/ARO_3004867 NDM-24 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase A class B New Delhi metallo-beta-lactamase. http://purl.obolibrary.org/obo/ARO_3004868 NDM-25 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase A class B New Delhi metallo-beta-lactamase. http://purl.obolibrary.org/obo/ARO_3004869 NDM-26 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase A class B New Delhi metallo-beta-lactamase and NDM-1 variant. http://purl.obolibrary.org/obo/ARO_3004870 NDM-27 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase A class B New Delhi metallo-beta-lactamase and NDM-1 variant. http://purl.obolibrary.org/obo/ARO_3004871 NDM-28 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase A class B New Delhi metallo-beta-lactamase and NDM-1 variant. http://purl.obolibrary.org/obo/ARO_3004873 Neisseria gonorrhoeae folP with mutation conferring resistance to sulfonamides http://purl.obolibrary.org/obo/ARO_3003415 sulfonamide resistant dihydropteroate synthase folP Point mutations in Neisseria gonorrhoeae dihydropteroate synthase folP prevent sulfonamide antibiotics from inhibiting its role in folate synthesis, thus conferring sulfonamide resistance. http://purl.obolibrary.org/obo/ARO_3004874 isoniazid resistant inhA http://purl.obolibrary.org/obo/ARO_3003417 antibiotic resistant inhA Genes with mutations in inhA which confer resistance to isoniazid class antibiotics. http://purl.obolibrary.org/obo/ARO_3004875 inhA with mutations with conferring resistance to ethionamide http://purl.obolibrary.org/obo/ARO_3003417 antibiotic resistant inhA Genes with mutations in inhA which confer resistance to ethionamide class antibiotics. http://purl.obolibrary.org/obo/ARO_3004876 Mycobacterium tuberculosis inhA mutations conferring resistance to ethionamide http://purl.obolibrary.org/obo/ARO_3004875 inhA with mutations with conferring resistance to ethionamide inhA is a enoyl-acyl carrier reductase used in lipid metabolism and farry acid biosynthesis. It is inhibited by ethionamide. Mutations in the promoter region or multiple copies of the inhA show marked resistance to ethionamide mediated inhibition of mycolic acid biosynthesis. http://purl.obolibrary.org/obo/ARO_3004877 antibiotic resistant clpC1 http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations that occur in the clp protease subunit clpC1 that increases resistance to antibiotics. http://purl.obolibrary.org/obo/ARO_3004878 pyrazinamide resistant clpC1 http://purl.obolibrary.org/obo/ARO_3004877 antibiotic resistant clpC1 clpC1 is a subunit of the clp protease that is ATP-dependent. It functions to direct the clp protease to specific substrates. In the presence of ATP it hydrolyses proteins and may be involved in the degradation of denatured proteins. http://purl.obolibrary.org/obo/ARO_3004879 antibiotic resistant gpsI http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations that occur in gpsI that increases resistance to antibiotics. http://purl.obolibrary.org/obo/ARO_3004880 pyrazinamide resistant gpsI http://purl.obolibrary.org/obo/ARO_3004879 antibiotic resistant gpsI gpsI codes for polyribonucleotide nucleotidyltransferase which is a protein involved in mRNA degradation. It catalyzes the phosphorolysis of single-stranded polyribonucleotides in the 3'- to 5'-direction. http://purl.obolibrary.org/obo/ARO_3004881 antibiotic resistant mas http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations that occur in the mas that increases resistance to antibiotics. http://purl.obolibrary.org/obo/ARO_3004882 pyrazinamide resistant mas http://purl.obolibrary.org/obo/ARO_3004881 antibiotic resistant mas Mas is a multifunctional mycocerosic acid synthase membrane-associated mas. It catalyzes the elongation of N-fatty acyl-CoA with methylamalonyl-CoA as the elongating agent to form mycocerosyl fatty acids present in mycobacterium. http://purl.obolibrary.org/obo/ARO_3004883 antibiotic resistant ppsC http://purl.obolibrary.org/obo/ARO_3005002 antibiotic resistant polyketide synthase genes Mutations that occur in the ppsC that increases resistance to antibiotics. http://purl.obolibrary.org/obo/ARO_3004884 pyrazinamide resistant ppsC http://purl.obolibrary.org/obo/ARO_3004883 antibiotic resistant ppsC ppsC codes for the phthiocerol synthesis polyketide synthase type 1. It is involved in the elongation of C22-24 fatty acids by the addition of methylmalonyl-CoA extender units to yield phthiocerol derivatives in a complete reduction. Research has pointed towards this protein to be a high confidence drug target. http://purl.obolibrary.org/obo/ARO_3004885 antibiotic resistant ppsD http://purl.obolibrary.org/obo/ARO_3005002 antibiotic resistant polyketide synthase genes Mutations that occur in the ppsD that increases resistance to antibiotics. http://purl.obolibrary.org/obo/ARO_3004886 pyrazinamide resistant ppsD http://purl.obolibrary.org/obo/ARO_3004885 antibiotic resistant ppsD ppsD codes for the phthiocerol synthesis polyketide synthase type 1. It is involved in the elongation of C22-24 fatty acids by the addition of malonyl-CoA extender units to yield phthiocerol derivatives in a partial reduction. http://purl.obolibrary.org/obo/ARO_3004887 antibiotic resistant fabG1 http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations that occur in the fabg1 gene resulting in the inability for the antibiotic to inhibit mycolic acid biosynthesis. http://purl.obolibrary.org/obo/ARO_3004888 ethionamide resistant fabG1 http://purl.obolibrary.org/obo/ARO_3004887 antibiotic resistant fabG1 fabG1 is involved in the fatty acid synthesis pathway, acting in the first reduction step for mycolic acid. It is associated with ethionamide resistance. http://purl.obolibrary.org/obo/ARO_3004889 antibiotic resistant mshC http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations that occur on the mshC gene resulting in the inability for antibiotic to function. http://purl.obolibrary.org/obo/ARO_3004890 ethionamide resistant mshC http://purl.obolibrary.org/obo/ARO_3004889 antibiotic resistant mshC Mutations that occur in mshC which is involved in the third step of mycothiol biosynthesis. It catalyzes the ATP-dependent condensation of GlcN-Ins and L-cysteine to form L-Cys-GlcN-Ins. The gene exhibits resistance to ethionamide. http://purl.obolibrary.org/obo/ARO_3004891 antibiotic resistant nudC http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations that occur on the nudC gene resulting in the inability for antibiotic to function. http://purl.obolibrary.org/obo/ARO_3004892 ethionamide resistant nudC http://purl.obolibrary.org/obo/ARO_3004891 antibiotic resistant nudC nudC is a NADH pyrophosphatase that is involved in nicotinate and nicotinamide metabolism. Mutations that occur on the nudC gene resulting in the inability for ethionamide to function. http://purl.obolibrary.org/obo/ARO_3004893 antibiotic resistant ahpC http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations in ahpC that contribute to antibiotic resistance by preventing ahpC from activating antibiotics. http://purl.obolibrary.org/obo/ARO_3004894 Isoniazid resistant ahpC http://purl.obolibrary.org/obo/ARO_3004893 antibiotic resistant ahpC An alkyl hydroperoxide reductase that catalyzes the reduction of organic hydrogen peroxide to water and organic alcohols. Plays a role in protecting oxidative stress. http://purl.obolibrary.org/obo/ARO_3004895 isoniazid resistant fabG1 http://purl.obolibrary.org/obo/ARO_3004887 antibiotic resistant fabG1 fabG1 is involved in the fatty acid synthesis pathway, acting in the first reduction step for mycolic acid. It is associated with isoniazid resistance. http://purl.obolibrary.org/obo/ARO_3004896 antibiotic resistant furA http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations that occur in furA which is in the regulatory region of katG. Mutations within the gene contribute to antibiotic resistance. http://purl.obolibrary.org/obo/ARO_3004897 isoniazid resistant furA http://purl.obolibrary.org/obo/ARO_3004896 antibiotic resistant furA Transcriptional regulator furA, represses the transcription of the catalase-peroxidase gene katG and its own transcription by binding to the promoter region. http://purl.obolibrary.org/obo/ARO_3004898 antibiotic resistant inbR http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations in inbR that contribute to antibiotic resistance by preventing antibiotic activation. http://purl.obolibrary.org/obo/ARO_3004899 isoniazid resistant inbR http://purl.obolibrary.org/obo/ARO_3004898 antibiotic resistant inbR inbR is part of the transcriptional factor family TetR. It acts as a repressor to regulate efflux pumps involved in antibiotic resistance. http://purl.obolibrary.org/obo/ARO_3004900 antibiotic resistant mshA http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations that occur in the mshA gene resulting in the inability for antibiotic to activate. http://purl.obolibrary.org/obo/ARO_3004901 isoniazid resistant mshA http://purl.obolibrary.org/obo/ARO_3004900 antibiotic resistant mshA mshA is a glycosyltransferase and is involved in the first step of mycothiol biosynthesis. This is a step that is required for growth in mycobacterium tuberculosis. Resistance has been shown in the gene to isoniazid. http://purl.obolibrary.org/obo/ARO_3004902 antibiotic resistant mshB http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations that occur in the mshB gene that results in antibiotic resistance. http://purl.obolibrary.org/obo/ARO_3004903 isoniazid resistant mshB http://purl.obolibrary.org/obo/ARO_3004902 antibiotic resistant mshB mshB is a deacetylase that is involved in the second step of mycothiol synthesis. GlcNAc-Ins is deacetylated by MshB to produce GlcN-Ins. http://purl.obolibrary.org/obo/ARO_3004904 isoniazid resistant mshC http://purl.obolibrary.org/obo/ARO_3004889 antibiotic resistant mshC Mutations that occur on the mshC gene resulting in the inability for isoniazid to function. It catalyzes the ATP-dependent condensation of GlcN-Ins and L-cysteine to form L-Cys-GlcN-Ins. http://purl.obolibrary.org/obo/ARO_3004905 antibiotic resistant mymA http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations that occur within the coding region of mymA that prevent effective antibiotic function. http://purl.obolibrary.org/obo/ARO_3004906 isoniazid resistant mymA http://purl.obolibrary.org/obo/ARO_3004905 antibiotic resistant mymA mymA is an operon that begins at Rv3083 and ends at Rv3089 and is required for maintaining the appropriate mycolic acid composition and permeability of the envelope on its exposure to acidic pH. It has shown to be resistant to isoniazid. http://purl.obolibrary.org/obo/ARO_3004907 antibiotic resistant mmaA3 http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations that occur in mmaA3 which decreases effective functioning of antibiotics. http://purl.obolibrary.org/obo/ARO_3004908 isoniazid resistant mmaA3 http://purl.obolibrary.org/obo/ARO_3004907 antibiotic resistant mmaA3 Methoxy mycolic acid synthase 3 is involved in the modification of mycolic acids. It represents a major part of the mycobacterial cell wall complex. http://purl.obolibrary.org/obo/ARO_3004909 Antibiotic resistant nat http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations that occur in nat inactivate antibiotic functioning and contribute to antibiotic resistance. http://purl.obolibrary.org/obo/ARO_3004910 isoniazid resistant nat http://purl.obolibrary.org/obo/ARO_3004909 Antibiotic resistant nat Arylamine N-acetyltransferase catalyzes the transfer of the acetyl group from acetyl coenzyme A to the free amino group of arylamines and hydrazines. Reports have shown that overexpression of this enzyme may be responsible for increased resistance to isoniazid. http://purl.obolibrary.org/obo/ARO_3004911 isoniazid resistant nudC http://purl.obolibrary.org/obo/ARO_3004891 antibiotic resistant nudC nudC is a NADH pyrophosphatase that is involved in nicotinate and nicotinamide metabolism. Mutations that occur on the nudC gene resulting in the inability for isoniazid to function. http://purl.obolibrary.org/obo/ARO_3004912 antibiotic resistant sigI http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations that occur in SigI sigma factor that increase resistance to antibiotics. http://purl.obolibrary.org/obo/ARO_3004913 isoniazid resistant sigI http://purl.obolibrary.org/obo/ARO_3004912 antibiotic resistant sigI A sigma factor that acts as an initiation factor that promotes attachment of the RNA polymerase to specific initiation sites and then is released. Transcriptional analyses indicate that katG is also regulated by the sigma factor sigl and indicate resistance to isoniaizd. http://purl.obolibrary.org/obo/ARO_3004915 fluoroquinolone-resistant ESX5 secretion system http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant ESX-5 secretion system is are important for virulence of mycobacteria and is required for mycobacterial cell wall stability and host cell lysis. The system is comprised of genes that encode the structural components of the secretion system. The system secrets mycobacterial proteins involved in virulence and pathogenicity and important for mycobacterium viability. Resistance has been shown to specific antibiotics. http://purl.obolibrary.org/obo/ARO_3004916 subunits of secretion system conferring antibiotic resistance http://purl.obolibrary.org/obo/ARO_3000000 determinant of antibiotic resistance Subunits of the secretion system complex that secretes proteins that contribute to resistance. http://purl.obolibrary.org/obo/ARO_3004917 fluoroquinolone resistant eccB5 http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations in the eccB5 gene contributing to antibiotic resistance to fluoroquinolone. http://purl.obolibrary.org/obo/ARO_3004918 Mycobacterium tuberculosis eccB5 conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3004917 fluoroquinolone resistant eccB5 eccB5 is a transmembrane protein within the ESX-5 secretion system complex. The complex is critical for mycobacterium viability and virulence in the host cell and mutations contribute to a decreased uptake of antibiotic in the outer membrane. http://purl.obolibrary.org/obo/ARO_3004919 Mycobacterium tuberculosis eccC5 conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3004920 fluoroquinolone resistant eccC5 eccC5 is a membrane-bound ATPase within the ESX-5 secretion system complex. The complex is critical for mycobacterium viability and virulence in the host cell and mutations contribute to a decreased uptake of antibiotic in the outer membrane, yet the Relational Sequencing Tuberculosis Data platform (ReSeqTB, https://platform.reseqtb.org) finds no evidence of an association between eccC5 mutations and drug resistance. http://purl.obolibrary.org/obo/ARO_3004920 fluoroquinolone resistant eccC5 http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations in the eccC5 gene contributing to antibiotic resistance to fluoroquinolone. http://purl.obolibrary.org/obo/ARO_3004921 Mycobacterium tuberculosis ahpC mutations confer resistance to isoniazid http://purl.obolibrary.org/obo/ARO_3004894 Isoniazid resistant ahpC Mutations that occur in ahpC that result in ahpC overexpression thus conferring or contributing to resistance to isoniazid. http://purl.obolibrary.org/obo/ARO_3004922 Mycobacterium tuberculosis fabG1 mutations confer resistance to isoniazid http://purl.obolibrary.org/obo/ARO_3004895 isoniazid resistant fabG1 Mutations that occur in fabG1 resulting in or contributing to resistance in isoniazid. http://purl.obolibrary.org/obo/ARO_3004923 Mycobacterium tuberculosis furA mutations confer resistance to isoniazid http://purl.obolibrary.org/obo/ARO_3004897 isoniazid resistant furA Mutations that occur in furA that result in or contribute to antibiotic resistance to isoniazid. http://purl.obolibrary.org/obo/ARO_3004924 Mycobacterium tuberculosis inbR mutations conferring resistance to isoniazid http://purl.obolibrary.org/obo/ARO_3004899 isoniazid resistant inbR Mutations that occur in inbR that result in or contribute to antibiotic resistance to isoniazid. http://purl.obolibrary.org/obo/ARO_3004925 Mycobacterium tuberculosis mshA mutations conferring resistance to isoniazid http://purl.obolibrary.org/obo/ARO_3004901 isoniazid resistant mshA Mutations that occur in Mycobacterium tuberculosis mshA that result in or contribute to antibiotic resistance to isoniazid. http://purl.obolibrary.org/obo/ARO_3004927 Mycobacterium tuberculosis mshC mutations conferring resistance to isoniazid http://purl.obolibrary.org/obo/ARO_3004904 isoniazid resistant mshC Mutations that occur in mshC that result in or contribute to antibiotic resistance to isoniazid. http://purl.obolibrary.org/obo/ARO_3004928 Mycobacterium tuberculosis mymA mutations conferring resistance to isoniazid http://purl.obolibrary.org/obo/ARO_3004906 isoniazid resistant mymA Mutations that occur in the mymA operon that result in or contribute to antibiotic resistance to isoniazid. http://purl.obolibrary.org/obo/ARO_3004929 Mycobacterium tuberculosis mmaA3 mutations conferring resistance to isoniazid http://purl.obolibrary.org/obo/ARO_3004908 isoniazid resistant mmaA3 Mutations that occur in mmaA3 that result in or contribute to antibiotic resistance to isoniazid. http://purl.obolibrary.org/obo/ARO_3004930 Mycobacterium tuberculosis nat mutations conferring resistance to isoniazid http://purl.obolibrary.org/obo/ARO_3004910 isoniazid resistant nat Mutations that occur in nat which through overexpression of the enzyme can result in or contribute to antibiotic resistance to isoniazid. http://purl.obolibrary.org/obo/ARO_3004931 Mycobacterium tuberculosis nudC mutations conferring resistance to isoniazid http://purl.obolibrary.org/obo/ARO_3004911 isoniazid resistant nudC Mutations that occur in nudC which through overexpression of the enzyme can result in or contribute to antibiotic resistance to isoniazid. http://purl.obolibrary.org/obo/ARO_3004932 Mycobacterium tuberculosis sigI mutations conferring resistance to isoniazid http://purl.obolibrary.org/obo/ARO_3004913 isoniazid resistant sigI Mycobacterium tuberculosis sigI mutations conferring resistance to isoniazid. http://purl.obolibrary.org/obo/ARO_3004933 Mycobacterium tuberculosis fabG1 mutation conferring resistance to ethionamide http://purl.obolibrary.org/obo/ARO_3004888 ethionamide resistant fabG1 Mutations that occur in Mycobacterium tuberculosis fabG1 resulting in or contributing to resistance in ethionamide. http://purl.obolibrary.org/obo/ARO_3004934 Mycobacterium tuberculosis mshC mutations conferring resistance to ethionamide http://purl.obolibrary.org/obo/ARO_3004890 ethionamide resistant mshC Mutations that occur in mshC resulting in or contributing to conferring resistance to ethionamide. http://purl.obolibrary.org/obo/ARO_3004935 Mycobacterium tuberculosis nudC mutations conferring resistance to ethionamide http://purl.obolibrary.org/obo/ARO_3004892 ethionamide resistant nudC Mutations that occur in nudC resulting in or contributing to conferring resistance to ethionamide. http://purl.obolibrary.org/obo/ARO_3004936 23s rRNA with mutation conferring resistance to aminoglycoside antibiotics http://purl.obolibrary.org/obo/ARO_3000336 23S rRNA with mutation conferring antibiotic resistance Point mutations in the 23S rRNA of bacteria can confer resistance to aminoglycosides. http://purl.obolibrary.org/obo/ARO_3004937 Mycobacterium tuberculosis 23S rRNA mutation conferring resistance to capreomycin http://purl.obolibrary.org/obo/ARO_3004936 23s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in 23S rRNA of Mycobacterium tuberculosis can confer resistance to capreomycin. http://purl.obolibrary.org/obo/ARO_3004938 antibiotic resistant ddlA http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations in the D-alanine synthase of Mycobacterium tuberculosis can confer resistance to antibiotics. http://purl.obolibrary.org/obo/ARO_3004939 cycloserine resistant ddlA http://purl.obolibrary.org/obo/ARO_3004938 antibiotic resistant ddlA ddlA catalyzes the ATP-driven ligation of two D-alanine molecules to form the D-alanyl-D-alanine dipeptide, key in forming the cell wall. Cycloserine has a similar structure to d-alanine and inhibits the growth of the cell wall. http://purl.obolibrary.org/obo/ARO_3004941 Mycobacterium tuberculosis ddlA mutations confer resistance to cycloserine http://purl.obolibrary.org/obo/ARO_3004939 cycloserine resistant ddlA Point mutations that occur within Mycobacterium tuberculosis ddlA gene resulting in resistance to cycloserine. http://purl.obolibrary.org/obo/ARO_3004942 antibiotic resistant ald http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations that occur in ald which decreases effective functioning of antibiotics. http://purl.obolibrary.org/obo/ARO_3004943 cycloserine resistant ald http://purl.obolibrary.org/obo/ARO_3004942 antibiotic resistant ald ald plays a role in cell wall synthesis as L-alanine is an important constituent of the peptidoglycan layer. Resistance due to mutations in ald can cause cycloserine to not function. http://purl.obolibrary.org/obo/ARO_3004944 antibiotic resistant alr http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations that occur in alr which decreases effective functioning of antibiotics. http://purl.obolibrary.org/obo/ARO_3004945 Mycobacterium tuberculosis ald mutations confer resistance to cycloserine http://purl.obolibrary.org/obo/ARO_3004943 cycloserine resistant ald Mutations in the ald gene that contribute to or confer resistance to cycloserine. http://purl.obolibrary.org/obo/ARO_3004946 cycloserine resistant alr http://purl.obolibrary.org/obo/ARO_3004944 antibiotic resistant alr Provides the D-alanine required for cell wall biosynthesis. Transforms L-alanine to D-alanine. Can confer resistance to cycloserine. http://purl.obolibrary.org/obo/ARO_3004947 Mycobacterium tuberculosis alr with mutation conferring resistance to cycloserine http://purl.obolibrary.org/obo/ARO_3004946 cycloserine resistant alr Mutations in the alr mutation contribute to or confer resistance to cycloserine. http://purl.obolibrary.org/obo/ARO_3004948 antibiotic resistant ubiA http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Decaprenylphosphoryl-5-phosphoribose (DPPR) synthase involved in arabinogalactan synthesis. http://purl.obolibrary.org/obo/ARO_3004949 ethambutol resistant ubiA http://purl.obolibrary.org/obo/ARO_3004948 antibiotic resistant ubiA DDPR synthase involved in arabinogalactan synthesis. Mutations can confer resistance to ethambutol. http://purl.obolibrary.org/obo/ARO_3004950 Mycobacterium tuberculosis ubiA mutations confer resistance to ethambutol http://purl.obolibrary.org/obo/ARO_3004949 ethambutol resistant ubiA Mutations in the ubiA gene contribute to or confer resistance to ethambutol. http://purl.obolibrary.org/obo/ARO_3004951 Mycobacterium tuberculosis aftA mutations confer resistance to ethambutol http://purl.obolibrary.org/obo/ARO_3002876 ethambutol resistant aftA Mutations in aftA gene contribute to or confer resistance to ethamutol. http://purl.obolibrary.org/obo/ARO_3004952 thioacetazone http://purl.obolibrary.org/obo/ARO_3007161 thiosemicarbazone antibiotic Thioacetazone is an inexpensive, antitubercular, bacteriostatic drug that has been widely used in combination with isoniazid in Africa and South America. This drug is rarely in use. http://purl.obolibrary.org/obo/ARO_3004953 antibiotic resistant Rv0565c http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Rv0565c is a bacterial monoxygenase that has been newly uncovered in recent literature to show resistance to antibiotic. http://purl.obolibrary.org/obo/ARO_3004954 Ethionamide resistant Rv0565c http://purl.obolibrary.org/obo/ARO_3004953 antibiotic resistant Rv0565c Mycobacterial monoxygenase has been shown to confer resistance to ethionamide in recent literature. http://purl.obolibrary.org/obo/ARO_3004955 Mycobacterium tuberculosis Rv0565c mutation conferring resistance to ethionamide http://purl.obolibrary.org/obo/ARO_3004954 Ethionamide resistant Rv0565c Mutations in a bacterial monooxygenase, Rv0565c, are significantly associated with ethionamide resistance as an activator of ethionamide. http://purl.obolibrary.org/obo/ARO_3004956 Neisseria gonorrhoeae rpld http://purl.obolibrary.org/obo/ARO_3005001 50S rRNA with mutation conferring resistance to macrolide antibiotics rpld encodes for the 50S L4 ribosomal protein, is a macrolide resistance protein identified in Neisseria gonorrhoeae. http://purl.obolibrary.org/obo/ARO_3004957 Mycobacterium tuberculosis clpC1 with mutation conferring resistance to pyrazinamide http://purl.obolibrary.org/obo/ARO_3004878 pyrazinamide resistant clpC1 Mutations that occur in clpC1 that result in or contribute to antibiotic resistance to pyrazinamide. http://purl.obolibrary.org/obo/ARO_3004958 antibiotic resistant ponA1 http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant A probable bifunctional penicillin-binding protein that is involved in the final stages of peptidoglycan synthesis. It has been shown to cause resistance to antibiotics. http://purl.obolibrary.org/obo/ARO_3004959 rifamycin resistant ponA1 http://purl.obolibrary.org/obo/ARO_3004958 antibiotic resistant ponA1 Mutations in the ponA1 gene that can contribute to or confer resistance to rifamycin-class antibiotics. http://purl.obolibrary.org/obo/ARO_3004960 Mycobacterium tuberculosis ponA1 mutations conferring resistance to rifabutin http://purl.obolibrary.org/obo/ARO_3004959 rifamycin resistant ponA1 Mutations in ponA1 that contribute to or confer resistance to rifabutin antibiotic. http://purl.obolibrary.org/obo/ARO_3004961 antibiotic resistant eis http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations in the eis gene that can contribute to antibiotic resistance. http://purl.obolibrary.org/obo/ARO_3004962 kanamycin resistant eis http://purl.obolibrary.org/obo/ARO_3004961 antibiotic resistant eis Involved in acetylation and intracellular survival. Associated with the cell surface and secretion proteins. http://purl.obolibrary.org/obo/ARO_3004963 Mycobacterium tuberculosis eis mutations confer resistance to kanamycin http://purl.obolibrary.org/obo/ARO_3004962 kanamycin resistant eis Mutations in eis that contribute to or confer resistance to kanamycin. http://purl.obolibrary.org/obo/ARO_3004964 antibiotic resistant whib7 http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations in the whib7 gene that cause antibiotic resistance. http://purl.obolibrary.org/obo/ARO_3004965 streptomycin resistant whib7 http://purl.obolibrary.org/obo/ARO_3004964 antibiotic resistant whib7 A protein involved in transcriptional mechanisms. Mutations in the gene can cause resistance to streptomycin. http://purl.obolibrary.org/obo/ARO_3004966 Kanamycin resistant whib7 http://purl.obolibrary.org/obo/ARO_3004964 antibiotic resistant whib7 whib7 is a protein involved in transcriptional mechanisms. Mutations in the gene can cause resistance to kanamycin. http://purl.obolibrary.org/obo/ARO_3004967 Mycobacterium tuberculosis whib7 mutations confer resistance to kanamycin http://purl.obolibrary.org/obo/ARO_3004966 Kanamycin resistant whib7 Mutations in whib7 that can contribute to or confer resistance to kanamycin. http://purl.obolibrary.org/obo/ARO_3004968 Mycobacterium tuberculosis whib7 mutation conferring resistance to streptomycin http://purl.obolibrary.org/obo/ARO_3004965 streptomycin resistant whib7 Mutations in whib7 that can contribute to or confer resistance to streptomycin. http://purl.obolibrary.org/obo/ARO_3004970 streptomycin resistant Rv1258c http://purl.obolibrary.org/obo/ARO_3007183 antibiotic resistant Rv1258c An efflux pump in mycobacterium that contributes to intrinsic antibiotic resistance. The pump uses the electrochemical gradient as a source of energy. http://purl.obolibrary.org/obo/ARO_3004971 Mycobacterium tuberculosis Rv1258c mutations confer resistance to streptomycin http://purl.obolibrary.org/obo/ARO_3004970 streptomycin resistant Rv1258c Mutations in the Rv1258c (Tap) gene that can contribute to or confer resistance to streptomycin. http://purl.obolibrary.org/obo/ARO_3004972 antibiotic resistant ppsA http://purl.obolibrary.org/obo/ARO_3005002 antibiotic resistant polyketide synthase genes Mutations in ppsA can result in antibiotic resistance. http://purl.obolibrary.org/obo/ARO_3004973 pyrazinamide resistant ppsA http://purl.obolibrary.org/obo/ARO_3004972 antibiotic resistant ppsA Involved in the elongation of either C22-24 fatty acids by the addition of malonyl-CoA and methylmalonyl-CoA extender units to yield phthiocerol derivatives. Mutations in the gene may confer resistance to pyrazinamide. http://purl.obolibrary.org/obo/ARO_3004975 Mycobacterium tuberculosis ppsC mutations confer resistance to pyrazinamide http://purl.obolibrary.org/obo/ARO_3004884 pyrazinamide resistant ppsC Mutations in ppsC can contribute to or confer resistance to pyrazinamide. http://purl.obolibrary.org/obo/ARO_3004976 Mycobacterium tuberculosis ppsD mutations confer resistance to pyrazinamide http://purl.obolibrary.org/obo/ARO_3004886 pyrazinamide resistant ppsD Mutations in ppsD can contribute to or confer resistance to pyrazinamide. http://purl.obolibrary.org/obo/ARO_3004977 Mycobacterium tuberculosis gpsI with mutations conferring resistance to pyrazinamide http://purl.obolibrary.org/obo/ARO_3004880 pyrazinamide resistant gpsI Mutations in gpsI that can contribute to or confer resistance to pyrazinamide. http://purl.obolibrary.org/obo/ARO_3004978 Mycobacterium tuberculosis mas mutations confer resistance to pyrazinamide http://purl.obolibrary.org/obo/ARO_3004882 pyrazinamide resistant mas Mutations in mas that can contribute to or confer resistance to pyrazinamide. http://purl.obolibrary.org/obo/ARO_3004979 antibiotic resistant Rv0191 http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations in the gene can contribute to antibiotic resistance. http://purl.obolibrary.org/obo/ARO_3004980 pyrazinamide resistant Rv0191 http://purl.obolibrary.org/obo/ARO_3004979 antibiotic resistant Rv0191 A probable conserved integral membrane protein that acts as an active efflux pump. Overexpression causes pyrazinamide resistance. http://purl.obolibrary.org/obo/ARO_3004981 Mycobacterium tuberculosis Rv0191 mutations confer resistance to pyrazinamide http://purl.obolibrary.org/obo/ARO_3004980 pyrazinamide resistant Rv0191 Mutations in the Rv0191 gene contribute to or confer resistance to pyrazinamide. http://purl.obolibrary.org/obo/ARO_3004982 antibiotic resistant Rv1667 http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations in the Rv1667 gene can contribute or confer resistance to antibiotics. http://purl.obolibrary.org/obo/ARO_3004983 pyrazinamide resistant Rv1667 http://purl.obolibrary.org/obo/ARO_3004982 antibiotic resistant Rv1667 A probable transport protein thought to be involved in the active transport of macrolide across the membrane in mycobacterium. http://purl.obolibrary.org/obo/ARO_3004984 Mycobacterium tuberculosis Rv1667 mutations confer resistance to pyrazinamide http://purl.obolibrary.org/obo/ARO_3004983 pyrazinamide resistant Rv1667 Mutations in the Rv1667 gene that can contribute to or confer resistance to pyrazinamide. Resistance may be due to an antibiotic export mechanism. http://purl.obolibrary.org/obo/ARO_3004985 antibiotic resistant Rv2731 http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations in the Rv2731 gene that contribute to antibiotic resistance. http://purl.obolibrary.org/obo/ARO_3004986 pyrazinamide resistant Rv2731 http://purl.obolibrary.org/obo/ARO_3004985 antibiotic resistant Rv2731 A conserved alanine and arginine-rich protein with an unknown function. The protein has shown to contribute to or confer resistance to pyrazinamide. http://purl.obolibrary.org/obo/ARO_3004987 Mycobacterium tuberculosis Rv2731 mutations confer resistance to pyrazinamide http://purl.obolibrary.org/obo/ARO_3004986 pyrazinamide resistant Rv2731 Mutations in the Rv2731 gene that contribute to or confer resistance to pyrazinamide. http://purl.obolibrary.org/obo/ARO_3004988 antibiotic resistant Rv3008 http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations in Rv3008 can contribute to or confer resistance to antibiotics. http://purl.obolibrary.org/obo/ARO_3004989 pyrazinamide resistant Rv3008 http://purl.obolibrary.org/obo/ARO_3004988 antibiotic resistant Rv3008 A hypothetical protein for which it has been predicted but no experimental evidence exists to determine its function. May contribute to pyrazinamide resistance. http://purl.obolibrary.org/obo/ARO_3004991 antibiotic resistant Rv3169 http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations in the Rv3169 gene contribute to or confer resistance to antibiotics. http://purl.obolibrary.org/obo/ARO_3004992 pyrazinamide resistant Rv3169 http://purl.obolibrary.org/obo/ARO_3004991 antibiotic resistant Rv3169 A conserved protein with an unknown function determined through proteomics study. May contribute or confer resistance to pyrazinamide resistance. http://purl.obolibrary.org/obo/ARO_3004993 Mycobacterium tuberculosis Rv3169 mutations confer resistance to pyrazinamide http://purl.obolibrary.org/obo/ARO_3004992 pyrazinamide resistant Rv3169 Mutations in the Rv3169 gene that can contribute to or confer resistance to pyrazinamide resistance. http://purl.obolibrary.org/obo/ARO_3004994 Mycobacterium tuberculosis rpoC mutations confer resistance to rifampicin http://purl.obolibrary.org/obo/ARO_3004995 rifampicin resistant rpoC Mutations in rpoC that contribute to or confer resistance to rifampicin antibiotic. http://purl.obolibrary.org/obo/ARO_3004995 rifampicin resistant rpoC http://purl.obolibrary.org/obo/ARO_3003289 antibiotic resistant rpoC rpoC catalyzes the transcription of DNA into RNA and mutations confer resistance to rifampicin. http://purl.obolibrary.org/obo/ARO_3004996 antibiotic sensitive beta-prime subunit of RNA polymerase (rpoA) http://purl.obolibrary.org/obo/ARO_3000712 nucleic acid synthesis machinery targeted by antibiotic RNA polymerase is a multisubunit enzyme that is necessary for transcription. Catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. http://purl.obolibrary.org/obo/ARO_3004997 antibiotic resistant rpoA http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant RNA polymerase is a multisubunit enzyme that is necessary for transcription. Mutations in rpoA gene confer antibiotic resistance. http://purl.obolibrary.org/obo/ARO_3004998 rifampicin resistant rpoA http://purl.obolibrary.org/obo/ARO_3004997 antibiotic resistant rpoA rpoA catalyzes the transcription of DNA into RNA and mutations confer resistance to rifampicin. http://purl.obolibrary.org/obo/ARO_3004999 Mycobacterium tuberculosis rpoA mutations confer resistance to rifampicin http://purl.obolibrary.org/obo/ARO_3004998 rifampicin resistant rpoA Mutations in rpoA that contribute to or confer resistance to rifampicin antibiotic. http://purl.obolibrary.org/obo/ARO_3005000 Zoliflodacin resistant gyrB http://purl.obolibrary.org/obo/ARO_3000220 antibiotic resistant DNA topoisomerase subunit gyrB Point mutations in DNA gyrase subunit B (gyrB) of Neisseria gonorrhoeae can result in resistance to Zoliflodacin. http://purl.obolibrary.org/obo/ARO_3005001 50S rRNA with mutation conferring resistance to macrolide antibiotics http://purl.obolibrary.org/obo/ARO_3005003 50S rRNA with mutation conferring antibiotic resistance Nucleotide point mutations in the 50S rRNA subunit (not in the 23s rRNA range) may confer resistance to macrolide antibiotics. http://purl.obolibrary.org/obo/ARO_3005002 antibiotic resistant polyketide synthase genes http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Genes ppsA-E constitute an operon encoding enzymes involved in the biosynthesis of phthiocerol dimycocerosate and other lipids in Mycobacterium tuberculosis. Mutations within this region can result in resistance to pyrazinamide. http://purl.obolibrary.org/obo/ARO_3005003 50S rRNA with mutation conferring antibiotic resistance http://purl.obolibrary.org/obo/ARO_3000328 rRNA with mutation conferring antibiotic resistance Mutations in the prokaryotic 50S ribosomal RNA subunit which disrupt binding sites and thereby reduce antibiotic efficacy. http://purl.obolibrary.org/obo/ARO_3009165 antifungal without defined classification http://purl.obolibrary.org/obo/ARO_3000003 antibiotic without defined classification Antifungal compounds with multiple applications and usages, including antimalarial, anti-cancer, anti-protist, etc. Often include ambiguous drug family classification. http://purl.obolibrary.org/obo/ARO_3009163 pyrimethamine http://purl.obolibrary.org/obo/ARO_3009165 antifungal without defined classification Pyrimethamine is a competitive inhibitor of dihydrofolate reductase (DHFR). DHFR is a key enzyme in the redox cycle for production of tetrahydrofolate, a cofactor that is required for the synthesis of DNA and proteins. It is typically used in combination with other drugs to treat parasitic infections, including malaria and toxoplasmosis. When combined with sulfadoxine, it can be used as prophylaxis for Pneumocystis jerovecii (fungi) induced pneumonia (PCP). However, this compound is generally not recommended for PCP prophylaxis unless trimethoprim-sulfamethoxazole, pentamidine, dapsone/pyrimethamine/leucovorin, atovaquone or dapsone cannot be used. http://purl.obolibrary.org/obo/ARO_3009161 benomyl http://purl.obolibrary.org/obo/ARO_3009165 antifungal without defined classification A foliar fungicide used to control a wide range of Ascomycetes and Fungi Imperfecti in a wide range of crops. http://purl.obolibrary.org/obo/ARO_3009179 diethofencarb http://purl.obolibrary.org/obo/ARO_3009165 antifungal without defined classification Diethofencarb is a fungicide typically used as an agrochemical. It is shown to have strong activity against Botrytis cinerea and benzimidazole-resistant strains of Botryis spp. It is a carbamate ester class fungicide, an aromatic ether and a carbanilate fungicide (subclass of carbamate fungicide). It is functionally related to an aniline. http://purl.obolibrary.org/obo/ARO_3009164 pyrifenox http://purl.obolibrary.org/obo/ARO_3009165 antifungal without defined classification A fungicide used for control of powdery mildew, scab and other fungal pathogens on a range of crops. Resistance was noted by Penicillium digitatum. http://purl.obolibrary.org/obo/ARO_3007843 VRA-F http://purl.obolibrary.org/obo/ARO_0010001 ATP-binding cassette (ABC) antibiotic efflux pump VRA-F is an ABC transporter ATP-binding protein, or ATP-binding cassette. http://purl.obolibrary.org/obo/ARO_3007844 KPC-135 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-135 is a KPC-type class A beta-lactamase. KPC-125 is a variant of KPC-44, differing by a 6 basepair deletion. http://purl.obolibrary.org/obo/ARO_3007845 SIE beta-lactamase http://purl.obolibrary.org/obo/ARO_3000571 subclass B3 (metallo-) beta-lactamase SIE is a subclass B3 metallo-beta-lactamase with enzymatic activity against cephalosporins and carbapanems, first identified from Sphingobium indicum. http://purl.obolibrary.org/obo/ARO_3007846 SIE-1 http://purl.obolibrary.org/obo/ARO_3007845 SIE beta-lactamase SIE-1 is SIE beta-lactamase gene family variant. http://purl.obolibrary.org/obo/ARO_3007847 NWM beta-lactamase http://purl.obolibrary.org/obo/ARO_3000571 subclass B3 (metallo-) beta-lactamase NWM is a subclass B3 metallo beta-lactamase with enzymatic activity against carbapenems, first identified in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3007848 NWM-1 http://purl.obolibrary.org/obo/ARO_3007847 NWM beta-lactamase NWM-1 is a NWM beta-lactamase gene family variant. http://purl.obolibrary.org/obo/ARO_3007849 Mycobacterium tuberculosis fgd1 with mutation conferring resistance to delamanid http://purl.obolibrary.org/obo/ARO_3007851 delamanid-resistant fgd1 Mutations in the F420-dependent glucose-6-phosphate dehydrogenase fgd1 which confer resistance to the nitroimidazole antibiotic delamanid. http://purl.obolibrary.org/obo/ARO_3007850 antibiotic resistant fgd1 http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Genetic variants of F420-dependent glucose-6-phosphate dehydrogenase fgd1 with mutations associated with antibiotic resistance. http://purl.obolibrary.org/obo/ARO_3007851 delamanid-resistant fgd1 http://purl.obolibrary.org/obo/ARO_3007850 antibiotic resistant fgd1 Genetic variants of F420-dependent glucose-6-phosphate dehydrogenase Fgd1 with mutations associated with resistance to the nitroimidazole antibiotic delamanid. http://purl.obolibrary.org/obo/ARO_3007852 Mycobacterium tuberculosis Rv0678 with mutation conferring resistance to clofazimine http://purl.obolibrary.org/obo/ARO_3007853 clofazimine resistant Rv0678 Genetic variants of the transcription factor Rv0678, which regulates expression of the mmpS5/L5 efflux pump, that are associated with resistance to clofazimine antibiotics. http://purl.obolibrary.org/obo/ARO_3007853 clofazimine resistant Rv0678 http://purl.obolibrary.org/obo/ARO_3007672 antibiotic resistant Rv0678 Loss-of-function mutations in the Mycobacterium Rv0678 gene associated with clofazimine resistance. http://purl.obolibrary.org/obo/ARO_3007854 Mycobacterium tuberculosis atpE with mutation conferring resistance to bedaquiline http://purl.obolibrary.org/obo/ARO_3007477 antibiotic resistant ATP synthase Genetic variants of ATPase subunit C atpE with mutations associated with resistance to bedaquiline antibiotics. http://purl.obolibrary.org/obo/ARO_3007855 CHM-1 http://purl.obolibrary.org/obo/ARO_3007856 CHM beta-lactamase CHM is a subclass B1 metallo B-lactamase with enzymatic activity against cephalosporins and carbapenems, first identified in the Chryseobacterium spp. functional gene library. http://purl.obolibrary.org/obo/ARO_3007856 CHM beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase CHM is a subclass B1 metallo B-lactamase with enzymatic activity against cephalosporins and carbapenems, first identified in the Chryseobacterium spp. functional gene library. http://purl.obolibrary.org/obo/ARO_3007857 KPC-134 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-134 is an inhibitor-resistant KPC-2 variant which confers resistance to ceftazidime-avibactam. http://purl.obolibrary.org/obo/ARO_3007858 BIM beta-lactamase http://purl.obolibrary.org/obo/ARO_3000004 class B (metallo-) beta-lactamase BIM is a family of ambler molecular class B beta-lactamases from Pseudomonas putida. It confers resistance to carbapenems and cephalosporins. http://purl.obolibrary.org/obo/ARO_3007859 BIM-1 http://purl.obolibrary.org/obo/ARO_3007858 BIM beta-lactamase BIM-1 is an ambler molecular class B beta-lactamase. It confers resistance to carbapenems and cephalosporins. http://purl.obolibrary.org/obo/ARO_3007860 DYB beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase DYB is a family of subclass B1 metallo-beta-lactamases identified from Dysgonomonas capnocytophagoides. These enzymes confer resistance to beta-lactam antibiotics, including carbapenems. http://purl.obolibrary.org/obo/ARO_3007861 DYB-1 http://purl.obolibrary.org/obo/ARO_3007860 DYB beta-lactamase DYB-1 is a subclass B1 metallo-beta-lactamases identified from Dysgonomonas capnocytophagoides. DYB-1 is associated with resistance to meropenem and ceftazidime. http://purl.obolibrary.org/obo/ARO_3007862 Canonical SMILES http://purl.obolibrary.org/obo/ARO_3000045 component of AMR genotypic or phenotypic terminology Simplified Molecular Input Line Entry System (SMILES), a chemical structure line notation (a typographical method using printable characters) for entering and representing molecules (description copied from PubChem). Canonical SMILES in CARD are acquired from ChEMBL. http://purl.obolibrary.org/obo/ARO_3007863 ASU1 beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase ASU1 is a family of class A beta-lactamase enzymes shown to confer resistance to beta-lactam and cephalosporin antibiotics through enzymatic inactivation. http://purl.obolibrary.org/obo/ARO_3007864 B3SU1 beta-lactamase http://purl.obolibrary.org/obo/ARO_3000571 subclass B3 (metallo-) beta-lactamase B3SU1 is a family of subclass B3 metallo-beta-lactamase enzymes which confer resistance to beta-lactam and cephalosporin antibiotics through enzymatic inactivation. http://purl.obolibrary.org/obo/ARO_3007865 B3SU2 beta-lactamase http://purl.obolibrary.org/obo/ARO_3000571 subclass B3 (metallo-) beta-lactamase B3SU2 is a family of subclass B3 metallo-beta-lactamases which confer resistance to beta-lactam and cephalosporin antibiotics through enzymatic inactivation. http://purl.obolibrary.org/obo/ARO_3007866 BMHC beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase BMHC is a family of subclass B1 metallo-beta-lactamase enzymes which confer resistance to carbapenem antibiotics through enzymatic inactivation. http://purl.obolibrary.org/obo/ARO_3007867 BOR beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase BOR is a family of class A beta-lactamase enzymes which confer resistance to beta-lactam antibiotics through enzymatic inactivation. http://purl.obolibrary.org/obo/ARO_3007868 GMA beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase GMA is a family of class A beta-lactamases which confer resistance to beta-lactam antibiotics through enzymatic inactivation. http://purl.obolibrary.org/obo/ARO_3007869 HBL beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase HBL is a family of class A beta-lactamases which enzymatically inactivate beta-lactam antibiotics. http://purl.obolibrary.org/obo/ARO_3007870 HER beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase HER is a family of class A beta-lactamases which enzymatically inactivation penam-type beta-lactam antibiotics. http://purl.obolibrary.org/obo/ARO_3007871 MUN beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase MUN is a family of extended-spectrum class A beta-lactamases which enzymatic inactivate beta-lactam and cephalosporin antibiotics. http://purl.obolibrary.org/obo/ARO_3007872 PAD beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase PAD is a family of carbapenem-hydrolyzing class A beta-lactamases which enzymatically inactivate beta-lactam and carbapenem antibiotics. http://purl.obolibrary.org/obo/ARO_3007873 PEN-A beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase PEN-A is a family of class A beta-lactamases which enzymatically inactivate beta-lactam antibiotics. http://purl.obolibrary.org/obo/ARO_3007874 PEN-B beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase PEN-B is a family of class A beta-lactamase enzymes which inactivate beta-lactam antibiotics. http://purl.obolibrary.org/obo/ARO_3007875 PNC beta-lactamase http://purl.obolibrary.org/obo/ARO_3000076 class C beta-lactamase PNC is a family of extended-spectrum class C beta-lactamases which enzymatically inactivate cephalosporin antibiotics. http://purl.obolibrary.org/obo/ARO_3007876 RAA beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase RAA is a family of class A extended-spectrum beta-lactamases which enzymatically inactivate cephalosporin antibiotics. http://purl.obolibrary.org/obo/ARO_3007877 RASA beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase RASA is a family of extended-spectrum class A beta-lactamases which enzymatically inactivate cephalosporin antibiotics. http://purl.obolibrary.org/obo/ARO_3007878 RSC1 beta-lactamase http://purl.obolibrary.org/obo/ARO_3000076 class C beta-lactamase RSC1 is a family of class C beta-lactamases which inactivate cephalosporin antibiotics. http://purl.obolibrary.org/obo/ARO_3007879 RSD1 http://purl.obolibrary.org/obo/ARO_3000075 class D beta-lactamase RSD1 is a family of class D beta-lactamases which confer resistance to beta-lactam antibiotics. http://purl.obolibrary.org/obo/ARO_3007880 SED beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase SED is a family of broad-spectrum class A beta-lactamases. http://purl.obolibrary.org/obo/ARO_3007881 SFDC beta-lactamase http://purl.obolibrary.org/obo/ARO_3000076 class C beta-lactamase SFDC is a family of extended-spectrum class C beta-lactamases which confer resistance to cephalosporin antibiotics. http://purl.obolibrary.org/obo/ARO_3007882 YOC beta-lactamase http://purl.obolibrary.org/obo/ARO_3000076 class C beta-lactamase YOC is a family of class C beta-lactamases which inactivate cephalosporin antibiotics. http://purl.obolibrary.org/obo/ARO_3007883 ACT-100 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-100. http://purl.obolibrary.org/obo/ARO_3007884 ACT-101 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-101. http://purl.obolibrary.org/obo/ARO_3007885 ACT-102 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-102. http://purl.obolibrary.org/obo/ARO_3007886 ACT-103 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-103. http://purl.obolibrary.org/obo/ARO_3007887 ACT-104 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-104. http://purl.obolibrary.org/obo/ARO_3007888 ACT-105 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-105. http://purl.obolibrary.org/obo/ARO_3007889 ACT-106 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-106. http://purl.obolibrary.org/obo/ARO_3007890 ACT-107 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-107. http://purl.obolibrary.org/obo/ARO_3007891 ACT-108 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-108. http://purl.obolibrary.org/obo/ARO_3007892 ACT-109 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-109. http://purl.obolibrary.org/obo/ARO_3007893 ACT-110 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-110. http://purl.obolibrary.org/obo/ARO_3007894 ACT-111 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-111. http://purl.obolibrary.org/obo/ARO_3007895 ACT-112 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-112. http://purl.obolibrary.org/obo/ARO_3007896 ACT-113 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-113. http://purl.obolibrary.org/obo/ARO_3007897 ACT-115 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-115. http://purl.obolibrary.org/obo/ARO_3007898 ACT-116 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-116. http://purl.obolibrary.org/obo/ARO_3007899 ACT-117 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-117. http://purl.obolibrary.org/obo/ARO_3007900 ACT-118 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-118. http://purl.obolibrary.org/obo/ARO_3007901 ACT-119 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-119. http://purl.obolibrary.org/obo/ARO_3007902 ACT-120 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-120. http://purl.obolibrary.org/obo/ARO_3007903 ACT-121 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-121. http://purl.obolibrary.org/obo/ARO_3007904 ACT-122 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-122. http://purl.obolibrary.org/obo/ARO_3007905 ACT-123 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-123. http://purl.obolibrary.org/obo/ARO_3007906 ACT-124 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-124. http://purl.obolibrary.org/obo/ARO_3007907 ACT-131 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-131. http://purl.obolibrary.org/obo/ARO_3007908 ACT-140 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-140. http://purl.obolibrary.org/obo/ARO_3007909 ACT-141 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-141. http://purl.obolibrary.org/obo/ARO_3007910 ACT-142 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-142. http://purl.obolibrary.org/obo/ARO_3007911 ACT-143 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-143. http://purl.obolibrary.org/obo/ARO_3007912 ACT-144 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-144. http://purl.obolibrary.org/obo/ARO_3007913 ACT-145 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-145. http://purl.obolibrary.org/obo/ARO_3007914 ACT-146 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-146. http://purl.obolibrary.org/obo/ARO_3007915 ACT-148 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-148. http://purl.obolibrary.org/obo/ARO_3007916 ACT-150 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-150. http://purl.obolibrary.org/obo/ARO_3007917 ACT-151 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-151. http://purl.obolibrary.org/obo/ARO_3007918 ACT-153 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-153. http://purl.obolibrary.org/obo/ARO_3007919 ACT-154 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-154. http://purl.obolibrary.org/obo/ARO_3007920 ACT-155 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-155. http://purl.obolibrary.org/obo/ARO_3007921 ACT-156 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-156. http://purl.obolibrary.org/obo/ARO_3007922 ACT-157 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-157. http://purl.obolibrary.org/obo/ARO_3007923 ACT-158 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-158. http://purl.obolibrary.org/obo/ARO_3007924 ACT-159 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-159. http://purl.obolibrary.org/obo/ARO_3007925 ACT-160 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-160. http://purl.obolibrary.org/obo/ARO_3007926 ACT-161 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-161. http://purl.obolibrary.org/obo/ARO_3007927 ACT-162 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-162. http://purl.obolibrary.org/obo/ARO_3007928 ACT-165 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-165. http://purl.obolibrary.org/obo/ARO_3007929 ACT-166 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-166. http://purl.obolibrary.org/obo/ARO_3007930 ACT-167 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-167. http://purl.obolibrary.org/obo/ARO_3007931 ACT-168 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-168. http://purl.obolibrary.org/obo/ARO_3007932 ACT-169 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-169. http://purl.obolibrary.org/obo/ARO_3007933 ACT-170 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-170. http://purl.obolibrary.org/obo/ARO_3007934 ACT-171 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-171. http://purl.obolibrary.org/obo/ARO_3007935 ACT-172 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-172. http://purl.obolibrary.org/obo/ARO_3007936 ACT-173 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-173. http://purl.obolibrary.org/obo/ARO_3007937 ACT-174 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-174. http://purl.obolibrary.org/obo/ARO_3007938 ACT-175 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-175. http://purl.obolibrary.org/obo/ARO_3007939 ACT-176 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-176. http://purl.obolibrary.org/obo/ARO_3007940 ACT-177 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-177. http://purl.obolibrary.org/obo/ARO_3007941 ACT-178 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-178. http://purl.obolibrary.org/obo/ARO_3007942 ACT-179 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-179. http://purl.obolibrary.org/obo/ARO_3007943 ACT-180 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-180. http://purl.obolibrary.org/obo/ARO_3007944 ACT-181 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-181. http://purl.obolibrary.org/obo/ARO_3007945 ACT-182 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-182. http://purl.obolibrary.org/obo/ARO_3007946 ACT-183 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-183. http://purl.obolibrary.org/obo/ARO_3007947 ACT-184 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-184. http://purl.obolibrary.org/obo/ARO_3007948 ACT-185 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-185. http://purl.obolibrary.org/obo/ARO_3007949 ACT-186 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-186. http://purl.obolibrary.org/obo/ARO_3007950 ACT-187 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-187. http://purl.obolibrary.org/obo/ARO_3007951 ACT-188 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-188. http://purl.obolibrary.org/obo/ARO_3007952 ACT-189 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-189. http://purl.obolibrary.org/obo/ARO_3007953 ACT-190 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-190. http://purl.obolibrary.org/obo/ARO_3007954 ACT-191 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-191. http://purl.obolibrary.org/obo/ARO_3007955 ACT-192 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-192. http://purl.obolibrary.org/obo/ARO_3007956 ACT-193 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-193. http://purl.obolibrary.org/obo/ARO_3007957 ACT-194 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-194. http://purl.obolibrary.org/obo/ARO_3007958 ACT-85 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Ceftazidime-hydrolyzing class C beta-lactamase ACT-85. http://purl.obolibrary.org/obo/ARO_3007959 ACT-86 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Ceftazidime-hydrolyzing class C beta-lactamase ACT-86. http://purl.obolibrary.org/obo/ARO_3007960 ACT-88 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-88. http://purl.obolibrary.org/obo/ARO_3007961 ACT-89 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-89. http://purl.obolibrary.org/obo/ARO_3007962 ACT-90 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-90. http://purl.obolibrary.org/obo/ARO_3007963 ACT-91 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-91. http://purl.obolibrary.org/obo/ARO_3007964 ACT-92 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-92. http://purl.obolibrary.org/obo/ARO_3007965 ACT-93 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-93. http://purl.obolibrary.org/obo/ARO_3007966 ACT-94 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-94. http://purl.obolibrary.org/obo/ARO_3007967 ACT-95 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-95. http://purl.obolibrary.org/obo/ARO_3007968 ACT-96 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-96. http://purl.obolibrary.org/obo/ARO_3007969 ACT-97 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-97. http://purl.obolibrary.org/obo/ARO_3007970 ACT-98 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-98. http://purl.obolibrary.org/obo/ARO_3007971 ACT-99 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase ACT-99. http://purl.obolibrary.org/obo/ARO_3007972 ACT-GC1 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase Extended spectrum class C beta-lactamase ACT-GC1. http://purl.obolibrary.org/obo/ARO_3007973 ADC-257 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-257. http://purl.obolibrary.org/obo/ARO_3007974 ADC-258 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-258. http://purl.obolibrary.org/obo/ARO_3007975 ADC-259 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-259. http://purl.obolibrary.org/obo/ARO_3007976 ADC-260 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-260. http://purl.obolibrary.org/obo/ARO_3007977 ADC-261 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Cefepime-hydrolyzing class C beta-lactamase ADC-261. http://purl.obolibrary.org/obo/ARO_3007978 ADC-262 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-262. http://purl.obolibrary.org/obo/ARO_3007979 ADC-263 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-263. http://purl.obolibrary.org/obo/ARO_3007980 ADC-264 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-264. http://purl.obolibrary.org/obo/ARO_3007981 ADC-265 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-265. http://purl.obolibrary.org/obo/ARO_3007982 ADC-266 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-266. http://purl.obolibrary.org/obo/ARO_3007983 ADC-267 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-267. http://purl.obolibrary.org/obo/ARO_3007984 ADC-268 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-268. http://purl.obolibrary.org/obo/ARO_3007985 ADC-269 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-269. http://purl.obolibrary.org/obo/ARO_3007986 ADC-270 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-270. http://purl.obolibrary.org/obo/ARO_3007987 ADC-271 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-271. http://purl.obolibrary.org/obo/ARO_3007988 ADC-272 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-272. http://purl.obolibrary.org/obo/ARO_3007989 ADC-273 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-273. http://purl.obolibrary.org/obo/ARO_3007990 ADC-274 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-274. http://purl.obolibrary.org/obo/ARO_3007991 ADC-275 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-275. http://purl.obolibrary.org/obo/ARO_3007992 ADC-276 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-276. http://purl.obolibrary.org/obo/ARO_3007993 ADC-277 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-277. http://purl.obolibrary.org/obo/ARO_3007994 ADC-278 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-278. http://purl.obolibrary.org/obo/ARO_3007995 ADC-279 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-279. http://purl.obolibrary.org/obo/ARO_3007996 ADC-280 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-280. http://purl.obolibrary.org/obo/ARO_3007997 ADC-281 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-281. http://purl.obolibrary.org/obo/ARO_3007998 ADC-282 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-282. http://purl.obolibrary.org/obo/ARO_3007999 ADC-283 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-283. http://purl.obolibrary.org/obo/ARO_3008000 ADC-284 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-284. http://purl.obolibrary.org/obo/ARO_3008001 ADC-285 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-285. http://purl.obolibrary.org/obo/ARO_3008002 ADC-286 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-286. http://purl.obolibrary.org/obo/ARO_3008003 ADC-287 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-287. http://purl.obolibrary.org/obo/ARO_3008004 ADC-288 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-288. http://purl.obolibrary.org/obo/ARO_3008005 ADC-289 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-289. http://purl.obolibrary.org/obo/ARO_3008006 ADC-290 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-290. http://purl.obolibrary.org/obo/ARO_3008007 ADC-291 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-291. http://purl.obolibrary.org/obo/ARO_3008008 ADC-292 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-292. http://purl.obolibrary.org/obo/ARO_3008009 ADC-293 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-293. http://purl.obolibrary.org/obo/ARO_3008010 ADC-294 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-294. http://purl.obolibrary.org/obo/ARO_3008011 ADC-295 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-295. http://purl.obolibrary.org/obo/ARO_3008012 ADC-302 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-302. http://purl.obolibrary.org/obo/ARO_3008013 ADC-303 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-303. http://purl.obolibrary.org/obo/ARO_3008014 ADC-304 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-304. http://purl.obolibrary.org/obo/ARO_3008015 ADC-305 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-305. http://purl.obolibrary.org/obo/ARO_3008016 ADC-306 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-306. http://purl.obolibrary.org/obo/ARO_3008017 ADC-307 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-307. http://purl.obolibrary.org/obo/ARO_3008018 ADC-308 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-308. http://purl.obolibrary.org/obo/ARO_3008019 ADC-309 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-309. http://purl.obolibrary.org/obo/ARO_3008020 ADC-310 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-310. http://purl.obolibrary.org/obo/ARO_3008021 ADC-311 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-311. http://purl.obolibrary.org/obo/ARO_3008022 ADC-312 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-312. http://purl.obolibrary.org/obo/ARO_3008023 ADC-313 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-313. http://purl.obolibrary.org/obo/ARO_3008024 ADC-314 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-314. http://purl.obolibrary.org/obo/ARO_3008025 ADC-315 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-315. http://purl.obolibrary.org/obo/ARO_3008026 ADC-316 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-316. http://purl.obolibrary.org/obo/ARO_3008027 ADC-317 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-317. http://purl.obolibrary.org/obo/ARO_3008028 ADC-318 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-318. http://purl.obolibrary.org/obo/ARO_3008029 ADC-319 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-319. http://purl.obolibrary.org/obo/ARO_3008030 ADC-320 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-320. http://purl.obolibrary.org/obo/ARO_3008031 ADC-321 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-321. http://purl.obolibrary.org/obo/ARO_3008032 ADC-322 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-322. http://purl.obolibrary.org/obo/ARO_3008033 ADC-323 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-323. http://purl.obolibrary.org/obo/ARO_3008034 ADC-324 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-324. http://purl.obolibrary.org/obo/ARO_3008035 ADC-325 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-325. http://purl.obolibrary.org/obo/ARO_3008036 ADC-326 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-326. http://purl.obolibrary.org/obo/ARO_3008037 ADC-327 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-327. http://purl.obolibrary.org/obo/ARO_3008038 ADC-328 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-328. http://purl.obolibrary.org/obo/ARO_3008039 ADC-329 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-329. http://purl.obolibrary.org/obo/ARO_3008040 ADC-330 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-330. http://purl.obolibrary.org/obo/ARO_3008041 ADC-331 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-331. http://purl.obolibrary.org/obo/ARO_3008042 ADC-332 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-332. http://purl.obolibrary.org/obo/ARO_3008043 ADC-333 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-333. http://purl.obolibrary.org/obo/ARO_3008044 ADC-334 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-334. http://purl.obolibrary.org/obo/ARO_3008045 ADC-335 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-335. http://purl.obolibrary.org/obo/ARO_3008046 ADC-336 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-336. http://purl.obolibrary.org/obo/ARO_3008047 ADC-337 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-337. http://purl.obolibrary.org/obo/ARO_3008048 ADC-338 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-338. http://purl.obolibrary.org/obo/ARO_3008049 ADC-339 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-339. http://purl.obolibrary.org/obo/ARO_3008050 ADC-340 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-340. http://purl.obolibrary.org/obo/ARO_3008051 ADC-341 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-341. http://purl.obolibrary.org/obo/ARO_3008052 ADC-342 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-342. http://purl.obolibrary.org/obo/ARO_3008053 ADC-343 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-343. http://purl.obolibrary.org/obo/ARO_3008054 ADC-344 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-344. http://purl.obolibrary.org/obo/ARO_3008055 ADC-345 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-345. http://purl.obolibrary.org/obo/ARO_3008056 ADC-346 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-346. http://purl.obolibrary.org/obo/ARO_3008057 ADC-347 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-347. http://purl.obolibrary.org/obo/ARO_3008058 ADC-348 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-348. http://purl.obolibrary.org/obo/ARO_3008059 ADC-349 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-349. http://purl.obolibrary.org/obo/ARO_3008060 ADC-350 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-350. http://purl.obolibrary.org/obo/ARO_3008061 ADC-351 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-351. http://purl.obolibrary.org/obo/ARO_3008062 ADC-352 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-352. http://purl.obolibrary.org/obo/ARO_3008063 ADC-353 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-353. http://purl.obolibrary.org/obo/ARO_3008064 ADC-354 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-354. http://purl.obolibrary.org/obo/ARO_3008065 ADC-355 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-355. http://purl.obolibrary.org/obo/ARO_3008066 ADC-356 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-356. http://purl.obolibrary.org/obo/ARO_3008067 ADC-357 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-357. http://purl.obolibrary.org/obo/ARO_3008068 ADC-358 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Extended-spectrum class C beta-lactamase ADC-358. http://purl.obolibrary.org/obo/ARO_3008069 ADC-359 http://purl.obolibrary.org/obo/ARO_3005460 ADC beta-lactamases pending classification for carbapenemase activity Class C beta-lactamase ADC-359. http://purl.obolibrary.org/obo/ARO_3008070 AFM-3 http://purl.obolibrary.org/obo/ARO_3005388 AFM beta-lactamase Subclass B1 metallo-beta-lactamase AFM-3. http://purl.obolibrary.org/obo/ARO_3008071 AFM-4 http://purl.obolibrary.org/obo/ARO_3005388 AFM beta-lactamase Subclass B1 metallo-beta-lactamase AFM-4. http://purl.obolibrary.org/obo/ARO_3008072 AFM-5 http://purl.obolibrary.org/obo/ARO_3005388 AFM beta-lactamase Subclass B1 metallo-beta-lactamase AFM-5. http://purl.obolibrary.org/obo/ARO_3008073 AIM-2 http://purl.obolibrary.org/obo/ARO_3004216 AIM beta-lactamase Subclass B3 metallo-beta-lactamase AIM-2. http://purl.obolibrary.org/obo/ARO_3008074 ASU1-1 http://purl.obolibrary.org/obo/ARO_3007863 ASU1 beta-lactamase Class A beta-lactamase ASU1-1. http://purl.obolibrary.org/obo/ARO_3008075 AXC-6 http://purl.obolibrary.org/obo/ARO_3005393 AXC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase AXC-6. http://purl.obolibrary.org/obo/ARO_3008076 AXC-7 http://purl.obolibrary.org/obo/ARO_3005393 AXC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase AXC-7. http://purl.obolibrary.org/obo/ARO_3008077 AXC-8 http://purl.obolibrary.org/obo/ARO_3005393 AXC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase AXC-8. http://purl.obolibrary.org/obo/ARO_3008078 B3SU1-1 http://purl.obolibrary.org/obo/ARO_3007864 B3SU1 beta-lactamase Subclass B3 metallo-beta-lactamase B3SU1-1. http://purl.obolibrary.org/obo/ARO_3008079 B3SU2-1 http://purl.obolibrary.org/obo/ARO_3007865 B3SU2 beta-lactamase Subclass B3 metallo-beta-lactamase B3SU2-1. http://purl.obolibrary.org/obo/ARO_3008080 BIC-2 http://purl.obolibrary.org/obo/ARO_3004752 BIC Beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase BIC-2. http://purl.obolibrary.org/obo/ARO_3008081 BMHC-1 http://purl.obolibrary.org/obo/ARO_3007866 BMHC beta-lactamase Subclass B1 metallo-beta-lactamase BMHC-1. http://purl.obolibrary.org/obo/ARO_3008082 BOR-1 http://purl.obolibrary.org/obo/ARO_3007867 BOR beta-lactamase Class A beta-lactamase BOR-1. http://purl.obolibrary.org/obo/ARO_3008083 CAM-2 http://purl.obolibrary.org/obo/ARO_3004558 CAM beta-lactamase Subclass B1 metallo-beta-lactamase CAM-2. http://purl.obolibrary.org/obo/ARO_3008084 CME-3 http://purl.obolibrary.org/obo/ARO_3004774 CME beta-lactamase Extended-spectrum class A beta-lactamase CME-3. http://purl.obolibrary.org/obo/ARO_3008085 CMH-10 http://purl.obolibrary.org/obo/ARO_3004776 CMH beta-lactamase Class C beta-lactamase CMH-10. http://purl.obolibrary.org/obo/ARO_3008086 CMH-11 http://purl.obolibrary.org/obo/ARO_3004776 CMH beta-lactamase Class C beta-lactamase CMH-11. http://purl.obolibrary.org/obo/ARO_3008087 CMH-12 http://purl.obolibrary.org/obo/ARO_3004776 CMH beta-lactamase Class C beta-lactamase CMH-12. http://purl.obolibrary.org/obo/ARO_3008088 CMH-13 http://purl.obolibrary.org/obo/ARO_3004776 CMH beta-lactamase Class C beta-lactamase CMH-13. http://purl.obolibrary.org/obo/ARO_3008089 CMH-14 http://purl.obolibrary.org/obo/ARO_3004776 CMH beta-lactamase Class C beta-lactamase CMH-14. http://purl.obolibrary.org/obo/ARO_3008090 CMH-15 http://purl.obolibrary.org/obo/ARO_3004776 CMH beta-lactamase Class C beta-lactamase CMH-15. http://purl.obolibrary.org/obo/ARO_3008091 CMH-16 http://purl.obolibrary.org/obo/ARO_3004776 CMH beta-lactamase Class C beta-lactamase CMH-16. http://purl.obolibrary.org/obo/ARO_3008092 CMH-17 http://purl.obolibrary.org/obo/ARO_3004776 CMH beta-lactamase Class C beta-lactamase CMH-17. http://purl.obolibrary.org/obo/ARO_3008093 CMH-18 http://purl.obolibrary.org/obo/ARO_3004776 CMH beta-lactamase Class C beta-lactamase CMH-18. http://purl.obolibrary.org/obo/ARO_3008094 CMH-19 http://purl.obolibrary.org/obo/ARO_3004776 CMH beta-lactamase Class C beta-lactamase CMH-19. http://purl.obolibrary.org/obo/ARO_3008095 CMH-20 http://purl.obolibrary.org/obo/ARO_3004776 CMH beta-lactamase Class C beta-lactamase CMH-20. http://purl.obolibrary.org/obo/ARO_3008096 CMH-21 http://purl.obolibrary.org/obo/ARO_3004776 CMH beta-lactamase Class C beta-lactamase CMH-21. http://purl.obolibrary.org/obo/ARO_3008097 CMH-24 http://purl.obolibrary.org/obo/ARO_3004776 CMH beta-lactamase Class C beta-lactamase CMH-24. http://purl.obolibrary.org/obo/ARO_3008098 CMH-25 http://purl.obolibrary.org/obo/ARO_3004776 CMH beta-lactamase Class C beta-lactamase CMH-25. http://purl.obolibrary.org/obo/ARO_3008099 CMH-26 http://purl.obolibrary.org/obo/ARO_3004776 CMH beta-lactamase Class C beta-lactamase CMH-26. http://purl.obolibrary.org/obo/ARO_3008100 CMH-27 http://purl.obolibrary.org/obo/ARO_3004776 CMH beta-lactamase Class C beta-lactamase CMH-27. http://purl.obolibrary.org/obo/ARO_3008101 CMH-28 http://purl.obolibrary.org/obo/ARO_3004776 CMH beta-lactamase Class C beta-lactamase CMH-28. http://purl.obolibrary.org/obo/ARO_3008102 CMH-29 http://purl.obolibrary.org/obo/ARO_3004776 CMH beta-lactamase Class C beta-lactamase CMH-29. http://purl.obolibrary.org/obo/ARO_3008103 CMH-30 http://purl.obolibrary.org/obo/ARO_3004776 CMH beta-lactamase Class C beta-lactamase CMH-30. http://purl.obolibrary.org/obo/ARO_3008104 CMH-31 http://purl.obolibrary.org/obo/ARO_3004776 CMH beta-lactamase Class C beta-lactamase CMH-31. http://purl.obolibrary.org/obo/ARO_3008105 CMH-32 http://purl.obolibrary.org/obo/ARO_3004776 CMH beta-lactamase Class C beta-lactamase CMH-32. http://purl.obolibrary.org/obo/ARO_3008106 CMH-33 http://purl.obolibrary.org/obo/ARO_3004776 CMH beta-lactamase Class C beta-lactamase CMH-33. http://purl.obolibrary.org/obo/ARO_3008107 CMH-34 http://purl.obolibrary.org/obo/ARO_3004776 CMH beta-lactamase Class C beta-lactamase CMH-34. http://purl.obolibrary.org/obo/ARO_3008108 CMH-7 http://purl.obolibrary.org/obo/ARO_3004776 CMH beta-lactamase Class C beta-lactamase CMH-7. http://purl.obolibrary.org/obo/ARO_3008109 CMH-8 http://purl.obolibrary.org/obo/ARO_3004776 CMH beta-lactamase Class C beta-lactamase CMH-8. http://purl.obolibrary.org/obo/ARO_3008110 CMH-9 http://purl.obolibrary.org/obo/ARO_3004776 CMH beta-lactamase Class C beta-lactamase CMH-9. http://purl.obolibrary.org/obo/ARO_3008111 CMY-172 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase Inhibitor-resistant extended-spectrum class C beta-lactamase CMY-172. http://purl.obolibrary.org/obo/ARO_3008112 CMY-175 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase Class C beta-lactamase CMY-175. http://purl.obolibrary.org/obo/ARO_3008113 CMY-176 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase Class C beta-lactamase CMY-176. http://purl.obolibrary.org/obo/ARO_3008114 CMY-177 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase Class C beta-lactamase CMY-177. http://purl.obolibrary.org/obo/ARO_3008115 CMY-178 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase Class C beta-lactamase CMY-178. http://purl.obolibrary.org/obo/ARO_3008116 CMY-179 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase Class C beta-lactamase CMY-179. http://purl.obolibrary.org/obo/ARO_3008117 CMY-180 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase Class C beta-lactamase CMY-180. http://purl.obolibrary.org/obo/ARO_3008118 CMY-181 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase Class C beta-lactamase CMY-181. http://purl.obolibrary.org/obo/ARO_3008119 CMY-182 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase Class C beta-lactamase CMY-182. http://purl.obolibrary.org/obo/ARO_3008120 CMY-183 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase Class C beta-lactamase CMY-183. http://purl.obolibrary.org/obo/ARO_3008121 CMY-184 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase Class C beta-lactamase CMY-184. http://purl.obolibrary.org/obo/ARO_3008122 CMY-186 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase Class C beta-lactamase CMY-186. http://purl.obolibrary.org/obo/ARO_3008123 CMY-188 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase Class C beta-lactamase CMY-188. http://purl.obolibrary.org/obo/ARO_3008124 CMY-189 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase Class C beta-lactamase CMY-189. http://purl.obolibrary.org/obo/ARO_3008125 CMY-190 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase Class C beta-lactamase CMY-190. http://purl.obolibrary.org/obo/ARO_3008126 CMY-191 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase Class C beta-lactamase CMY-191. http://purl.obolibrary.org/obo/ARO_3008127 CMY-192 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase Class C beta-lactamase CMY-192. http://purl.obolibrary.org/obo/ARO_3008128 CMY-194 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase Class C beta-lactamase CMY-194. http://purl.obolibrary.org/obo/ARO_3008129 CMY-195 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase Class C beta-lactamase CMY-195. http://purl.obolibrary.org/obo/ARO_3008130 CMY-196 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase Class C beta-lactamase CMY-196. http://purl.obolibrary.org/obo/ARO_3008131 CMY-197 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase Class C beta-lactamase CMY-197. http://purl.obolibrary.org/obo/ARO_3008132 CMY-198 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase Class C beta-lactamase CMY-198. http://purl.obolibrary.org/obo/ARO_3008133 CMY-199 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase Class C beta-lactamase CMY-199. http://purl.obolibrary.org/obo/ARO_3008134 CTX-M-243 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase Extended-spectrum class A beta-lactamase CTX-M-243. http://purl.obolibrary.org/obo/ARO_3008135 CTX-M-245 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase Extended-spectrum class A beta-lactamase CTX-M-245. http://purl.obolibrary.org/obo/ARO_3008136 CTX-M-246 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase Extended-spectrum class A beta-lactamase CTX-M-246. http://purl.obolibrary.org/obo/ARO_3008137 CTX-M-247 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase Extended-spectrum class A beta-lactamase CTX-M-247. http://purl.obolibrary.org/obo/ARO_3008138 CTX-M-248 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase Extended-spectrum class A beta-lactamase CTX-M-248. http://purl.obolibrary.org/obo/ARO_3008139 CTX-M-249 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase Extended-spectrum class A beta-lactamase CTX-M-249. http://purl.obolibrary.org/obo/ARO_3008140 CTX-M-251 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase Extended-spectrum class A beta-lactamase CTX-M-251. http://purl.obolibrary.org/obo/ARO_3008141 CTX-M-252 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase Extended-spectrum class A beta-lactamase CTX-M-252. http://purl.obolibrary.org/obo/ARO_3008142 CTX-M-253 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase Extended-spectrum class A beta-lactamase CTX-M-253. http://purl.obolibrary.org/obo/ARO_3008143 CTX-M-254 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase Extended-spectrum class A beta-lactamase CTX-M-254. http://purl.obolibrary.org/obo/ARO_3008144 CTX-M-255 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase Inhibitor-resistant class A beta-lactamase CTX-M-255. http://purl.obolibrary.org/obo/ARO_3008145 CTX-M-256 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase Extended-spectrum class A beta-lactamase CTX-M-256. http://purl.obolibrary.org/obo/ARO_3008146 CTX-M-257 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase Extended-spectrum class A beta-lactamase CTX-M-257. http://purl.obolibrary.org/obo/ARO_3008147 CTX-M-258 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase Extended-spectrum class A beta-lactamase CTX-M-258. http://purl.obolibrary.org/obo/ARO_3008148 CTX-M-259 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase Extended-spectrum class A beta-lactamase CTX-M-259. http://purl.obolibrary.org/obo/ARO_3008149 CTX-M-260 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase Extended-spectrum class A beta-lactamase CTX-M-260. http://purl.obolibrary.org/obo/ARO_3008150 CTX-M-261 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase Extended-spectrum class A beta-lactamase CTX-M-261. http://purl.obolibrary.org/obo/ARO_3008151 CTX-M-262 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase Extended-spectrum class A beta-lactamase CTX-M-262. http://purl.obolibrary.org/obo/ARO_3008152 CTX-M-263 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase Extended-spectrum class A beta-lactamase CTX-M-263. http://purl.obolibrary.org/obo/ARO_3008153 CTX-M-264 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase Extended-spectrum class A beta-lactamase CTX-M-264. http://purl.obolibrary.org/obo/ARO_3008154 CTX-M-265 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase Extended-spectrum class A beta-lactamase CTX-M-265. http://purl.obolibrary.org/obo/ARO_3008155 CTX-M-266 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase Extended-spectrum class A beta-lactamase CTX-M-266. http://purl.obolibrary.org/obo/ARO_3008156 CTX-M-267 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase Extended-spectrum class A beta-lactamase CTX-M-267. http://purl.obolibrary.org/obo/ARO_3008157 CTX-M-268 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase Extended-spectrum class A beta-lactamase CTX-M-268. http://purl.obolibrary.org/obo/ARO_3008158 CTX-M-269 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase Extended-spectrum class A beta-lactamase CTX-M-269. http://purl.obolibrary.org/obo/ARO_3008159 CTX-M-270 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase Extended-spectrum class A beta-lactamase CTX-M-270. http://purl.obolibrary.org/obo/ARO_3008160 CTX-M-271 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase Extended-spectrum class A beta-lactamase CTX-M-271. http://purl.obolibrary.org/obo/ARO_3008161 CTX-M-272 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase Extended-spectrum class A beta-lactamase CTX-M-272. http://purl.obolibrary.org/obo/ARO_3008162 CTX-M-273 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase Extended-spectrum class A beta-lactamase CTX-M-273. http://purl.obolibrary.org/obo/ARO_3008163 CTX-M-274 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase Extended-spectrum class A beta-lactamase CTX-M-274. http://purl.obolibrary.org/obo/ARO_3008164 CTX-M-275 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase Extended-spectrum class A beta-lactamase CTX-M-275. http://purl.obolibrary.org/obo/ARO_3008165 CTX-M-276 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase Extended-spectrum class A beta-lactamase CTX-M-276. http://purl.obolibrary.org/obo/ARO_3008166 CTX-M-277 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase Extended-spectrum class A beta-lactamase CTX-M-277. http://purl.obolibrary.org/obo/ARO_3008167 CTX-M-278 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase Extended-spectrum class A beta-lactamase CTX-M-278. http://purl.obolibrary.org/obo/ARO_3008168 DHA-30 http://purl.obolibrary.org/obo/ARO_3000068 DHA beta-lactamase Class C beta-lactamase DHA-30. http://purl.obolibrary.org/obo/ARO_3008169 DHA-31 http://purl.obolibrary.org/obo/ARO_3000068 DHA beta-lactamase Class C beta-lactamase DHA-31. http://purl.obolibrary.org/obo/ARO_3008170 DHA-32 http://purl.obolibrary.org/obo/ARO_3000068 DHA beta-lactamase Class C beta-lactamase DHA-32. http://purl.obolibrary.org/obo/ARO_3008171 DHA-33 http://purl.obolibrary.org/obo/ARO_3000068 DHA beta-lactamase Class C beta-lactamase DHA-33. http://purl.obolibrary.org/obo/ARO_3008172 DHA-34 http://purl.obolibrary.org/obo/ARO_3000068 DHA beta-lactamase Class C beta-lactamase DHA-34. http://purl.obolibrary.org/obo/ARO_3008173 FONA-10 http://purl.obolibrary.org/obo/ARO_3004787 FONA beta-lactamase Class A beta-lactamase FONA-10. http://purl.obolibrary.org/obo/ARO_3008174 FONA-11 http://purl.obolibrary.org/obo/ARO_3004787 FONA beta-lactamase Class A beta-lactamase FONA-11. http://purl.obolibrary.org/obo/ARO_3008175 FONA-12 http://purl.obolibrary.org/obo/ARO_3004787 FONA beta-lactamase Class A beta-lactamase FONA-12. http://purl.obolibrary.org/obo/ARO_3008176 FONA-13 http://purl.obolibrary.org/obo/ARO_3004787 FONA beta-lactamase Class A beta-lactamase FONA-13. http://purl.obolibrary.org/obo/ARO_3008177 FONA-7 http://purl.obolibrary.org/obo/ARO_3004787 FONA beta-lactamase Class A beta-lactamase FONA-7. http://purl.obolibrary.org/obo/ARO_3008178 FONA-8 http://purl.obolibrary.org/obo/ARO_3004787 FONA beta-lactamase Class A beta-lactamase FONA-8. http://purl.obolibrary.org/obo/ARO_3008179 FONA-9 http://purl.obolibrary.org/obo/ARO_3004787 FONA beta-lactamase Class A beta-lactamase FONA-9. http://purl.obolibrary.org/obo/ARO_3008180 FOX-18 http://purl.obolibrary.org/obo/ARO_3000067 FOX beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase FOX-18. http://purl.obolibrary.org/obo/ARO_3008181 FOX-19 http://purl.obolibrary.org/obo/ARO_3000067 FOX beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase FOX-19. http://purl.obolibrary.org/obo/ARO_3008182 FOX-20 http://purl.obolibrary.org/obo/ARO_3000067 FOX beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase FOX-20. http://purl.obolibrary.org/obo/ARO_3008183 FOX-21 http://purl.obolibrary.org/obo/ARO_3000067 FOX beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase FOX-21. http://purl.obolibrary.org/obo/ARO_3008184 FRI-12 http://purl.obolibrary.org/obo/ARO_3004796 FRI beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase FRI-12. http://purl.obolibrary.org/obo/ARO_3008185 GES-58 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase Class A beta-lactamase GES-58. http://purl.obolibrary.org/obo/ARO_3008186 GES-59 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase Class A beta-lactamase GES-59. http://purl.obolibrary.org/obo/ARO_3008187 GES-60 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase Extended-spectrum class A beta-lactamase GES-60. http://purl.obolibrary.org/obo/ARO_3008188 GES-61 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase Class A beta-lactamase GES-61. http://purl.obolibrary.org/obo/ARO_3008189 GES-62 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase Class A beta-lactamase GES-62. http://purl.obolibrary.org/obo/ARO_3008190 GES-65 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase Class A beta-lactamase GES-65. http://purl.obolibrary.org/obo/ARO_3008191 GES-66 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase GES-66. http://purl.obolibrary.org/obo/ARO_3008192 GIM-3 http://purl.obolibrary.org/obo/ARO_3003195 GIM beta-lactamase Subclass B1 metallo-beta-lactamase GIM-3. http://purl.obolibrary.org/obo/ARO_3008193 GMA-1 http://purl.obolibrary.org/obo/ARO_3007868 GMA beta-lactamase GMA family class A beta-lactamase GMA-1. http://purl.obolibrary.org/obo/ARO_3008194 GMA-2 http://purl.obolibrary.org/obo/ARO_3007868 GMA beta-lactamase GMA family class A beta-lactamase GMA-2. http://purl.obolibrary.org/obo/ARO_3008195 GOB-17 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase Subclass B3 metallo-beta-lactamase GOB-17. http://purl.obolibrary.org/obo/ARO_3008196 GOB-47 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase Subclass B3 metallo-beta-lactamase GOB-47. http://purl.obolibrary.org/obo/ARO_3008197 GOB-52 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase Subclass B3 metallo-beta-lactamase GOB-52. http://purl.obolibrary.org/obo/ARO_3008198 GOB-53 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase Subclass B3 metallo-beta-lactamase GOB-53. http://purl.obolibrary.org/obo/ARO_3008199 HBL-1 http://purl.obolibrary.org/obo/ARO_3007869 HBL beta-lactamase Class A beta-lactamase HBL-1. http://purl.obolibrary.org/obo/ARO_3008200 HER-1 http://purl.obolibrary.org/obo/ARO_3007870 HER beta-lactamase Penicillin-hydrolyzing class A beta-lactamase HER-1. http://purl.obolibrary.org/obo/ARO_3008201 HER-2 http://purl.obolibrary.org/obo/ARO_3007870 HER beta-lactamase Class A beta-lactamase HER-2. http://purl.obolibrary.org/obo/ARO_3008202 HER-3 http://purl.obolibrary.org/obo/ARO_3007870 HER beta-lactamase Class A beta-lactamase HER-3. http://purl.obolibrary.org/obo/ARO_3008203 HER-4 http://purl.obolibrary.org/obo/ARO_3007870 HER beta-lactamase Class A beta-lactamase HER-4. http://purl.obolibrary.org/obo/ARO_3008204 HER-5 http://purl.obolibrary.org/obo/ARO_3007870 HER beta-lactamase Class A beta-lactamase HER-5. http://purl.obolibrary.org/obo/ARO_3008205 HER-6 http://purl.obolibrary.org/obo/ARO_3007870 HER beta-lactamase Class A beta-lactamase HER-6. http://purl.obolibrary.org/obo/ARO_3008206 HER-8 http://purl.obolibrary.org/obo/ARO_3007870 HER beta-lactamase Class A beta-lactamase HER-8. http://purl.obolibrary.org/obo/ARO_3008207 HMB-2 http://purl.obolibrary.org/obo/ARO_3004209 HMB beta-lactamase Subclass B1 metallo-beta-lactamase HMB-2. http://purl.obolibrary.org/obo/ARO_3008208 IMI-10 http://purl.obolibrary.org/obo/ARO_3000018 IMI beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase IMI-10. http://purl.obolibrary.org/obo/ARO_3008209 IMI-22 http://purl.obolibrary.org/obo/ARO_3000018 IMI beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase IMI-22. http://purl.obolibrary.org/obo/ARO_3008210 IMI-23 http://purl.obolibrary.org/obo/ARO_3000018 IMI beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase IMI-23. http://purl.obolibrary.org/obo/ARO_3008211 IMI-24 http://purl.obolibrary.org/obo/ARO_3000018 IMI beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase IMI-24. http://purl.obolibrary.org/obo/ARO_3008212 IMI-25 http://purl.obolibrary.org/obo/ARO_3000018 IMI beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase IMI-25. http://purl.obolibrary.org/obo/ARO_3008213 IMI-26 http://purl.obolibrary.org/obo/ARO_3000018 IMI beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase IMI-26. http://purl.obolibrary.org/obo/ARO_3008214 IMI-27 http://purl.obolibrary.org/obo/ARO_3000018 IMI beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase IMI-27. http://purl.obolibrary.org/obo/ARO_3008215 IMP-100 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase Subclass B1 metallo-beta-lactamase IMP-100. http://purl.obolibrary.org/obo/ARO_3008216 IMP-101 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase Subclass B1 metallo-beta-lactamase IMP-101. http://purl.obolibrary.org/obo/ARO_3008217 IMP-102 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase Subclass B1 metallo-beta-lactamase IMP-102. http://purl.obolibrary.org/obo/ARO_3008218 IMP-104 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase Subclass B1 metallo-beta-lactamase IMP-104. http://purl.obolibrary.org/obo/ARO_3008219 IMP-105 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase Subclass B1 metallo-beta-lactamase IMP-105. http://purl.obolibrary.org/obo/ARO_3008220 IMP-86 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase Subclass B1 metallo-beta-lactamase IMP-86. http://purl.obolibrary.org/obo/ARO_3008221 IMP-87 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase Subclass B1 metallo-beta-lactamase IMP-87. http://purl.obolibrary.org/obo/ARO_3008222 IMP-90 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase Subclass B1 metallo-beta-lactamase IMP-90. http://purl.obolibrary.org/obo/ARO_3008223 IMP-97 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase Subclass B1 metallo-beta-lactamase IMP-97. http://purl.obolibrary.org/obo/ARO_3008224 IMP-98 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase Subclass B1 metallo-beta-lactamase IMP-98. http://purl.obolibrary.org/obo/ARO_3008225 IMP-99 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase Subclass B1 metallo-beta-lactamase IMP-99. http://purl.obolibrary.org/obo/ARO_3008226 IND-18 http://purl.obolibrary.org/obo/ARO_3000060 IND beta-lactamase Subclass B1 metallo-beta-lactamase IND-18. http://purl.obolibrary.org/obo/ARO_3008227 IND-19 http://purl.obolibrary.org/obo/ARO_3000060 IND beta-lactamase Subclass B1 metallo-beta-lactamase IND-19. http://purl.obolibrary.org/obo/ARO_3008228 KHM-2 http://purl.obolibrary.org/obo/ARO_3004207 KHM beta-lactamase Subclass B1 metallo-beta-lactamase KHM-2. http://purl.obolibrary.org/obo/ARO_3008229 KLUC-6 http://purl.obolibrary.org/obo/ARO_3005417 KLUC beta-lactamase Extended-spectrum class A beta-lactamase KLUC-6. http://purl.obolibrary.org/obo/ARO_3008230 KLUG-1 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M family extended-spectrum class A beta-lactamase KLUG-1. http://purl.obolibrary.org/obo/ARO_3008231 KPC-101 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase KPC-101. http://purl.obolibrary.org/obo/ARO_3008232 KPC-102 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-102. http://purl.obolibrary.org/obo/ARO_3008233 KPC-103 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Class A beta-lactamase KPC-103. http://purl.obolibrary.org/obo/ARO_3008234 KPC-104 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Class A beta-lactamase KPC-104. http://purl.obolibrary.org/obo/ARO_3008235 KPC-105 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Class A beta-lactamase KPC-105. http://purl.obolibrary.org/obo/ARO_3008236 KPC-106 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Class A beta-lactamase KPC-106. http://purl.obolibrary.org/obo/ARO_3008237 KPC-107 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Class A beta-lactamase KPC-107. http://purl.obolibrary.org/obo/ARO_3008238 KPC-108 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Class A beta-lactamase KPC-108. http://purl.obolibrary.org/obo/ARO_3008239 KPC-109 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase KPC-109. http://purl.obolibrary.org/obo/ARO_3008240 KPC-110 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant class A beta-lactamase KPC-110. http://purl.obolibrary.org/obo/ARO_3008241 KPC-111 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant class A beta-lactamase KPC-111. http://purl.obolibrary.org/obo/ARO_3008242 KPC-112 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant extended-spectrum class A beta-lactamase KPC-112. http://purl.obolibrary.org/obo/ARO_3008243 KPC-113 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase KPC-113. http://purl.obolibrary.org/obo/ARO_3008244 KPC-114 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase KPC-114. http://purl.obolibrary.org/obo/ARO_3008245 KPC-115 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant class A beta-lactamase KPC-115. http://purl.obolibrary.org/obo/ARO_3008246 KPC-116 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-116. http://purl.obolibrary.org/obo/ARO_3008247 KPC-117 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase KPC-117. http://purl.obolibrary.org/obo/ARO_3008248 KPC-118 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-118. http://purl.obolibrary.org/obo/ARO_3008249 KPC-119 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-119. http://purl.obolibrary.org/obo/ARO_3008250 KPC-120 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-120. http://purl.obolibrary.org/obo/ARO_3008251 KPC-121 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-121. http://purl.obolibrary.org/obo/ARO_3008252 KPC-122 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-122. http://purl.obolibrary.org/obo/ARO_3008253 KPC-124 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase KPC-124. http://purl.obolibrary.org/obo/ARO_3008254 KPC-126 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-126. http://purl.obolibrary.org/obo/ARO_3008255 KPC-127 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-127. http://purl.obolibrary.org/obo/ARO_3008256 KPC-128 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-128. http://purl.obolibrary.org/obo/ARO_3008257 KPC-129 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Class A beta-lactamase KPC-129. http://purl.obolibrary.org/obo/ARO_3008258 KPC-130 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Class A beta-lactamase KPC-130. http://purl.obolibrary.org/obo/ARO_3008259 KPC-131 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-131. http://purl.obolibrary.org/obo/ARO_3008260 KPC-132 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant class A beta-lactamase KPC-132. http://purl.obolibrary.org/obo/ARO_3008261 KPC-133 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-133. http://purl.obolibrary.org/obo/ARO_3008262 KPC-136 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-136. http://purl.obolibrary.org/obo/ARO_3008263 KPC-137 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant class A beta-lactamase KPC-137. http://purl.obolibrary.org/obo/ARO_3008264 KPC-138 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant extended-spectrum class A beta-lactamase KPC-138. http://purl.obolibrary.org/obo/ARO_3008265 KPC-139 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase KPC-139. http://purl.obolibrary.org/obo/ARO_3008266 KPC-140 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase KPC-140. http://purl.obolibrary.org/obo/ARO_3008267 KPC-141 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase KPC-141. http://purl.obolibrary.org/obo/ARO_3008268 KPC-142 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase KPC-142. http://purl.obolibrary.org/obo/ARO_3008269 KPC-143 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase KPC-143. http://purl.obolibrary.org/obo/ARO_3008270 KPC-144 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase KPC-144. http://purl.obolibrary.org/obo/ARO_3008271 KPC-145 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant extended-spectrum class A beta-lactamase KPC-145. http://purl.obolibrary.org/obo/ARO_3008272 KPC-146 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-146. http://purl.obolibrary.org/obo/ARO_3008273 KPC-147 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-147. http://purl.obolibrary.org/obo/ARO_3008274 KPC-148 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Class A beta-lactamase KPC-148. http://purl.obolibrary.org/obo/ARO_3008275 KPC-149 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-149. http://purl.obolibrary.org/obo/ARO_3008276 KPC-150 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant class A beta-lactamase KPC-150. http://purl.obolibrary.org/obo/ARO_3008277 KPC-151 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant extended-spectrum class A beta-lactamase KPC-151. http://purl.obolibrary.org/obo/ARO_3008278 KPC-152 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant extended-spectrum class A beta-lactamase KPC-152. http://purl.obolibrary.org/obo/ARO_3008279 KPC-153 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant extended-spectrum class A beta-lactamase KPC-153. http://purl.obolibrary.org/obo/ARO_3008280 KPC-154 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant extended-spectrum class A beta-lactamase KPC-154. http://purl.obolibrary.org/obo/ARO_3008281 KPC-155 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant class A beta-lactamase KPC-155. http://purl.obolibrary.org/obo/ARO_3008282 KPC-156 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-156. http://purl.obolibrary.org/obo/ARO_3008283 KPC-157 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-157. http://purl.obolibrary.org/obo/ARO_3008284 KPC-158 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase KPC-158. http://purl.obolibrary.org/obo/ARO_3008285 KPC-159 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant extended-spectrum class A beta-lactamase KPC-159. http://purl.obolibrary.org/obo/ARO_3008286 KPC-160 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-160. http://purl.obolibrary.org/obo/ARO_3008287 KPC-161 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-161. http://purl.obolibrary.org/obo/ARO_3008288 KPC-162 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-162. http://purl.obolibrary.org/obo/ARO_3008289 KPC-163 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-163. http://purl.obolibrary.org/obo/ARO_3008290 KPC-164 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-164. http://purl.obolibrary.org/obo/ARO_3008291 KPC-165 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-165. http://purl.obolibrary.org/obo/ARO_3008292 KPC-166 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-166. http://purl.obolibrary.org/obo/ARO_3008293 KPC-167 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Class A beta-lactamase KPC-167. http://purl.obolibrary.org/obo/ARO_3008294 KPC-168 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase KPC-168. http://purl.obolibrary.org/obo/ARO_3008295 KPC-169 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant extended-spectrum class A beta-lactamase KPC-169. http://purl.obolibrary.org/obo/ARO_3008296 KPC-170 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant extended-spectrum class A beta-lactamase KPC-170. http://purl.obolibrary.org/obo/ARO_3008297 KPC-171 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase KPC-171. http://purl.obolibrary.org/obo/ARO_3008298 KPC-172 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant extended-spectrum class A beta-lactamase KPC-172. http://purl.obolibrary.org/obo/ARO_3008299 KPC-173 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant extended-spectrum class A beta-lactamase KPC-173. http://purl.obolibrary.org/obo/ARO_3008300 KPC-174 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase KPC-174. http://purl.obolibrary.org/obo/ARO_3008301 KPC-175 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant extended-spectrum class A beta-lactamase KPC-175. http://purl.obolibrary.org/obo/ARO_3008302 KPC-176 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase KPC-176. http://purl.obolibrary.org/obo/ARO_3008303 KPC-177 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase KPC-177. http://purl.obolibrary.org/obo/ARO_3008304 KPC-178 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant class A beta-lactamase KPC-178. http://purl.obolibrary.org/obo/ARO_3008305 KPC-179 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Class A beta-lactamase KPC-179. http://purl.obolibrary.org/obo/ARO_3008306 KPC-180 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase KPC-180. http://purl.obolibrary.org/obo/ARO_3008307 KPC-181 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-181. http://purl.obolibrary.org/obo/ARO_3008308 KPC-182 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-182. http://purl.obolibrary.org/obo/ARO_3008309 KPC-183 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-183. http://purl.obolibrary.org/obo/ARO_3008310 KPC-184 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-184. http://purl.obolibrary.org/obo/ARO_3008311 KPC-185 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant extended-spectrum class A beta-lactamase KPC-185. http://purl.obolibrary.org/obo/ARO_3008312 KPC-186 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant extended-spectrum class A beta-lactamase KPC-186. http://purl.obolibrary.org/obo/ARO_3008313 KPC-187 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant class A beta-lactamase KPC-187. http://purl.obolibrary.org/obo/ARO_3008314 KPC-188 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant class A beta-lactamase KPC-188. http://purl.obolibrary.org/obo/ARO_3008315 KPC-189 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Extended-spectrum class A beta-lactamase KPC-189. http://purl.obolibrary.org/obo/ARO_3008316 KPC-190 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant class A beta-lactamase KPC-190. http://purl.obolibrary.org/obo/ARO_3008317 KPC-191 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant class A beta-lactamase KPC-191. http://purl.obolibrary.org/obo/ARO_3008318 KPC-192 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase KPC-192. http://purl.obolibrary.org/obo/ARO_3008319 KPC-193 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Class A beta-lactamase KPC-193. http://purl.obolibrary.org/obo/ARO_3008320 KPC-194 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant extended-spectrum class A beta-lactamase KPC-194. http://purl.obolibrary.org/obo/ARO_3008321 KPC-195 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-195. http://purl.obolibrary.org/obo/ARO_3008322 KPC-196 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase KPC-196. http://purl.obolibrary.org/obo/ARO_3008323 KPC-197 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant extended-spectrum class A beta-lactamase KPC-197. http://purl.obolibrary.org/obo/ARO_3008324 KPC-201 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant extended-spectrum class A beta-lactamase KPC-201. http://purl.obolibrary.org/obo/ARO_3008325 KPC-202 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase KPC-202. http://purl.obolibrary.org/obo/ARO_3008326 KPC-203 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant extended-spectrum class A beta-lactamase KPC-203. http://purl.obolibrary.org/obo/ARO_3008327 KPC-204 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase KPC-204. http://purl.obolibrary.org/obo/ARO_3008328 KPC-205 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant class A beta-lactamase KPC-205. http://purl.obolibrary.org/obo/ARO_3008329 KPC-206 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant extended-spectrum class A beta-lactamase KPC-206. http://purl.obolibrary.org/obo/ARO_3008330 KPC-207 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant extended-spectrum class A beta-lactamase KPC-207. http://purl.obolibrary.org/obo/ARO_3008331 KPC-208 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant extended-spectrum class A beta-lactamase KPC-208. http://purl.obolibrary.org/obo/ARO_3008332 KPC-209 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant extended-spectrum class A beta-lactamase KPC-209. http://purl.obolibrary.org/obo/ARO_3008333 KPC-211 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-211. http://purl.obolibrary.org/obo/ARO_3008334 KPC-212 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-212. http://purl.obolibrary.org/obo/ARO_3008335 KPC-213 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase KPC-213. http://purl.obolibrary.org/obo/ARO_3008336 KPC-214 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase KPC-214. http://purl.obolibrary.org/obo/ARO_3008337 KPC-215 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase KPC-215. http://purl.obolibrary.org/obo/ARO_3008338 KPC-216 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase KPC-216. http://purl.obolibrary.org/obo/ARO_3008339 KPC-217 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant class A beta-lactamase KPC-217. http://purl.obolibrary.org/obo/ARO_3008340 KPC-218 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant class A beta-lactamase KPC-218. http://purl.obolibrary.org/obo/ARO_3008341 KPC-223 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-223. http://purl.obolibrary.org/obo/ARO_3008342 KPC-224 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase KPC-224. http://purl.obolibrary.org/obo/ARO_3008343 KPC-225 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase KPC-225. http://purl.obolibrary.org/obo/ARO_3008344 KPC-226 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant extended-spectrum class A beta-lactamase KPC-226. http://purl.obolibrary.org/obo/ARO_3008345 KPC-227 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase KPC-227. http://purl.obolibrary.org/obo/ARO_3008346 KPC-228 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant extended-spectrum class A beta-lactamase KPC-228. http://purl.obolibrary.org/obo/ARO_3008347 KPC-230 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant extended-spectrum class A beta-lactamase KPC-230. http://purl.obolibrary.org/obo/ARO_3008348 KPC-231 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-231. http://purl.obolibrary.org/obo/ARO_3008349 KPC-232 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-232. http://purl.obolibrary.org/obo/ARO_3008350 KPC-233 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase KPC-233. http://purl.obolibrary.org/obo/ARO_3008351 KPC-234 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase KPC-234. http://purl.obolibrary.org/obo/ARO_3008352 KPC-236 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-236. http://purl.obolibrary.org/obo/ARO_3008353 KPC-237 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-237. http://purl.obolibrary.org/obo/ARO_3008354 KPC-238 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-238. http://purl.obolibrary.org/obo/ARO_3008355 KPC-239 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-239. http://purl.obolibrary.org/obo/ARO_3008356 KPC-240 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-240. http://purl.obolibrary.org/obo/ARO_3008357 KPC-241 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-241. http://purl.obolibrary.org/obo/ARO_3008358 KPC-242 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-242. http://purl.obolibrary.org/obo/ARO_3008359 KPC-47 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant extended-spectrum class A beta-lactamase KPC-47. http://purl.obolibrary.org/obo/ARO_3008360 KPC-48 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant extended-spectrum class A beta-lactamase KPC-48. http://purl.obolibrary.org/obo/ARO_3008361 KPC-53 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant extended-spectrum class A beta-lactamase KPC-53. http://purl.obolibrary.org/obo/ARO_3008362 KPC-67 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase KPC-67. http://purl.obolibrary.org/obo/ARO_3008363 KPC-68 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant extended-spectrum class A beta-lactamase KPC-68. http://purl.obolibrary.org/obo/ARO_3008364 KPC-69 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant extended-spectrum class A beta-lactamase KPC-69. http://purl.obolibrary.org/obo/ARO_3008365 KPC-70 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant extended-spectrum class A beta-lactamase KPC-70. http://purl.obolibrary.org/obo/ARO_3008366 KPC-84 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant carbapenem-hydrolyzing class A beta-lactamase KPC-84. http://purl.obolibrary.org/obo/ARO_3008367 KPC-85 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-85. http://purl.obolibrary.org/obo/ARO_3008368 KPC-88 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant extended-spectrum class A beta-lactamase KPC-88. http://purl.obolibrary.org/obo/ARO_3008369 KPC-89 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-89. http://purl.obolibrary.org/obo/ARO_3008370 KPC-91 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase KPC-91. http://purl.obolibrary.org/obo/ARO_3008371 KPC-92 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase Inhibitor-resistant extended-spectrum class A beta-lactamase KPC-92. http://purl.obolibrary.org/obo/ARO_3008372 LHK-7 http://purl.obolibrary.org/obo/ARO_3005418 LHK beta-lactamase Class C beta-lactamase LHK-7. http://purl.obolibrary.org/obo/ARO_3008373 MIR-24 http://purl.obolibrary.org/obo/ARO_3000058 MIR beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase MIR-24. http://purl.obolibrary.org/obo/ARO_3008374 MIR-25 http://purl.obolibrary.org/obo/ARO_3000058 MIR beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase MIR-25. http://purl.obolibrary.org/obo/ARO_3008375 MIR-27 http://purl.obolibrary.org/obo/ARO_3000058 MIR beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase MIR-27. http://purl.obolibrary.org/obo/ARO_3008376 MIR-28 http://purl.obolibrary.org/obo/ARO_3000058 MIR beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase MIR-28. http://purl.obolibrary.org/obo/ARO_3008377 MIR-30 http://purl.obolibrary.org/obo/ARO_3000058 MIR beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase MIR-30. http://purl.obolibrary.org/obo/ARO_3008378 MIR-31 http://purl.obolibrary.org/obo/ARO_3000058 MIR beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase MIR-31. http://purl.obolibrary.org/obo/ARO_3008379 MIR-32 http://purl.obolibrary.org/obo/ARO_3000058 MIR beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase MIR-32. http://purl.obolibrary.org/obo/ARO_3008380 MIR-33 http://purl.obolibrary.org/obo/ARO_3000058 MIR beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase MIR-33. http://purl.obolibrary.org/obo/ARO_3008381 MIR-34 http://purl.obolibrary.org/obo/ARO_3000058 MIR beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase MIR-34. http://purl.obolibrary.org/obo/ARO_3008382 MIR-35 http://purl.obolibrary.org/obo/ARO_3000058 MIR beta-lactamase Cephalosporin-hydrolyzing class C beta-lactamase MIR-35. http://purl.obolibrary.org/obo/ARO_3008383 MOX-15 http://purl.obolibrary.org/obo/ARO_3000083 MOX beta-lactamase CMY-1/MOX family class C beta-lactamase MOX-15. http://purl.obolibrary.org/obo/ARO_3008384 MOX-16 http://purl.obolibrary.org/obo/ARO_3000083 MOX beta-lactamase CMY-1/MOX family class C beta-lactamase MOX-16. http://purl.obolibrary.org/obo/ARO_3008385 MOX-17 http://purl.obolibrary.org/obo/ARO_3000083 MOX beta-lactamase CMY-1/MOX family class C beta-lactamase MOX-17. http://purl.obolibrary.org/obo/ARO_3008386 MOX-18 http://purl.obolibrary.org/obo/ARO_3000083 MOX beta-lactamase CMY-1/MOX family class C beta-lactamase MOX-18. http://purl.obolibrary.org/obo/ARO_3008387 MOX-19 http://purl.obolibrary.org/obo/ARO_3000083 MOX beta-lactamase CMY-1/MOX family class C beta-lactamase MOX-19. http://purl.obolibrary.org/obo/ARO_3008388 MOX-20 http://purl.obolibrary.org/obo/ARO_3000083 MOX beta-lactamase CMY-1/MOX family class C beta-lactamase MOX-20. http://purl.obolibrary.org/obo/ARO_3008389 MOX-21 http://purl.obolibrary.org/obo/ARO_3000083 MOX beta-lactamase CMY-1/MOX family class C beta-lactamase MOX-21. http://purl.obolibrary.org/obo/ARO_3008390 MOX-22 http://purl.obolibrary.org/obo/ARO_3000083 MOX beta-lactamase CMY-1/MOX family class C beta-lactamase MOX-22. http://purl.obolibrary.org/obo/ARO_3008391 MOX-23 http://purl.obolibrary.org/obo/ARO_3000083 MOX beta-lactamase CMY-1/MOX family class C beta-lactamase MOX-23. http://purl.obolibrary.org/obo/ARO_3008392 MOX-24 http://purl.obolibrary.org/obo/ARO_3000083 MOX beta-lactamase CMY-1/MOX family class C beta-lactamase MOX-24. http://purl.obolibrary.org/obo/ARO_3008393 MOX-25 http://purl.obolibrary.org/obo/ARO_3000083 MOX beta-lactamase CMY-1/MOX family class C beta-lactamase MOX-25. http://purl.obolibrary.org/obo/ARO_3008394 MUN-1 http://purl.obolibrary.org/obo/ARO_3007871 MUN beta-lactamase MUN family extended-spectrum class A beta-lactamase MUN-1. http://purl.obolibrary.org/obo/ARO_3008395 MUN-6 http://purl.obolibrary.org/obo/ARO_3007871 MUN beta-lactamase MUN family extended-spectrum class A beta-lactamase MUN-6. http://purl.obolibrary.org/obo/ARO_3008396 NDM-48 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase Subclass B1 metallo-beta-lactamase NDM-48. http://purl.obolibrary.org/obo/ARO_3008397 NDM-49 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase Subclass B1 metallo-beta-lactamase NDM-49. http://purl.obolibrary.org/obo/ARO_3008398 NDM-50 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase Subclass B1 metallo-beta-lactamase NDM-50. http://purl.obolibrary.org/obo/ARO_3008399 NDM-51 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase Subclass B1 metallo-beta-lactamase NDM-51. http://purl.obolibrary.org/obo/ARO_3008400 NDM-52 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase Subclass B1 metallo-beta-lactamase NDM-52. http://purl.obolibrary.org/obo/ARO_3008401 NDM-53 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase Subclass B1 metallo-beta-lactamase NDM-53. http://purl.obolibrary.org/obo/ARO_3008402 NDM-54 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase Subclass B1 metallo-beta-lactamase NDM-54. http://purl.obolibrary.org/obo/ARO_3008403 NDM-55 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase Subclass B1 metallo-beta-lactamase NDM-55. http://purl.obolibrary.org/obo/ARO_3008404 NDM-56 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase Subclass B1 metallo-beta-lactamase NDM-56. http://purl.obolibrary.org/obo/ARO_3008405 NDM-57 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase Subclass B1 metallo-beta-lactamase NDM-57. http://purl.obolibrary.org/obo/ARO_3008406 NDM-58 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase Subclass B1 metallo-beta-lactamase NDM-58. http://purl.obolibrary.org/obo/ARO_3008407 NDM-60 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase Subclass B1 metallo-beta-lactamase NDM-60. http://purl.obolibrary.org/obo/ARO_3008408 NDM-61 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase Subclass B1 metallo-beta-lactamase NDM-61. http://purl.obolibrary.org/obo/ARO_3008409 NDM-64 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase Subclass B1 metallo-beta-lactamase NDM-64. http://purl.obolibrary.org/obo/ARO_3008410 NDM-65 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase Subclass B1 metallo-beta-lactamase NDM-65. http://purl.obolibrary.org/obo/ARO_3008411 NDM-66 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase Subclass B1 metallo-beta-lactamase NDM-66. http://purl.obolibrary.org/obo/ARO_3008412 NDM-67 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase Subclass B1 metallo-beta-lactamase NDM-67. http://purl.obolibrary.org/obo/ARO_3008413 NDM-68 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase Subclass B1 metallo-beta-lactamase NDM-68. http://purl.obolibrary.org/obo/ARO_3008414 NDM-69 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase Subclass B1 metallo-beta-lactamase NDM-69. http://purl.obolibrary.org/obo/ARO_3008415 NDM-70 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase Subclass B1 metallo-beta-lactamase NDM-70. http://purl.obolibrary.org/obo/ARO_3008416 NDM-71 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase Subclass B1 metallo-beta-lactamase NDM-71. http://purl.obolibrary.org/obo/ARO_3008417 NDM-72 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase Subclass B1 metallo-beta-lactamase NDM-72. http://purl.obolibrary.org/obo/ARO_3008418 NDM-73 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase Subclass B1 metallo-beta-lactamase NDM-73. http://purl.obolibrary.org/obo/ARO_3008419 NDM-74 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase Subclass B1 metallo-beta-lactamase NDM-74. http://purl.obolibrary.org/obo/ARO_3008421 OXA-1000 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-213 family carbapenem-hydrolyzing class D beta-lactamase OXA-1000. http://purl.obolibrary.org/obo/ARO_3008422 OXA-1001 http://purl.obolibrary.org/obo/ARO_3007709 OXA-229-like beta-lactamase OXA-229 family carbapenem-hydrolyzing class D beta-lactamase OXA-1001. http://purl.obolibrary.org/obo/ARO_3008423 OXA-1002 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-213 family carbapenem-hydrolyzing class D beta-lactamase OXA-1002. http://purl.obolibrary.org/obo/ARO_3008424 OXA-1003 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-213 family carbapenem-hydrolyzing class D beta-lactamase OXA-1003. http://purl.obolibrary.org/obo/ARO_3008425 OXA-1004 http://purl.obolibrary.org/obo/ARO_3007715 OXA-294-like beta-lactamase OXA-294 family class D beta-lactamase OXA-1004. http://purl.obolibrary.org/obo/ARO_3008426 OXA-1005 http://purl.obolibrary.org/obo/ARO_3007700 OXA-134-like beta-lactamase OXA-134 family carbapenem-hydrolyzing class D beta-lactamase OXA-1005. http://purl.obolibrary.org/obo/ARO_3008427 OXA-1006 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase Class D beta-lactamase OXA-1006. http://purl.obolibrary.org/obo/ARO_3008428 OXA-1007 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-213 family carbapenem-hydrolyzing class D beta-lactamase OXA-1007. http://purl.obolibrary.org/obo/ARO_3008429 OXA-1008 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-213 family carbapenem-hydrolyzing class D beta-lactamase OXA-1008. http://purl.obolibrary.org/obo/ARO_3008430 OXA-1009 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-213 family carbapenem-hydrolyzing class D beta-lactamase OXA-1009. http://purl.obolibrary.org/obo/ARO_3008431 OXA-1010 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-213 family carbapenem-hydrolyzing class D beta-lactamase OXA-1010. http://purl.obolibrary.org/obo/ARO_3008432 OXA-1011 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase Class D beta-lactamase OXA-1011. http://purl.obolibrary.org/obo/ARO_3008433 OXA-1012 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-48 family class D beta-lactamase OXA-1012. http://purl.obolibrary.org/obo/ARO_3008434 OXA-1013 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1013. http://purl.obolibrary.org/obo/ARO_3008435 OXA-1014 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1014. http://purl.obolibrary.org/obo/ARO_3008436 OXA-1015 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-10 family class D beta-lactamase OXA-1015. http://purl.obolibrary.org/obo/ARO_3008437 OXA-1016 http://purl.obolibrary.org/obo/ARO_3007717 OXA-372-like beta-lactamase OXA-372 family carbapenem-hydrolyzing class D beta-lactamase OXA-1016. http://purl.obolibrary.org/obo/ARO_3008438 OXA-1017 http://purl.obolibrary.org/obo/ARO_3007704 OXA-2-like beta-lactamase OXA-2 family class D beta-lactamase OXA-1017. http://purl.obolibrary.org/obo/ARO_3008439 OXA-1018 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1018. http://purl.obolibrary.org/obo/ARO_3008440 OXA-1019 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1019. http://purl.obolibrary.org/obo/ARO_3008441 OXA-1020 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1020. http://purl.obolibrary.org/obo/ARO_3008442 OXA-1021 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1021. http://purl.obolibrary.org/obo/ARO_3008443 OXA-1022 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1022. http://purl.obolibrary.org/obo/ARO_3008444 OXA-1023 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1023. http://purl.obolibrary.org/obo/ARO_3008445 OXA-1024 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1024. http://purl.obolibrary.org/obo/ARO_3008446 OXA-1025 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1025. http://purl.obolibrary.org/obo/ARO_3008447 OXA-1026 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1026. http://purl.obolibrary.org/obo/ARO_3008448 OXA-1027 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1027. http://purl.obolibrary.org/obo/ARO_3008449 OXA-1028 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1028. http://purl.obolibrary.org/obo/ARO_3008450 OXA-1029 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1029. http://purl.obolibrary.org/obo/ARO_3008451 OXA-1030 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1030. http://purl.obolibrary.org/obo/ARO_3008452 OXA-1031 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1031. http://purl.obolibrary.org/obo/ARO_3008453 OXA-1032 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1032. http://purl.obolibrary.org/obo/ARO_3008454 OXA-1033 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1033. http://purl.obolibrary.org/obo/ARO_3008455 OXA-1034 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1034. http://purl.obolibrary.org/obo/ARO_3008456 OXA-1035 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1035. http://purl.obolibrary.org/obo/ARO_3008457 OXA-1036 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase Carbapenem-hydrolyzing class D beta-lactamase OXA-1036. http://purl.obolibrary.org/obo/ARO_3008458 OXA-1037 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase Class D beta-lactamase OXA-1037. http://purl.obolibrary.org/obo/ARO_3008459 OXA-1040 http://purl.obolibrary.org/obo/ARO_3007711 OXA-24-like beta-lactamase OXA-24 family carbapenem-hydrolyzing class D beta-lactamase OXA-1040. http://purl.obolibrary.org/obo/ARO_3008460 OXA-1041 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase Carbapenem-hydrolyzing class D beta-lactamase OXA-1041. http://purl.obolibrary.org/obo/ARO_3008461 OXA-1042 http://purl.obolibrary.org/obo/ARO_3007696 OXA-1-like beta-lactamase OXA-1 family class D beta-lactamase OXA-1042. http://purl.obolibrary.org/obo/ARO_3008462 OXA-1043 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase Class D beta-lactamase OXA-1043. http://purl.obolibrary.org/obo/ARO_3008463 OXA-1044 http://purl.obolibrary.org/obo/ARO_3007705 OXA-211-like beta-lactamase OXA-211 family carbapenem-hydrolyzing class D beta-lactamase OXA-1044. http://purl.obolibrary.org/obo/ARO_3008464 OXA-1045 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-213 family carbapenem-hydrolyzing class D beta-lactamase OXA-1045. http://purl.obolibrary.org/obo/ARO_3008465 OXA-1046 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-10 family class D beta-lactamase OXA-1046. http://purl.obolibrary.org/obo/ARO_3008466 OXA-1047 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1047. http://purl.obolibrary.org/obo/ARO_3008467 OXA-1048 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1048. http://purl.obolibrary.org/obo/ARO_3008468 OXA-1049 http://purl.obolibrary.org/obo/ARO_3007704 OXA-2-like beta-lactamase OXA-2 family class D beta-lactamase OXA-1049. http://purl.obolibrary.org/obo/ARO_3008469 OXA-1050 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-213 family carbapenem-hydrolyzing class D beta-lactamase OXA-1050. http://purl.obolibrary.org/obo/ARO_3008470 OXA-1051 http://purl.obolibrary.org/obo/ARO_3007733 OXA-679-like beta-lactamase OXA-679 family carbapenem-hydrolyzing class D beta-lactamase OXA-1051. http://purl.obolibrary.org/obo/ARO_3008471 OXA-1052 http://purl.obolibrary.org/obo/ARO_3007709 OXA-229-like beta-lactamase OXA-229 family carbapenem-hydrolyzing class D beta-lactamase OXA-1052. http://purl.obolibrary.org/obo/ARO_3008472 OXA-1053 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-10 family class D beta-lactamase OXA-1053. http://purl.obolibrary.org/obo/ARO_3008473 OXA-1055 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-48 family class D beta-lactamase OXA-1055. http://purl.obolibrary.org/obo/ARO_3008474 OXA-1056 http://purl.obolibrary.org/obo/ARO_3007703 OXA-198-like beta-lactamase OXA-198 family carbapenem-hydrolyzing class D beta-lactamase OXA-1056. http://purl.obolibrary.org/obo/ARO_3008475 OXA-1057 http://purl.obolibrary.org/obo/ARO_3007703 OXA-198-like beta-lactamase OXA-198 family carbapenem-hydrolyzing class D beta-lactamase OXA-1057. http://purl.obolibrary.org/obo/ARO_3008476 OXA-1058 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1058. http://purl.obolibrary.org/obo/ARO_3008477 OXA-1059 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1059. http://purl.obolibrary.org/obo/ARO_3008478 OXA-1060 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1060. http://purl.obolibrary.org/obo/ARO_3008479 OXA-1061 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1061. http://purl.obolibrary.org/obo/ARO_3008480 OXA-1062 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1062. http://purl.obolibrary.org/obo/ARO_3008481 OXA-1063 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1063. http://purl.obolibrary.org/obo/ARO_3008482 OXA-1064 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1064. http://purl.obolibrary.org/obo/ARO_3008483 OXA-1065 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1065. http://purl.obolibrary.org/obo/ARO_3008484 OXA-1066 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1066. http://purl.obolibrary.org/obo/ARO_3008485 OXA-1067 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1067. http://purl.obolibrary.org/obo/ARO_3008486 OXA-1068 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1068. http://purl.obolibrary.org/obo/ARO_3008487 OXA-1069 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1069. http://purl.obolibrary.org/obo/ARO_3008488 OXA-1070 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1070. http://purl.obolibrary.org/obo/ARO_3008489 OXA-1071 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1071. http://purl.obolibrary.org/obo/ARO_3008490 OXA-1072 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1072. http://purl.obolibrary.org/obo/ARO_3008491 OXA-1073 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1073. http://purl.obolibrary.org/obo/ARO_3008492 OXA-1074 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1074. http://purl.obolibrary.org/obo/ARO_3008493 OXA-1075 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1075. http://purl.obolibrary.org/obo/ARO_3008494 OXA-1076 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1076. http://purl.obolibrary.org/obo/ARO_3008495 OXA-1077 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1077. http://purl.obolibrary.org/obo/ARO_3008496 OXA-1078 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1078. http://purl.obolibrary.org/obo/ARO_3008497 OXA-1079 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1079. http://purl.obolibrary.org/obo/ARO_3008498 OXA-1080 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1080. http://purl.obolibrary.org/obo/ARO_3008499 OXA-1081 http://purl.obolibrary.org/obo/ARO_3007711 OXA-24-like beta-lactamase OXA-24 family carbapenem-hydrolyzing class D beta-lactamase OXA-1081. http://purl.obolibrary.org/obo/ARO_3008500 OXA-1082 http://purl.obolibrary.org/obo/ARO_3007704 OXA-2-like beta-lactamase OXA-2 family class D beta-lactamase OXA-1082. http://purl.obolibrary.org/obo/ARO_3008501 OXA-1083 http://purl.obolibrary.org/obo/ARO_3007704 OXA-2-like beta-lactamase OXA-2 family class D beta-lactamase OXA-1083. http://purl.obolibrary.org/obo/ARO_3008502 OXA-1084 http://purl.obolibrary.org/obo/ARO_3007704 OXA-2-like beta-lactamase OXA-2 family class D beta-lactamase OXA-1084. http://purl.obolibrary.org/obo/ARO_3008503 OXA-1085 http://purl.obolibrary.org/obo/ARO_3007704 OXA-2-like beta-lactamase OXA-2 family class D beta-lactamase OXA-1085. http://purl.obolibrary.org/obo/ARO_3008504 OXA-1086 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-10 family class D beta-lactamase OXA-1086. http://purl.obolibrary.org/obo/ARO_3008505 OXA-1087 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-10 family class D beta-lactamase OXA-1087. http://purl.obolibrary.org/obo/ARO_3008506 OXA-1088 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-10 family class D beta-lactamase OXA-1088. http://purl.obolibrary.org/obo/ARO_3008507 OXA-1089 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase Carbapenem-hydrolyzing class D beta-lactamase OXA-1089. http://purl.obolibrary.org/obo/ARO_3008508 OXA-1090 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase Carbapenem-hydrolyzing class D beta-lactamase OXA-1090. http://purl.obolibrary.org/obo/ARO_3008509 OXA-1091 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase Oxacillin-hydrolyzing class D beta-lactamase OXA-1091. http://purl.obolibrary.org/obo/ARO_3008510 OXA-1092 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1092. http://purl.obolibrary.org/obo/ARO_3008511 OXA-1093 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1093. http://purl.obolibrary.org/obo/ARO_3008512 OXA-1094 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1094. http://purl.obolibrary.org/obo/ARO_3008513 OXA-1095 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-23 family carbapenem-hydrolyzing class D beta-lactamase OXA-1095. http://purl.obolibrary.org/obo/ARO_3008514 OXA-1096 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1096. http://purl.obolibrary.org/obo/ARO_3008515 OXA-1097 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1097. http://purl.obolibrary.org/obo/ARO_3008516 OXA-1098 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1098. http://purl.obolibrary.org/obo/ARO_3008517 OXA-1099 http://purl.obolibrary.org/obo/ARO_3007732 OXA-63-like beta-lactamase OXA-63 family oxacillin-hydrolyzing class D beta-lactamase OXA-1099. http://purl.obolibrary.org/obo/ARO_3008518 OXA-1100 http://purl.obolibrary.org/obo/ARO_3007732 OXA-63-like beta-lactamase OXA-63 family oxacillin-hydrolyzing class D beta-lactamase OXA-1100. http://purl.obolibrary.org/obo/ARO_3008519 OXA-1101 http://purl.obolibrary.org/obo/ARO_3007732 OXA-63-like beta-lactamase OXA-63 family oxacillin-hydrolyzing class D beta-lactamase OXA-1101. http://purl.obolibrary.org/obo/ARO_3008520 OXA-1102 http://purl.obolibrary.org/obo/ARO_3007732 OXA-63-like beta-lactamase OXA-63 family oxacillin-hydrolyzing class D beta-lactamase OXA-1102. http://purl.obolibrary.org/obo/ARO_3008521 OXA-1103 http://purl.obolibrary.org/obo/ARO_3007732 OXA-63-like beta-lactamase OXA-63 family oxacillin-hydrolyzing class D beta-lactamase OXA-1103. http://purl.obolibrary.org/obo/ARO_3008522 OXA-1104 http://purl.obolibrary.org/obo/ARO_3007732 OXA-63-like beta-lactamase OXA-63 family oxacillin-hydrolyzing class D beta-lactamase OXA-1104. http://purl.obolibrary.org/obo/ARO_3008523 OXA-1105 http://purl.obolibrary.org/obo/ARO_3007732 OXA-63-like beta-lactamase OXA-63 family oxacillin-hydrolyzing class D beta-lactamase OXA-1105. http://purl.obolibrary.org/obo/ARO_3008524 OXA-1106 http://purl.obolibrary.org/obo/ARO_3007732 OXA-63-like beta-lactamase OXA-63 family oxacillin-hydrolyzing class D beta-lactamase OXA-1106. http://purl.obolibrary.org/obo/ARO_3008525 OXA-1107 http://purl.obolibrary.org/obo/ARO_3007732 OXA-63-like beta-lactamase OXA-63 family oxacillin-hydrolyzing class D beta-lactamase OXA-1107. http://purl.obolibrary.org/obo/ARO_3008526 OXA-1108 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase Class D beta-lactamase OXA-1108. http://purl.obolibrary.org/obo/ARO_3008527 OXA-1109 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1109. http://purl.obolibrary.org/obo/ARO_3008528 OXA-1110 http://purl.obolibrary.org/obo/ARO_3007700 OXA-134-like beta-lactamase OXA-134 family carbapenem-hydrolyzing class D beta-lactamase OXA-1110. http://purl.obolibrary.org/obo/ARO_3008529 OXA-1111 http://purl.obolibrary.org/obo/ARO_3007700 OXA-134-like beta-lactamase OXA-134 family carbapenem-hydrolyzing class D beta-lactamase OXA-1111. http://purl.obolibrary.org/obo/ARO_3008530 OXA-1112 http://purl.obolibrary.org/obo/ARO_3007700 OXA-134-like beta-lactamase OXA-134 family carbapenem-hydrolyzing class D beta-lactamase OXA-1112. http://purl.obolibrary.org/obo/ARO_3008531 OXA-1113 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-213 family carbapenem-hydrolyzing class D beta-lactamase OXA-1113. http://purl.obolibrary.org/obo/ARO_3008532 OXA-1114 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-213 family carbapenem-hydrolyzing class D beta-lactamase OXA-1114. http://purl.obolibrary.org/obo/ARO_3008533 OXA-1115 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-213 family carbapenem-hydrolyzing class D beta-lactamase OXA-1115. http://purl.obolibrary.org/obo/ARO_3008534 OXA-1116 http://purl.obolibrary.org/obo/ARO_3007700 OXA-134-like beta-lactamase OXA-134 family carbapenem-hydrolyzing class D beta-lactamase OXA-1116. http://purl.obolibrary.org/obo/ARO_3008535 OXA-1117 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1117. http://purl.obolibrary.org/obo/ARO_3008536 OXA-1118 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1118. http://purl.obolibrary.org/obo/ARO_3008537 OXA-1119 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-48 family class D beta-lactamase OXA-1119. http://purl.obolibrary.org/obo/ARO_3008538 OXA-1120 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-10 family class D beta-lactamase OXA-1120. http://purl.obolibrary.org/obo/ARO_3008539 OXA-1121 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1121. http://purl.obolibrary.org/obo/ARO_3008540 OXA-1122 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1122. http://purl.obolibrary.org/obo/ARO_3008541 OXA-1123 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1123. http://purl.obolibrary.org/obo/ARO_3008542 OXA-1124 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1124. http://purl.obolibrary.org/obo/ARO_3008543 OXA-1125 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1125. http://purl.obolibrary.org/obo/ARO_3008544 OXA-1126 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1126. http://purl.obolibrary.org/obo/ARO_3008545 OXA-1127 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1127. http://purl.obolibrary.org/obo/ARO_3008546 OXA-1128 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1128. http://purl.obolibrary.org/obo/ARO_3008547 OXA-1129 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1129. http://purl.obolibrary.org/obo/ARO_3008548 OXA-1130 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1130. http://purl.obolibrary.org/obo/ARO_3008549 OXA-1131 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1131. http://purl.obolibrary.org/obo/ARO_3008550 OXA-1132 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1132. http://purl.obolibrary.org/obo/ARO_3008551 OXA-1133 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1133. http://purl.obolibrary.org/obo/ARO_3008552 OXA-1134 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1134. http://purl.obolibrary.org/obo/ARO_3008553 OXA-1135 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1135. http://purl.obolibrary.org/obo/ARO_3008554 OXA-1136 http://purl.obolibrary.org/obo/ARO_3007704 OXA-2-like beta-lactamase OXA-2 family class D beta-lactamase OXA-1136. http://purl.obolibrary.org/obo/ARO_3008555 OXA-1137 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-213 family carbapenem-hydrolyzing class D beta-lactamase OXA-1137. http://purl.obolibrary.org/obo/ARO_3008556 OXA-1138 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-213 family carbapenem-hydrolyzing class D beta-lactamase OXA-1138. http://purl.obolibrary.org/obo/ARO_3008557 OXA-1139 http://purl.obolibrary.org/obo/ARO_3007701 OXA-143-like beta-lactamase OXA-143 family carbapenem-hydrolyzing class D beta-lactamase OXA-1139. http://purl.obolibrary.org/obo/ARO_3008558 OXA-1140 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1140. http://purl.obolibrary.org/obo/ARO_3008559 OXA-1141 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-10 family class D beta-lactamase OXA-1141. http://purl.obolibrary.org/obo/ARO_3008560 OXA-1142 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase Class D beta-lactamase OXA-1142. http://purl.obolibrary.org/obo/ARO_3008561 OXA-1143 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase Class D beta-lactamase OXA-1143. http://purl.obolibrary.org/obo/ARO_3008562 OXA-1144 http://purl.obolibrary.org/obo/ARO_3007709 OXA-229-like beta-lactamase OXA-229 family carbapenem-hydrolyzing class D beta-lactamase OXA-1144. http://purl.obolibrary.org/obo/ARO_3008563 OXA-1145 http://purl.obolibrary.org/obo/ARO_3007714 OXA-286-like beta-lactamase OXA-286 family carbapenem-hydrolyzing class D beta-lactamase OXA-1145. http://purl.obolibrary.org/obo/ARO_3008564 OXA-1146 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-48 family class D beta-lactamase OXA-1146. http://purl.obolibrary.org/obo/ARO_3008565 OXA-1147 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-10 family class D beta-lactamase OXA-1147. http://purl.obolibrary.org/obo/ARO_3008566 OXA-1148 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-10 family class D beta-lactamase OXA-1148. http://purl.obolibrary.org/obo/ARO_3008567 OXA-1149 http://purl.obolibrary.org/obo/ARO_3007731 OXA-62-like beta-lactamase OXA-62 family carbapenem-hydrolyzing class D beta-lactamase OXA-1149. http://purl.obolibrary.org/obo/ARO_3008568 OXA-1150 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-213 family carbapenem-hydrolyzing class D beta-lactamase OXA-1150. http://purl.obolibrary.org/obo/ARO_3008569 OXA-1151 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-213 family carbapenem-hydrolyzing class D beta-lactamase OXA-1151. http://purl.obolibrary.org/obo/ARO_3008570 OXA-1152 http://purl.obolibrary.org/obo/ARO_3007731 OXA-62-like beta-lactamase OXA-62 family carbapenem-hydrolyzing class D beta-lactamase OXA-1152. http://purl.obolibrary.org/obo/ARO_3008571 OXA-1153 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase Class D beta-lactamase OXA-1153. http://purl.obolibrary.org/obo/ARO_3008572 OXA-1154 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase Class D beta-lactamase OXA-1154. http://purl.obolibrary.org/obo/ARO_3008573 OXA-1155 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase Class D beta-lactamase OXA-1155. http://purl.obolibrary.org/obo/ARO_3008574 OXA-1156 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase Class D beta-lactamase OXA-1156. http://purl.obolibrary.org/obo/ARO_3008575 OXA-1157 http://purl.obolibrary.org/obo/ARO_3007699 OXA-12-like beta-lactamase OXA-12 family class D beta-lactamase OXA-1157. http://purl.obolibrary.org/obo/ARO_3008576 OXA-1158 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase Class D beta-lactamase OXA-1158. http://purl.obolibrary.org/obo/ARO_3008577 OXA-1159 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase Class D beta-lactamase OXA-1159. http://purl.obolibrary.org/obo/ARO_3008578 OXA-1160 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase Class D beta-lactamase OXA-1160. http://purl.obolibrary.org/obo/ARO_3008579 OXA-1161 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase Class D beta-lactamase OXA-1161. http://purl.obolibrary.org/obo/ARO_3008580 OXA-1162 http://purl.obolibrary.org/obo/ARO_3007699 OXA-12-like beta-lactamase OXA-12 family class D beta-lactamase OXA-1162. http://purl.obolibrary.org/obo/ARO_3008581 OXA-1163 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase Class D beta-lactamase OXA-1163. http://purl.obolibrary.org/obo/ARO_3008582 OXA-1164 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-213 family carbapenem-hydrolyzing class D beta-lactamase OXA-1164. http://purl.obolibrary.org/obo/ARO_3008583 OXA-1165 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-213 family carbapenem-hydrolyzing class D beta-lactamase OXA-1165. http://purl.obolibrary.org/obo/ARO_3008584 OXA-1166 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-213 family carbapenem-hydrolyzing class D beta-lactamase OXA-1166. http://purl.obolibrary.org/obo/ARO_3008585 OXA-1167 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-48 family class D beta-lactamase OXA-1167. http://purl.obolibrary.org/obo/ARO_3008586 OXA-1168 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-10 family class D beta-lactamase OXA-1168. http://purl.obolibrary.org/obo/ARO_3008587 OXA-1169 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-10 family class D beta-lactamase OXA-1169. http://purl.obolibrary.org/obo/ARO_3008588 OXA-1170 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-10 family class D beta-lactamase OXA-1170. http://purl.obolibrary.org/obo/ARO_3008589 OXA-1171 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-10 family class D beta-lactamase OXA-1171. http://purl.obolibrary.org/obo/ARO_3008590 OXA-1172 http://purl.obolibrary.org/obo/ARO_3007704 OXA-2-like beta-lactamase OXA-2 family class D beta-lactamase OXA-1172. http://purl.obolibrary.org/obo/ARO_3008591 OXA-1173 http://purl.obolibrary.org/obo/ARO_3007704 OXA-2-like beta-lactamase OXA-2 family class D beta-lactamase OXA-1173. http://purl.obolibrary.org/obo/ARO_3008592 OXA-1174 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1174. http://purl.obolibrary.org/obo/ARO_3008593 OXA-1175 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-10 family class D beta-lactamase OXA-1175. http://purl.obolibrary.org/obo/ARO_3008594 OXA-1176 http://purl.obolibrary.org/obo/ARO_3007729 OXA-60-like beta-lactamase OXA-60 family carbapenem-hydrolyzing class D beta-lactamase OXA-1176. http://purl.obolibrary.org/obo/ARO_3008595 OXA-1177 http://purl.obolibrary.org/obo/ARO_3007708 OXA-22-like beta-lactamase OXA-22 family class D beta-lactamase OXA-1177. http://purl.obolibrary.org/obo/ARO_3008596 OXA-1178 http://purl.obolibrary.org/obo/ARO_3007728 OXA-58-like beta-lactamase OXA-58 family carbapenem-hydrolyzing class D beta-lactamase OXA-1178. http://purl.obolibrary.org/obo/ARO_3008597 OXA-1181 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-48 family class D beta-lactamase OXA-1181. http://purl.obolibrary.org/obo/ARO_3008598 OXA-1182 http://purl.obolibrary.org/obo/ARO_3007701 OXA-143-like beta-lactamase OXA-143 family carbapenem-hydrolyzing class D beta-lactamase OXA-1182. http://purl.obolibrary.org/obo/ARO_3008599 OXA-1183 http://purl.obolibrary.org/obo/ARO_3007704 OXA-2-like beta-lactamase OXA-2 family class D beta-lactamase OXA-1183. http://purl.obolibrary.org/obo/ARO_3008600 OXA-1184 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-10 family class D beta-lactamase OXA-1184. http://purl.obolibrary.org/obo/ARO_3008601 OXA-1185 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-213 family carbapenem-hydrolyzing class D beta-lactamase OXA-1185. http://purl.obolibrary.org/obo/ARO_3008602 OXA-1186 http://purl.obolibrary.org/obo/ARO_3007703 OXA-198-like beta-lactamase OXA-198 family carbapenem-hydrolyzing class D beta-lactamase OXA-1186. http://purl.obolibrary.org/obo/ARO_3008603 OXA-1187 http://purl.obolibrary.org/obo/ARO_3007704 OXA-2-like beta-lactamase OXA-2 family class D beta-lactamase OXA-1187. http://purl.obolibrary.org/obo/ARO_3008604 OXA-1188 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1188. http://purl.obolibrary.org/obo/ARO_3008605 OXA-1189 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-213 family carbapenem-hydrolyzing class D beta-lactamase OXA-1189. http://purl.obolibrary.org/obo/ARO_3008606 OXA-1190 http://purl.obolibrary.org/obo/ARO_3007709 OXA-229-like beta-lactamase OXA-229 family carbapenem-hydrolyzing class D beta-lactamase OXA-1190. http://purl.obolibrary.org/obo/ARO_3008607 OXA-1191 http://purl.obolibrary.org/obo/ARO_3007709 OXA-229-like beta-lactamase OXA-229 family carbapenem-hydrolyzing class D beta-lactamase OXA-1191. http://purl.obolibrary.org/obo/ARO_3008608 OXA-1193 http://purl.obolibrary.org/obo/ARO_3007709 OXA-229-like beta-lactamase OXA-229 family carbapenem-hydrolyzing class D beta-lactamase OXA-1193. http://purl.obolibrary.org/obo/ARO_3008609 OXA-1194 http://purl.obolibrary.org/obo/ARO_3007709 OXA-229-like beta-lactamase OXA-229 family carbapenem-hydrolyzing class D beta-lactamase OXA-1194. http://purl.obolibrary.org/obo/ARO_3008610 OXA-1198 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1198. http://purl.obolibrary.org/obo/ARO_3008611 OXA-1199 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1199. http://purl.obolibrary.org/obo/ARO_3008612 OXA-1200 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-48 family class D beta-lactamase OXA-1200. http://purl.obolibrary.org/obo/ARO_3008613 OXA-1201 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-48 family class D beta-lactamase OXA-1201. http://purl.obolibrary.org/obo/ARO_3008614 OXA-1202 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-10 family class D beta-lactamase OXA-1202. http://purl.obolibrary.org/obo/ARO_3008615 OXA-1203 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-10 family class D beta-lactamase OXA-1203. http://purl.obolibrary.org/obo/ARO_3008616 OXA-1204 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-10 family class D beta-lactamase OXA-1204. http://purl.obolibrary.org/obo/ARO_3008617 OXA-1205 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-48 family class D beta-lactamase OXA-1205. http://purl.obolibrary.org/obo/ARO_3008618 OXA-1206 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase Class D beta-lactamase OXA-1206. http://purl.obolibrary.org/obo/ARO_3008619 OXA-1207 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-48 family class D beta-lactamase OXA-1207. http://purl.obolibrary.org/obo/ARO_3008620 OXA-1208 http://purl.obolibrary.org/obo/ARO_3007705 OXA-211-like beta-lactamase OXA-211 family carbapenem-hydrolyzing class D beta-lactamase OXA-1208. http://purl.obolibrary.org/obo/ARO_3008621 OXA-1211 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-48 family class D beta-lactamase OXA-1211. http://purl.obolibrary.org/obo/ARO_3008622 OXA-1212 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-48 family class D beta-lactamase OXA-1212. http://purl.obolibrary.org/obo/ARO_3008623 OXA-1213 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-48 family class D beta-lactamase OXA-1213. http://purl.obolibrary.org/obo/ARO_3008624 OXA-1214 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1214. http://purl.obolibrary.org/obo/ARO_3008625 OXA-1215 http://purl.obolibrary.org/obo/ARO_3007714 OXA-286-like beta-lactamase OXA-286 family carbapenem-hydrolyzing class D beta-lactamase OXA-1215. http://purl.obolibrary.org/obo/ARO_3008626 OXA-1216 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-23 family carbapenem-hydrolyzing class D beta-lactamase OXA-1216. http://purl.obolibrary.org/obo/ARO_3008627 OXA-1217 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1217. http://purl.obolibrary.org/obo/ARO_3008628 OXA-1218 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1218. http://purl.obolibrary.org/obo/ARO_3008629 OXA-1219 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1219. http://purl.obolibrary.org/obo/ARO_3008630 OXA-1220 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1220. http://purl.obolibrary.org/obo/ARO_3008631 OXA-1221 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-23 family carbapenem-hydrolyzing class D beta-lactamase OXA-1221. http://purl.obolibrary.org/obo/ARO_3008632 OXA-1222 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-213 family carbapenem-hydrolyzing class D beta-lactamase OXA-1222. http://purl.obolibrary.org/obo/ARO_3008633 OXA-1223 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-23 family carbapenem-hydrolyzing class D beta-lactamase OXA-1223. http://purl.obolibrary.org/obo/ARO_3008634 OXA-1224 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-213 family carbapenem-hydrolyzing class D beta-lactamase OXA-1224. http://purl.obolibrary.org/obo/ARO_3008635 OXA-1225 http://purl.obolibrary.org/obo/ARO_3007711 OXA-24-like beta-lactamase OXA-24 family carbapenem-hydrolyzing class D beta-lactamase OXA-1225. http://purl.obolibrary.org/obo/ARO_3008636 OXA-1226 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-48 family class D beta-lactamase OXA-1226. http://purl.obolibrary.org/obo/ARO_3008637 OXA-1227 http://purl.obolibrary.org/obo/ARO_3007731 OXA-62-like beta-lactamase OXA-62 family carbapenem-hydrolyzing class D beta-lactamase OXA-1227. http://purl.obolibrary.org/obo/ARO_3008638 OXA-1228 http://purl.obolibrary.org/obo/ARO_3007731 OXA-62-like beta-lactamase OXA-62 family carbapenem-hydrolyzing class D beta-lactamase OXA-1228. http://purl.obolibrary.org/obo/ARO_3008639 OXA-1229 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1229. http://purl.obolibrary.org/obo/ARO_3008640 OXA-1230 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1230. http://purl.obolibrary.org/obo/ARO_3008641 OXA-1231 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-10 family class D beta-lactamase OXA-1231. http://purl.obolibrary.org/obo/ARO_3008642 OXA-1232 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-10 family class D beta-lactamase OXA-1232. http://purl.obolibrary.org/obo/ARO_3008643 OXA-1233 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-10 family class D beta-lactamase OXA-1233. http://purl.obolibrary.org/obo/ARO_3008644 OXA-1234 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-213 family carbapenem-hydrolyzing class D beta-lactamase OXA-1234. http://purl.obolibrary.org/obo/ARO_3008645 OXA-1235 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-213 family carbapenem-hydrolyzing class D beta-lactamase OXA-1235. http://purl.obolibrary.org/obo/ARO_3008646 OXA-1236 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-23 family carbapenem-hydrolyzing class D beta-lactamase OXA-1236. http://purl.obolibrary.org/obo/ARO_3008647 OXA-1237 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-213 family carbapenem-hydrolyzing class D beta-lactamase OXA-1237. http://purl.obolibrary.org/obo/ARO_3008648 OXA-1238 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase Class D beta-lactamase OXA-1238. http://purl.obolibrary.org/obo/ARO_3008649 OXA-1239 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase Carbapenem-hydrolyzing class D beta-lactamase OXA-1239. http://purl.obolibrary.org/obo/ARO_3008650 OXA-1240 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-48 family class D beta-lactamase OXA-1240. http://purl.obolibrary.org/obo/ARO_3008651 OXA-1241 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-23 family carbapenem-hydrolyzing class D beta-lactamase OXA-1241. http://purl.obolibrary.org/obo/ARO_3008652 OXA-1242 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-48 family class D beta-lactamase OXA-1242. http://purl.obolibrary.org/obo/ARO_3008653 OXA-1243 http://purl.obolibrary.org/obo/ARO_3007704 OXA-2-like beta-lactamase OXA-2 family class D beta-lactamase OXA-1243. http://purl.obolibrary.org/obo/ARO_3008654 OXA-1244 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1244. http://purl.obolibrary.org/obo/ARO_3008655 OXA-1245 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1245. http://purl.obolibrary.org/obo/ARO_3008656 OXA-1246 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1246. http://purl.obolibrary.org/obo/ARO_3008657 OXA-1247 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-10 family class D beta-lactamase OXA-1247. http://purl.obolibrary.org/obo/ARO_3008658 OXA-1248 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-10 family class D beta-lactamase OXA-1248. http://purl.obolibrary.org/obo/ARO_3008659 OXA-1249 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1249. http://purl.obolibrary.org/obo/ARO_3008660 OXA-1250 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1250. http://purl.obolibrary.org/obo/ARO_3008661 OXA-1251 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-258 family class D beta-lactamase OXA-1251. http://purl.obolibrary.org/obo/ARO_3008662 OXA-1252 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1252. http://purl.obolibrary.org/obo/ARO_3008663 OXA-1253 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1253. http://purl.obolibrary.org/obo/ARO_3008664 OXA-1254 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1254. http://purl.obolibrary.org/obo/ARO_3008665 OXA-1255 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1255. http://purl.obolibrary.org/obo/ARO_3008666 OXA-1256 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1256. http://purl.obolibrary.org/obo/ARO_3008667 OXA-1257 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-10 family class D beta-lactamase OXA-1257. http://purl.obolibrary.org/obo/ARO_3008668 OXA-1258 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase Class D beta-lactamase OXA-1258. http://purl.obolibrary.org/obo/ARO_3008669 OXA-1259 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-1258 family class D beta-lactamase OXA-1259. http://purl.obolibrary.org/obo/ARO_3008670 OXA-1260 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-1258 family class D beta-lactamase OXA-1260. http://purl.obolibrary.org/obo/ARO_3008671 OXA-1261 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-1258 family class D beta-lactamase OXA-1261. http://purl.obolibrary.org/obo/ARO_3008672 OXA-1262 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase OXA-1258 family class D beta-lactamase OXA-1262. http://purl.obolibrary.org/obo/ARO_3008673 OXA-1263 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase OXA-1258 family class D beta-lactamase OXA-1263. http://purl.obolibrary.org/obo/ARO_3008674 OXA-1264 http://purl.obolibrary.org/obo/ARO_3007731 OXA-62-like beta-lactamase OXA-62 family carbapenem-hydrolyzing class D beta-lactamase OXA-1264. http://purl.obolibrary.org/obo/ARO_3008675 OXA-1265 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-1265. http://purl.obolibrary.org/obo/ARO_3008676 OXA-1266 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-213 family carbapenem-hydrolyzing class D beta-lactamase OXA-1266. http://purl.obolibrary.org/obo/ARO_3008677 OXA-1267 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1267. http://purl.obolibrary.org/obo/ARO_3008678 OXA-1268 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1268. http://purl.obolibrary.org/obo/ARO_3008679 OXA-1269 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1269. http://purl.obolibrary.org/obo/ARO_3008680 OXA-1270 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1270. http://purl.obolibrary.org/obo/ARO_3008681 OXA-1271 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1271. http://purl.obolibrary.org/obo/ARO_3008682 OXA-1272 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1272. http://purl.obolibrary.org/obo/ARO_3008683 OXA-1273 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1273. http://purl.obolibrary.org/obo/ARO_3008684 OXA-1274 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1274. http://purl.obolibrary.org/obo/ARO_3008685 OXA-1275 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50-var family class D beta-lactamase OXA-1275. http://purl.obolibrary.org/obo/ARO_3008686 OXA-1276 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1276. http://purl.obolibrary.org/obo/ARO_3008687 OXA-1277 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1277. http://purl.obolibrary.org/obo/ARO_3008688 OXA-1278 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1278. http://purl.obolibrary.org/obo/ARO_3008689 OXA-1279 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1279. http://purl.obolibrary.org/obo/ARO_3008690 OXA-1280 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1280. http://purl.obolibrary.org/obo/ARO_3008691 OXA-1281 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1281. http://purl.obolibrary.org/obo/ARO_3008692 OXA-1282 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1282. http://purl.obolibrary.org/obo/ARO_3008693 OXA-1283 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1283. http://purl.obolibrary.org/obo/ARO_3008694 OXA-1284 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50-var family class D beta-lactamase OXA-1284. http://purl.obolibrary.org/obo/ARO_3008695 OXA-1285 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1285. http://purl.obolibrary.org/obo/ARO_3008696 OXA-1286 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1286. http://purl.obolibrary.org/obo/ARO_3008697 OXA-1287 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1287. http://purl.obolibrary.org/obo/ARO_3008698 OXA-1288 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1288. http://purl.obolibrary.org/obo/ARO_3008699 OXA-1289 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1289. http://purl.obolibrary.org/obo/ARO_3008700 OXA-1290 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50-var family class D beta-lactamase OXA-1290. http://purl.obolibrary.org/obo/ARO_3008701 OXA-1291 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1291. http://purl.obolibrary.org/obo/ARO_3008702 OXA-1292 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1292. http://purl.obolibrary.org/obo/ARO_3008703 OXA-1293 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1293. http://purl.obolibrary.org/obo/ARO_3008704 OXA-1294 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50-var family class D beta-lactamase OXA-1294. http://purl.obolibrary.org/obo/ARO_3008705 OXA-1295 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1295. http://purl.obolibrary.org/obo/ARO_3008706 OXA-1296 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1296. http://purl.obolibrary.org/obo/ARO_3008707 OXA-1297 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1297. http://purl.obolibrary.org/obo/ARO_3008708 OXA-1298 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1298. http://purl.obolibrary.org/obo/ARO_3008709 OXA-1299 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1299. http://purl.obolibrary.org/obo/ARO_3008710 OXA-1300 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1300. http://purl.obolibrary.org/obo/ARO_3008711 OXA-1301 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-1301. http://purl.obolibrary.org/obo/ARO_3008712 OXA-1302 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-10 family class D beta-lactamase OXA-1302. http://purl.obolibrary.org/obo/ARO_3008713 OXA-1303 http://purl.obolibrary.org/obo/ARO_3007711 OXA-24-like beta-lactamase OXA-24 family carbapenem-hydrolyzing class D beta-lactamase OXA-1303. http://purl.obolibrary.org/obo/ARO_3008714 OXA-1304 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-48 family class D beta-lactamase OXA-1304. http://purl.obolibrary.org/obo/ARO_3008715 OXA-1305 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-48 family class D beta-lactamase OXA-1305. http://purl.obolibrary.org/obo/ARO_3008716 OXA-1306 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-48 family class D beta-lactamase OXA-1306. http://purl.obolibrary.org/obo/ARO_3008717 OXA-1307 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-48 family class D beta-lactamase OXA-1307. http://purl.obolibrary.org/obo/ARO_3008718 OXA-1308 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-48 family class D beta-lactamase OXA-1308. http://purl.obolibrary.org/obo/ARO_3008719 OXA-1309 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-48 family class D beta-lactamase OXA-1309. http://purl.obolibrary.org/obo/ARO_3008720 OXA-725 http://purl.obolibrary.org/obo/ARO_3007699 OXA-12-like beta-lactamase OXA-12 family class D beta-lactamase AmpS/OXA-725. http://purl.obolibrary.org/obo/ARO_3008721 OXA-790 http://purl.obolibrary.org/obo/ARO_3007698 OXA-114-like beta-lactamase OXA-114 family class D beta-lactamase OXA-790. http://purl.obolibrary.org/obo/ARO_3008722 OXA-791 http://purl.obolibrary.org/obo/ARO_3007698 OXA-114-like beta-lactamase OXA-114 family class D beta-lactamase OXA-791. http://purl.obolibrary.org/obo/ARO_3008723 OXA-933 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-48 family class D beta-lactamase OXA-933. http://purl.obolibrary.org/obo/ARO_3008724 OXA-934 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-48 family class D beta-lactamase OXA-934. http://purl.obolibrary.org/obo/ARO_3008725 OXA-936 http://purl.obolibrary.org/obo/ARO_3007707 OXA-214-like beta-lactamase OXA-214 family carbapenem-hydrolyzing class D beta-lactamase OXA-936. http://purl.obolibrary.org/obo/ARO_3008726 OXA-944 http://purl.obolibrary.org/obo/ARO_3007713 OXA-274-like beta-lactamase OXA-274 family carbapenem-hydrolyzing class D beta-lactamase OXA-944. http://purl.obolibrary.org/obo/ARO_3008727 OXA-950 http://purl.obolibrary.org/obo/ARO_3007699 OXA-12-like beta-lactamase OXA-12 family class D beta-lactamase OXA-950. http://purl.obolibrary.org/obo/ARO_3008728 OXA-951 http://purl.obolibrary.org/obo/ARO_3007699 OXA-12-like beta-lactamase OXA-12 family class D beta-lactamase OXA-951. http://purl.obolibrary.org/obo/ARO_3008729 OXA-952 http://purl.obolibrary.org/obo/ARO_3007709 OXA-229-like beta-lactamase OXA-229 family carbapenem-hydrolyzing class D beta-lactamase OXA-952. http://purl.obolibrary.org/obo/ARO_3008730 OXA-953 http://purl.obolibrary.org/obo/ARO_3007709 OXA-229-like beta-lactamase OXA-229 family carbapenem-hydrolyzing class D beta-lactamase OXA-953. http://purl.obolibrary.org/obo/ARO_3008731 OXA-954 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-954. http://purl.obolibrary.org/obo/ARO_3008732 OXA-955 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-955. http://purl.obolibrary.org/obo/ARO_3008733 OXA-956 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase Class D beta-lactamase OXA-956. http://purl.obolibrary.org/obo/ARO_3008734 OXA-957 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase Class D beta-lactamase OXA-957. http://purl.obolibrary.org/obo/ARO_3008735 OXA-958 http://purl.obolibrary.org/obo/ARO_3007699 OXA-12-like beta-lactamase OXA-12 family class D beta-lactamase OXA-958. http://purl.obolibrary.org/obo/ARO_3008736 OXA-959 http://purl.obolibrary.org/obo/ARO_3007699 OXA-12-like beta-lactamase OXA-12 family class D beta-lactamase OXA-959. http://purl.obolibrary.org/obo/ARO_3008737 OXA-960 http://purl.obolibrary.org/obo/ARO_3007727 OXA-55-like beta-lactamase OXA-55 family carbapenem-hydrolyzing class D beta-lactamase OXA-960. http://purl.obolibrary.org/obo/ARO_3008738 OXA-961 http://purl.obolibrary.org/obo/ARO_3007727 OXA-55-like beta-lactamase OXA-55 family carbapenem-hydrolyzing class D beta-lactamase OXA-961. http://purl.obolibrary.org/obo/ARO_3008739 OXA-962 http://purl.obolibrary.org/obo/ARO_3007727 OXA-55-like beta-lactamase OXA-55 family carbapenem-hydrolyzing class D beta-lactamase OXA-962. http://purl.obolibrary.org/obo/ARO_3008740 OXA-963 http://purl.obolibrary.org/obo/ARO_3007727 OXA-55-like beta-lactamase OXA-55 family carbapenem-hydrolyzing class D beta-lactamase OXA-963. http://purl.obolibrary.org/obo/ARO_3008741 OXA-964 http://purl.obolibrary.org/obo/ARO_3007727 OXA-55-like beta-lactamase OXA-55 family carbapenem-hydrolyzing class D beta-lactamase OXA-964. http://purl.obolibrary.org/obo/ARO_3008742 OXA-965 http://purl.obolibrary.org/obo/ARO_3007727 OXA-55-like beta-lactamase OXA-55 family carbapenem-hydrolyzing class D beta-lactamase OXA-965. http://purl.obolibrary.org/obo/ARO_3008743 OXA-966 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-23 family carbapenem-hydrolyzing class D beta-lactamase OXA-966. http://purl.obolibrary.org/obo/ARO_3008744 OXA-967 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-23 family carbapenem-hydrolyzing class D beta-lactamase OXA-967. http://purl.obolibrary.org/obo/ARO_3008745 OXA-968 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-23 family carbapenem-hydrolyzing class D beta-lactamase OXA-968. http://purl.obolibrary.org/obo/ARO_3008746 OXA-969 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-23 family carbapenem-hydrolyzing class D beta-lactamase OXA-969. http://purl.obolibrary.org/obo/ARO_3008747 OXA-970 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-970. http://purl.obolibrary.org/obo/ARO_3008748 OXA-971 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-971. http://purl.obolibrary.org/obo/ARO_3008749 OXA-972 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-972. http://purl.obolibrary.org/obo/ARO_3008750 OXA-973 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-973. http://purl.obolibrary.org/obo/ARO_3008751 OXA-974 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-974. http://purl.obolibrary.org/obo/ARO_3008752 OXA-975 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-975. http://purl.obolibrary.org/obo/ARO_3008753 OXA-976 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-976. http://purl.obolibrary.org/obo/ARO_3008754 OXA-977 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 family carbapenem-hydrolyzing class D beta-lactamase OXA-977. http://purl.obolibrary.org/obo/ARO_3008755 OXA-978 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-213 family carbapenem-hydrolyzing class D beta-lactamase OXA-978. http://purl.obolibrary.org/obo/ARO_3008756 OXA-979 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-213 family carbapenem-hydrolyzing class D beta-lactamase OXA-979. http://purl.obolibrary.org/obo/ARO_3008757 OXA-980 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-213 family carbapenem-hydrolyzing class D beta-lactamase OXA-980. http://purl.obolibrary.org/obo/ARO_3008758 OXA-981 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase Class D beta-lactamase OXA-981. http://purl.obolibrary.org/obo/ARO_3008759 OXA-982 http://purl.obolibrary.org/obo/ARO_3007715 OXA-294-like beta-lactamase OXA-294 family class D beta-lactamase OXA-982. http://purl.obolibrary.org/obo/ARO_3008760 OXA-983 http://purl.obolibrary.org/obo/ARO_3007709 OXA-229-like beta-lactamase OXA-229 family carbapenem-hydrolyzing class D beta-lactamase OXA-983. http://purl.obolibrary.org/obo/ARO_3008761 OXA-984 http://purl.obolibrary.org/obo/ARO_3007715 OXA-294-like beta-lactamase OXA-294 family class D beta-lactamase OXA-984. http://purl.obolibrary.org/obo/ARO_3008762 OXA-985 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-213 family carbapenem-hydrolyzing class D beta-lactamase OXA-985. http://purl.obolibrary.org/obo/ARO_3008763 OXA-986 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-213 family carbapenem-hydrolyzing class D beta-lactamase OXA-986. http://purl.obolibrary.org/obo/ARO_3008764 OXA-987 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-213 family carbapenem-hydrolyzing class D beta-lactamase OXA-987. http://purl.obolibrary.org/obo/ARO_3008765 OXA-988 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-213 family carbapenem-hydrolyzing class D beta-lactamase OXA-988. http://purl.obolibrary.org/obo/ARO_3008766 OXA-989 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-213 family carbapenem-hydrolyzing class D beta-lactamase OXA-989. http://purl.obolibrary.org/obo/ARO_3008767 OXA-990 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-213 family carbapenem-hydrolyzing class D beta-lactamase OXA-990. http://purl.obolibrary.org/obo/ARO_3008768 OXA-991 http://purl.obolibrary.org/obo/ARO_3007700 OXA-134-like beta-lactamase OXA-134 family carbapenem-hydrolyzing class D beta-lactamase OXA-991. http://purl.obolibrary.org/obo/ARO_3008769 OXA-992 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-213 family carbapenem-hydrolyzing class D beta-lactamase OXA-992. http://purl.obolibrary.org/obo/ARO_3008770 OXA-993 http://purl.obolibrary.org/obo/ARO_3007715 OXA-294-like beta-lactamase OXA-294 family class D beta-lactamase OXA-993. http://purl.obolibrary.org/obo/ARO_3008771 OXA-994 http://purl.obolibrary.org/obo/ARO_3007715 OXA-294-like beta-lactamase OXA-294 family class D beta-lactamase OXA-994. http://purl.obolibrary.org/obo/ARO_3008772 OXA-995 http://purl.obolibrary.org/obo/ARO_3007715 OXA-294-like beta-lactamase OXA-294 family class D beta-lactamase OXA-995. http://purl.obolibrary.org/obo/ARO_3008773 OXA-996 http://purl.obolibrary.org/obo/ARO_3007715 OXA-294-like beta-lactamase OXA-294 family class D beta-lactamase OXA-996. http://purl.obolibrary.org/obo/ARO_3008774 OXA-997 http://purl.obolibrary.org/obo/ARO_3007715 OXA-294-like beta-lactamase OXA-294 family class D beta-lactamase OXA-997. http://purl.obolibrary.org/obo/ARO_3008775 OXA-998 http://purl.obolibrary.org/obo/ARO_3007715 OXA-294-like beta-lactamase OXA-294 family class D beta-lactamase OXA-998. http://purl.obolibrary.org/obo/ARO_3008776 OXA-999 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase Class D beta-lactamase OXA-999. http://purl.obolibrary.org/obo/ARO_3008777 OXY-1-11 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-1-11. http://purl.obolibrary.org/obo/ARO_3008778 OXY-1-12 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-1-12. http://purl.obolibrary.org/obo/ARO_3008779 OXY-1-13 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-1-13. http://purl.obolibrary.org/obo/ARO_3008780 OXY-1-16 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-1-16. http://purl.obolibrary.org/obo/ARO_3008781 OXY-1-17 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-1-17. http://purl.obolibrary.org/obo/ARO_3008782 OXY-1-18 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-1-18. http://purl.obolibrary.org/obo/ARO_3008783 OXY-1-19 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-1-19. http://purl.obolibrary.org/obo/ARO_3008784 OXY-10-1 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-10-1. http://purl.obolibrary.org/obo/ARO_3008785 OXY-11-1 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-11-1. http://purl.obolibrary.org/obo/ARO_3008786 OXY-12-1 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-12-1. http://purl.obolibrary.org/obo/ARO_3008787 OXY-12-2 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-12-2. http://purl.obolibrary.org/obo/ARO_3008788 OXY-2-17 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-2-17. http://purl.obolibrary.org/obo/ARO_3008789 OXY-2-18 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-2-18. http://purl.obolibrary.org/obo/ARO_3008790 OXY-2-19 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-2-19. http://purl.obolibrary.org/obo/ARO_3008791 OXY-2-20 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-2-20. http://purl.obolibrary.org/obo/ARO_3008792 OXY-2-21 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-2-21. http://purl.obolibrary.org/obo/ARO_3008793 OXY-2-22 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-2-22. http://purl.obolibrary.org/obo/ARO_3008794 OXY-2-23 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-2-23. http://purl.obolibrary.org/obo/ARO_3008795 OXY-2-24 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-2-24. http://purl.obolibrary.org/obo/ARO_3008796 OXY-2-25 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-2-25. http://purl.obolibrary.org/obo/ARO_3008797 OXY-2-26 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-2-26. http://purl.obolibrary.org/obo/ARO_3008798 OXY-2-27 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-2-27. http://purl.obolibrary.org/obo/ARO_3008799 OXY-2-28 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-2-28. http://purl.obolibrary.org/obo/ARO_3008800 OXY-2-30 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-2-30. http://purl.obolibrary.org/obo/ARO_3008801 OXY-3-2 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-3-2. http://purl.obolibrary.org/obo/ARO_3008802 OXY-3-3 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-3-3. http://purl.obolibrary.org/obo/ARO_3008803 OXY-4-2 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-4-2. http://purl.obolibrary.org/obo/ARO_3008804 OXY-4-3 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-4-3. http://purl.obolibrary.org/obo/ARO_3008805 OXY-4-4 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-4-4. http://purl.obolibrary.org/obo/ARO_3008806 OXY-4-5 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-4-5. http://purl.obolibrary.org/obo/ARO_3008807 OXY-5-10 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-5-10. http://purl.obolibrary.org/obo/ARO_3008808 OXY-5-11 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-5-11. http://purl.obolibrary.org/obo/ARO_3008809 OXY-5-6 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-5-6. http://purl.obolibrary.org/obo/ARO_3008810 OXY-5-7 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-5-7. http://purl.obolibrary.org/obo/ARO_3008811 OXY-5-8 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-5-8. http://purl.obolibrary.org/obo/ARO_3008812 OXY-6-10 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-6-10. http://purl.obolibrary.org/obo/ARO_3008813 OXY-6-11 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-6-11. http://purl.obolibrary.org/obo/ARO_3008814 OXY-6-5 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-6-5. http://purl.obolibrary.org/obo/ARO_3008815 OXY-6-7 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-6-7. http://purl.obolibrary.org/obo/ARO_3008816 OXY-7-1 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-7-1. http://purl.obolibrary.org/obo/ARO_3008817 OXY-8-1 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-8-1. http://purl.obolibrary.org/obo/ARO_3008818 OXY-8-2 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-8-2. http://purl.obolibrary.org/obo/ARO_3008819 OXY-8-3 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-8-3. http://purl.obolibrary.org/obo/ARO_3008820 OXY-9-1 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase Extended-spectrum class A beta-lactamase OXY-9-1. http://purl.obolibrary.org/obo/ARO_3008821 PAD-1 http://purl.obolibrary.org/obo/ARO_3007872 PAD beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase PAD-1. http://purl.obolibrary.org/obo/ARO_3008822 PAM-5 http://purl.obolibrary.org/obo/ARO_3007198 PAM beta-lactamase Subclass B3 metallo-beta-lactamase PAM-5. http://purl.obolibrary.org/obo/ARO_3008823 PC1 http://purl.obolibrary.org/obo/ARO_3004197 BlaZ beta-lactamase BlaZ family penicillin-hydrolyzing class A beta-lactamase PC1. http://purl.obolibrary.org/obo/ARO_3008824 PDC-477 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Inhibitor-resistant class C beta-lactamase PDC-477. http://purl.obolibrary.org/obo/ARO_3008825 PDC-478 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Inhibitor-resistant class C beta-lactamase PDC-478. http://purl.obolibrary.org/obo/ARO_3008826 PDC-479 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Inhibitor-resistant extended-spectrum class C beta-lactamase PDC-479. http://purl.obolibrary.org/obo/ARO_3008827 PDC-480 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Inhibitor-resistant extended-spectrum class C beta-lactamase PDC-480. http://purl.obolibrary.org/obo/ARO_3008828 PDC-481 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Inhibitor-resistant extended-spectrum class C beta-lactamase PDC-481. http://purl.obolibrary.org/obo/ARO_3008829 PDC-482 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Inhibitor-resistant extended-spectrum class C beta-lactamase PDC-482. http://purl.obolibrary.org/obo/ARO_3008830 PDC-483 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Inhibitor-resistant class C beta-lactamase PDC-483. http://purl.obolibrary.org/obo/ARO_3008831 PDC-484 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-484. http://purl.obolibrary.org/obo/ARO_3008832 PDC-485 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-485. http://purl.obolibrary.org/obo/ARO_3008833 PDC-486 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-486. http://purl.obolibrary.org/obo/ARO_3008834 PDC-487 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Inhibitor-resistant extended-spectrum class C beta-lactamase PDC-487. http://purl.obolibrary.org/obo/ARO_3008835 PDC-488 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-488. http://purl.obolibrary.org/obo/ARO_3008836 PDC-489 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-489. http://purl.obolibrary.org/obo/ARO_3008837 PDC-490 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-490. http://purl.obolibrary.org/obo/ARO_3008838 PDC-491 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-491. http://purl.obolibrary.org/obo/ARO_3008839 PDC-492 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-492. http://purl.obolibrary.org/obo/ARO_3008840 PDC-493 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-493. http://purl.obolibrary.org/obo/ARO_3008841 PDC-494 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-494. http://purl.obolibrary.org/obo/ARO_3008842 PDC-495 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-495. http://purl.obolibrary.org/obo/ARO_3008843 PDC-496 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-496. http://purl.obolibrary.org/obo/ARO_3008844 PDC-497 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Inhibitor-resistant extended-spectrum class C beta-lactamase PDC-497. http://purl.obolibrary.org/obo/ARO_3008845 PDC-498 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-498. http://purl.obolibrary.org/obo/ARO_3008846 PDC-499 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-499. http://purl.obolibrary.org/obo/ARO_3008847 PDC-500 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Inhibitor-resistant class C beta-lactamase PDC-500. http://purl.obolibrary.org/obo/ARO_3008848 PDC-501 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-501. http://purl.obolibrary.org/obo/ARO_3008849 PDC-502 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-502. http://purl.obolibrary.org/obo/ARO_3008850 PDC-503 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-503. http://purl.obolibrary.org/obo/ARO_3008851 PDC-504 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-504. http://purl.obolibrary.org/obo/ARO_3008852 PDC-505 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-505. http://purl.obolibrary.org/obo/ARO_3008853 PDC-506 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-506. http://purl.obolibrary.org/obo/ARO_3008854 PDC-507 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-507. http://purl.obolibrary.org/obo/ARO_3008855 PDC-508 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-508. http://purl.obolibrary.org/obo/ARO_3008856 PDC-509 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-509. http://purl.obolibrary.org/obo/ARO_3008857 PDC-510 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Inhibitor-resistant class C beta-lactamase PDC-510. http://purl.obolibrary.org/obo/ARO_3008858 PDC-511 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-511. http://purl.obolibrary.org/obo/ARO_3008859 PDC-512 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-512. http://purl.obolibrary.org/obo/ARO_3008860 PDC-513 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-513. http://purl.obolibrary.org/obo/ARO_3008861 PDC-514 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-514. http://purl.obolibrary.org/obo/ARO_3008862 PDC-515 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Inhibitor-resistant extended-spectrum class C beta-lactamase PDC-515. http://purl.obolibrary.org/obo/ARO_3008863 PDC-516 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-516. http://purl.obolibrary.org/obo/ARO_3008864 PDC-517 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-517. http://purl.obolibrary.org/obo/ARO_3008865 PDC-518 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-518. http://purl.obolibrary.org/obo/ARO_3008866 PDC-519 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Inhibitor-resistant cephalosporin-hydrolyzing class C beta-lactamase PDC-519. http://purl.obolibrary.org/obo/ARO_3008867 PDC-520 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-520. http://purl.obolibrary.org/obo/ARO_3008868 PDC-521 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-521. http://purl.obolibrary.org/obo/ARO_3008869 PDC-522 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-522. http://purl.obolibrary.org/obo/ARO_3008870 PDC-523 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-523. http://purl.obolibrary.org/obo/ARO_3008871 PDC-524 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-524. http://purl.obolibrary.org/obo/ARO_3008872 PDC-525 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-525. http://purl.obolibrary.org/obo/ARO_3008873 PDC-526 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-526. http://purl.obolibrary.org/obo/ARO_3008874 PDC-527 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-527. http://purl.obolibrary.org/obo/ARO_3008875 PDC-528 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-528. http://purl.obolibrary.org/obo/ARO_3008876 PDC-529 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-529. http://purl.obolibrary.org/obo/ARO_3008877 PDC-530 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-530. http://purl.obolibrary.org/obo/ARO_3008878 PDC-531 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Inhibitor-resistant class C beta-lactamase PDC-531. http://purl.obolibrary.org/obo/ARO_3008879 PDC-532 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-532. http://purl.obolibrary.org/obo/ARO_3008880 PDC-533 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-533. http://purl.obolibrary.org/obo/ARO_3008881 PDC-534 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-534. http://purl.obolibrary.org/obo/ARO_3008882 PDC-535 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-535. http://purl.obolibrary.org/obo/ARO_3008883 PDC-536 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-536. http://purl.obolibrary.org/obo/ARO_3008884 PDC-537 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Inhibitor-resistant extended-spectrum class C beta-lactamase PDC-537. http://purl.obolibrary.org/obo/ARO_3008885 PDC-538 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-538. http://purl.obolibrary.org/obo/ARO_3008886 PDC-539 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-539. http://purl.obolibrary.org/obo/ARO_3008887 PDC-540 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-540. http://purl.obolibrary.org/obo/ARO_3008888 PDC-541 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-541. http://purl.obolibrary.org/obo/ARO_3008889 PDC-542 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-542. http://purl.obolibrary.org/obo/ARO_3008890 PDC-543 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-543. http://purl.obolibrary.org/obo/ARO_3008891 PDC-544 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-544. http://purl.obolibrary.org/obo/ARO_3008892 PDC-545 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-545. http://purl.obolibrary.org/obo/ARO_3008893 PDC-546 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-546. http://purl.obolibrary.org/obo/ARO_3008894 PDC-547 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-547. http://purl.obolibrary.org/obo/ARO_3008895 PDC-548 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-548. http://purl.obolibrary.org/obo/ARO_3008896 PDC-549 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-549. http://purl.obolibrary.org/obo/ARO_3008897 PDC-550 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-550. http://purl.obolibrary.org/obo/ARO_3008898 PDC-551 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-551. http://purl.obolibrary.org/obo/ARO_3008899 PDC-552 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-552. http://purl.obolibrary.org/obo/ARO_3008900 PDC-553 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-553. http://purl.obolibrary.org/obo/ARO_3008901 PDC-554 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-554. http://purl.obolibrary.org/obo/ARO_3008902 PDC-555 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-555. http://purl.obolibrary.org/obo/ARO_3008903 PDC-556 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-556. http://purl.obolibrary.org/obo/ARO_3008904 PDC-557 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-557. http://purl.obolibrary.org/obo/ARO_3008905 PDC-558 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-558. http://purl.obolibrary.org/obo/ARO_3008906 PDC-559 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-559. http://purl.obolibrary.org/obo/ARO_3008907 PDC-560 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-560. http://purl.obolibrary.org/obo/ARO_3008908 PDC-561 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-561. http://purl.obolibrary.org/obo/ARO_3008909 PDC-562 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-562. http://purl.obolibrary.org/obo/ARO_3008910 PDC-563 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-563. http://purl.obolibrary.org/obo/ARO_3008911 PDC-564 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-564. http://purl.obolibrary.org/obo/ARO_3008912 PDC-565 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-565. http://purl.obolibrary.org/obo/ARO_3008913 PDC-566 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-566. http://purl.obolibrary.org/obo/ARO_3008914 PDC-567 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-567. http://purl.obolibrary.org/obo/ARO_3008915 PDC-568 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-568. http://purl.obolibrary.org/obo/ARO_3008916 PDC-569 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-569. http://purl.obolibrary.org/obo/ARO_3008917 PDC-570 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-570. http://purl.obolibrary.org/obo/ARO_3008918 PDC-571 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-571. http://purl.obolibrary.org/obo/ARO_3008919 PDC-572 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-572. http://purl.obolibrary.org/obo/ARO_3008920 PDC-573 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-573. http://purl.obolibrary.org/obo/ARO_3008921 PDC-574 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-574. http://purl.obolibrary.org/obo/ARO_3008922 PDC-575 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-575. http://purl.obolibrary.org/obo/ARO_3008923 PDC-576 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-576. http://purl.obolibrary.org/obo/ARO_3008924 PDC-577 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Inhibitor-resistant extended-spectrum class C beta-lactamase PDC-577. http://purl.obolibrary.org/obo/ARO_3008925 PDC-578 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-578. http://purl.obolibrary.org/obo/ARO_3008926 PDC-579 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-579. http://purl.obolibrary.org/obo/ARO_3008927 PDC-580 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-580. http://purl.obolibrary.org/obo/ARO_3008928 PDC-581 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-581. http://purl.obolibrary.org/obo/ARO_3008929 PDC-582 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-582. http://purl.obolibrary.org/obo/ARO_3008930 PDC-583 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-583. http://purl.obolibrary.org/obo/ARO_3008931 PDC-584 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-584. http://purl.obolibrary.org/obo/ARO_3008932 PDC-585 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-585. http://purl.obolibrary.org/obo/ARO_3008933 PDC-586 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-586. http://purl.obolibrary.org/obo/ARO_3008934 PDC-587 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-587. http://purl.obolibrary.org/obo/ARO_3008935 PDC-588 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-588. http://purl.obolibrary.org/obo/ARO_3008936 PDC-589 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-589. http://purl.obolibrary.org/obo/ARO_3008937 PDC-590 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-590. http://purl.obolibrary.org/obo/ARO_3008938 PDC-591 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-591. http://purl.obolibrary.org/obo/ARO_3008939 PDC-592 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-592. http://purl.obolibrary.org/obo/ARO_3008940 PDC-593 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-593. http://purl.obolibrary.org/obo/ARO_3008941 PDC-594 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-594. http://purl.obolibrary.org/obo/ARO_3008942 PDC-595 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-595. http://purl.obolibrary.org/obo/ARO_3008943 PDC-596 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-596. http://purl.obolibrary.org/obo/ARO_3008944 PDC-597 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-597. http://purl.obolibrary.org/obo/ARO_3008945 PDC-598 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-598. http://purl.obolibrary.org/obo/ARO_3008946 PDC-599 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-599. http://purl.obolibrary.org/obo/ARO_3008947 PDC-600 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-600. http://purl.obolibrary.org/obo/ARO_3008948 PDC-601 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-601. http://purl.obolibrary.org/obo/ARO_3008949 PDC-602 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-602. http://purl.obolibrary.org/obo/ARO_3008950 PDC-603 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-603. http://purl.obolibrary.org/obo/ARO_3008951 PDC-604 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-604. http://purl.obolibrary.org/obo/ARO_3008952 PDC-605 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-605. http://purl.obolibrary.org/obo/ARO_3008953 PDC-606 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-606. http://purl.obolibrary.org/obo/ARO_3008954 PDC-607 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-607. http://purl.obolibrary.org/obo/ARO_3008955 PDC-608 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-608. http://purl.obolibrary.org/obo/ARO_3008956 PDC-609 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-609. http://purl.obolibrary.org/obo/ARO_3008957 PDC-610 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-610. http://purl.obolibrary.org/obo/ARO_3008958 PDC-611 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-611. http://purl.obolibrary.org/obo/ARO_3008959 PDC-612 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-612. http://purl.obolibrary.org/obo/ARO_3008960 PDC-613 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-613. http://purl.obolibrary.org/obo/ARO_3008961 PDC-614 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-614. http://purl.obolibrary.org/obo/ARO_3008962 PDC-615 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-615. http://purl.obolibrary.org/obo/ARO_3008963 PDC-616 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-616. http://purl.obolibrary.org/obo/ARO_3008964 PDC-617 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-617. http://purl.obolibrary.org/obo/ARO_3008965 PDC-618 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-618. http://purl.obolibrary.org/obo/ARO_3008966 PDC-619 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-619. http://purl.obolibrary.org/obo/ARO_3008967 PDC-620 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-620. http://purl.obolibrary.org/obo/ARO_3008968 PDC-621 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-621. http://purl.obolibrary.org/obo/ARO_3008969 PDC-622 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-622. http://purl.obolibrary.org/obo/ARO_3008970 PDC-623 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-623. http://purl.obolibrary.org/obo/ARO_3008971 PDC-624 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-624. http://purl.obolibrary.org/obo/ARO_3008972 PDC-625 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-625. http://purl.obolibrary.org/obo/ARO_3008973 PDC-626 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-626. http://purl.obolibrary.org/obo/ARO_3008974 PDC-627 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-627. http://purl.obolibrary.org/obo/ARO_3008975 PDC-628 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-628. http://purl.obolibrary.org/obo/ARO_3008976 PDC-629 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-629. http://purl.obolibrary.org/obo/ARO_3008977 PDC-630 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-630. http://purl.obolibrary.org/obo/ARO_3008978 PDC-631 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-631. http://purl.obolibrary.org/obo/ARO_3008979 PDC-632 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-632. http://purl.obolibrary.org/obo/ARO_3008980 PDC-633 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-633. http://purl.obolibrary.org/obo/ARO_3008981 PDC-634 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-634. http://purl.obolibrary.org/obo/ARO_3008982 PDC-635 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-635. http://purl.obolibrary.org/obo/ARO_3008983 PDC-636 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-636. http://purl.obolibrary.org/obo/ARO_3008984 PDC-637 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-637. http://purl.obolibrary.org/obo/ARO_3008985 PDC-638 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-638. http://purl.obolibrary.org/obo/ARO_3008986 PDC-639 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-639. http://purl.obolibrary.org/obo/ARO_3008987 PDC-640 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase Class C beta-lactamase PDC-640. http://purl.obolibrary.org/obo/ARO_3008988 PEN-A10 http://purl.obolibrary.org/obo/ARO_3007873 PEN-A beta-lactamase Class A beta-lactamase PEN-A10. http://purl.obolibrary.org/obo/ARO_3008989 PEN-A11 http://purl.obolibrary.org/obo/ARO_3007873 PEN-A beta-lactamase Class A beta-lactamase PEN-A11. http://purl.obolibrary.org/obo/ARO_3008990 PEN-A12 http://purl.obolibrary.org/obo/ARO_3007873 PEN-A beta-lactamase Class A beta-lactamase PEN-A12. http://purl.obolibrary.org/obo/ARO_3008991 PEN-A13 http://purl.obolibrary.org/obo/ARO_3007873 PEN-A beta-lactamase Class A beta-lactamase PEN-A13. http://purl.obolibrary.org/obo/ARO_3008992 PEN-A15 http://purl.obolibrary.org/obo/ARO_3007873 PEN-A beta-lactamase Class A beta-lactamase PEN-A15. http://purl.obolibrary.org/obo/ARO_3008993 PEN-A16 http://purl.obolibrary.org/obo/ARO_3007873 PEN-A beta-lactamase Class A beta-lactamase PEN-A16. http://purl.obolibrary.org/obo/ARO_3008994 PEN-A17 http://purl.obolibrary.org/obo/ARO_3007873 PEN-A beta-lactamase Class A beta-lactamase PEN-A17. http://purl.obolibrary.org/obo/ARO_3008995 PEN-A18 http://purl.obolibrary.org/obo/ARO_3007873 PEN-A beta-lactamase Class A beta-lactamase PEN-A18. http://purl.obolibrary.org/obo/ARO_3008996 PEN-A19 http://purl.obolibrary.org/obo/ARO_3007873 PEN-A beta-lactamase Class A beta-lactamase PEN-A19. http://purl.obolibrary.org/obo/ARO_3008997 PEN-A1 http://purl.obolibrary.org/obo/ARO_3007873 PEN-A beta-lactamase Class A beta-lactamase PEN-A1. http://purl.obolibrary.org/obo/ARO_3008998 PEN-A20 http://purl.obolibrary.org/obo/ARO_3007873 PEN-A beta-lactamase Class A beta-lactamase PEN-A20. http://purl.obolibrary.org/obo/ARO_3008999 PEN-A21 http://purl.obolibrary.org/obo/ARO_3007873 PEN-A beta-lactamase Class A beta-lactamase PEN-A21. http://purl.obolibrary.org/obo/ARO_3009000 PEN-A22 http://purl.obolibrary.org/obo/ARO_3007873 PEN-A beta-lactamase Class A beta-lactamase PEN-A22. http://purl.obolibrary.org/obo/ARO_3009001 PEN-A23 http://purl.obolibrary.org/obo/ARO_3007873 PEN-A beta-lactamase Class A beta-lactamase PEN-A23. http://purl.obolibrary.org/obo/ARO_3009002 PEN-A24 http://purl.obolibrary.org/obo/ARO_3007873 PEN-A beta-lactamase Class A beta-lactamase PEN-A24. http://purl.obolibrary.org/obo/ARO_3009003 PEN-A25 http://purl.obolibrary.org/obo/ARO_3007873 PEN-A beta-lactamase Class A beta-lactamase PEN-A25. http://purl.obolibrary.org/obo/ARO_3009004 PEN-A26 http://purl.obolibrary.org/obo/ARO_3007873 PEN-A beta-lactamase Class A beta-lactamase PEN-A26. http://purl.obolibrary.org/obo/ARO_3009005 PEN-A27 http://purl.obolibrary.org/obo/ARO_3007873 PEN-A beta-lactamase Class A beta-lactamase PEN-A27. http://purl.obolibrary.org/obo/ARO_3009006 PEN-A28 http://purl.obolibrary.org/obo/ARO_3007873 PEN-A beta-lactamase Class A beta-lactamase PEN-A28. http://purl.obolibrary.org/obo/ARO_3009007 PEN-A29 http://purl.obolibrary.org/obo/ARO_3007873 PEN-A beta-lactamase Class A beta-lactamase PEN-A29. http://purl.obolibrary.org/obo/ARO_3009008 PEN-A2 http://purl.obolibrary.org/obo/ARO_3007873 PEN-A beta-lactamase Class A beta-lactamase PEN-A2. http://purl.obolibrary.org/obo/ARO_3009009 PEN-A30 http://purl.obolibrary.org/obo/ARO_3007873 PEN-A beta-lactamase Class A beta-lactamase PEN-A30. http://purl.obolibrary.org/obo/ARO_3009010 PEN-A31 http://purl.obolibrary.org/obo/ARO_3007873 PEN-A beta-lactamase Class A beta-lactamase PEN-A31. http://purl.obolibrary.org/obo/ARO_3009011 PEN-A32 http://purl.obolibrary.org/obo/ARO_3007873 PEN-A beta-lactamase Class A beta-lactamase PEN-A32. http://purl.obolibrary.org/obo/ARO_3009012 PEN-A33 http://purl.obolibrary.org/obo/ARO_3007873 PEN-A beta-lactamase Class A beta-lactamase PEN-A33. http://purl.obolibrary.org/obo/ARO_3009013 PEN-A34 http://purl.obolibrary.org/obo/ARO_3007873 PEN-A beta-lactamase Class A beta-lactamase PEN-A34. http://purl.obolibrary.org/obo/ARO_3009014 PEN-A35 http://purl.obolibrary.org/obo/ARO_3007873 PEN-A beta-lactamase Class A beta-lactamase PEN-A35. http://purl.obolibrary.org/obo/ARO_3009015 PEN-A37 http://purl.obolibrary.org/obo/ARO_3007873 PEN-A beta-lactamase Class A beta-lactamase PEN-A37. http://purl.obolibrary.org/obo/ARO_3009016 PEN-A38 http://purl.obolibrary.org/obo/ARO_3007873 PEN-A beta-lactamase Class A beta-lactamase PEN-A38. http://purl.obolibrary.org/obo/ARO_3009017 PEN-A3 http://purl.obolibrary.org/obo/ARO_3007873 PEN-A beta-lactamase Class A beta-lactamase PEN-A3. http://purl.obolibrary.org/obo/ARO_3009018 PEN-A5 http://purl.obolibrary.org/obo/ARO_3007873 PEN-A beta-lactamase Class A beta-lactamase PEN-A5. http://purl.obolibrary.org/obo/ARO_3009019 PEN-A6 http://purl.obolibrary.org/obo/ARO_3007873 PEN-A beta-lactamase Class A beta-lactamase PEN-A6. http://purl.obolibrary.org/obo/ARO_3009020 PEN-A7 http://purl.obolibrary.org/obo/ARO_3007873 PEN-A beta-lactamase Class A beta-lactamase PEN-A7. http://purl.obolibrary.org/obo/ARO_3009021 PEN-A8 http://purl.obolibrary.org/obo/ARO_3007873 PEN-A beta-lactamase Class A beta-lactamase PEN-A8. http://purl.obolibrary.org/obo/ARO_3009022 PEN-A9 http://purl.obolibrary.org/obo/ARO_3007873 PEN-A beta-lactamase Class A beta-lactamase PEN-A9. http://purl.obolibrary.org/obo/ARO_3009023 PEN-B1 http://purl.obolibrary.org/obo/ARO_3007874 PEN-B beta-lactamase Class A beta-lactamase PEN-B1. http://purl.obolibrary.org/obo/ARO_3009024 PEN-B2 http://purl.obolibrary.org/obo/ARO_3007874 PEN-B beta-lactamase Class A beta-lactamase PEN-B2. http://purl.obolibrary.org/obo/ARO_3009025 PEN-B3 http://purl.obolibrary.org/obo/ARO_3007874 PEN-B beta-lactamase Class A beta-lactamase PEN-B3. http://purl.obolibrary.org/obo/ARO_3009026 PEN-B4 http://purl.obolibrary.org/obo/ARO_3007874 PEN-B beta-lactamase Class A beta-lactamase PEN-B4. http://purl.obolibrary.org/obo/ARO_3009027 PER-17 http://purl.obolibrary.org/obo/ARO_3000056 PER beta-lactamase Extended-spectrum class A beta-lactamase PER-17. http://purl.obolibrary.org/obo/ARO_3009028 PER-18 http://purl.obolibrary.org/obo/ARO_3000056 PER beta-lactamase Extended-spectrum class A beta-lactamase PER-18. http://purl.obolibrary.org/obo/ARO_3009029 PJM-2 http://purl.obolibrary.org/obo/ARO_3007373 PJM beta-lactamase Subclass B3 metallo-beta-lactamase PJM-2. http://purl.obolibrary.org/obo/ARO_3009030 PLA-4 http://purl.obolibrary.org/obo/ARO_3005433 PLA beta-lactamase Class A beta-lactamase PLA-4. http://purl.obolibrary.org/obo/ARO_3009031 PLA-5 http://purl.obolibrary.org/obo/ARO_3005433 PLA beta-lactamase Class A beta-lactamase PLA-5. http://purl.obolibrary.org/obo/ARO_3009032 PNC-1 http://purl.obolibrary.org/obo/ARO_3007875 PNC beta-lactamase Class C beta-lactamase PNC-1. http://purl.obolibrary.org/obo/ARO_3009033 PNC-2 http://purl.obolibrary.org/obo/ARO_3007875 PNC beta-lactamase Extended-spectrum class C beta-lactamase PNC-2. http://purl.obolibrary.org/obo/ARO_3009034 PNC-3 http://purl.obolibrary.org/obo/ARO_3007875 PNC beta-lactamase Extended-spectrum class C beta-lactamase PNC-3. http://purl.obolibrary.org/obo/ARO_3009035 RAA-1 http://purl.obolibrary.org/obo/ARO_3007876 RAA beta-lactamase Extended-spectrum beta-lactamase RAA-1. http://purl.obolibrary.org/obo/ARO_3009036 RAHN-3 http://purl.obolibrary.org/obo/ARO_3005439 RAHN beta-lactamase Extended-spectrum class A beta-lactamase RAHN-3. http://purl.obolibrary.org/obo/ARO_3009037 RAHN-4 http://purl.obolibrary.org/obo/ARO_3005439 RAHN beta-lactamase Extended-spectrum class A beta-lactamase RAHN-4. http://purl.obolibrary.org/obo/ARO_3009038 RAHN-5 http://purl.obolibrary.org/obo/ARO_3005439 RAHN beta-lactamase Extended-spectrum class A beta-lactamase RAHN-5. http://purl.obolibrary.org/obo/ARO_3009039 RAHN-6 http://purl.obolibrary.org/obo/ARO_3005439 RAHN beta-lactamase Extended-spectrum class A beta-lactamase RAHN-6. http://purl.obolibrary.org/obo/ARO_3009040 RASA-1 http://purl.obolibrary.org/obo/ARO_3007877 RASA beta-lactamase Extended-spectrum class A beta-lactamase RASA-1. http://purl.obolibrary.org/obo/ARO_3009041 RSC1-1 http://purl.obolibrary.org/obo/ARO_3007878 RSC1 beta-lactamase Class C beta-lactamase RSC1-1. http://purl.obolibrary.org/obo/ARO_3009042 RSD1-1 http://purl.obolibrary.org/obo/ARO_3007879 RSD1 Class D beta-lactamase RSD1-1. http://purl.obolibrary.org/obo/ARO_3009044 SED-2 http://purl.obolibrary.org/obo/ARO_3007880 SED beta-lactamase Class A beta-lactamase SED-2. http://purl.obolibrary.org/obo/ARO_3009045 SFC-2 http://purl.obolibrary.org/obo/ARO_3005443 SFC beta-lactamase Carbapenem-hydrolyzing class A beta-lactamase SFC-2. http://purl.obolibrary.org/obo/ARO_3009046 SFDC-1 http://purl.obolibrary.org/obo/ARO_3007881 SFDC beta-lactamase Extended-spectrum class C beta-lactamase SFDC-1. http://purl.obolibrary.org/obo/ARO_3009048 SHV-229 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase Broad-spectrum class A beta-lactamase SHV-229. http://purl.obolibrary.org/obo/ARO_3009049 SHV-230 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase Extended-spectrum class A beta-lactamase SHV-230. http://purl.obolibrary.org/obo/ARO_3009050 SHV-231 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase Inhibitor-resistant extended-spectrum class A beta-lactamase SHV-231. http://purl.obolibrary.org/obo/ARO_3009051 SHV-232 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase Class A beta-lactamase SHV-232. http://purl.obolibrary.org/obo/ARO_3009052 SHV-233 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase Inhibitor-resistant class A beta-lactamase SHV-233. http://purl.obolibrary.org/obo/ARO_3009053 SHV-234 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase Inhibitor-resistant class A beta-lactamase SHV-234. http://purl.obolibrary.org/obo/ARO_3009054 SHV-235 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase Class A beta-lactamase SHV-235. http://purl.obolibrary.org/obo/ARO_3009055 SHV-236 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase Class A beta-lactamase SHV-236. http://purl.obolibrary.org/obo/ARO_3009056 SHV-237 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase Class A beta-lactamase SHV-237. http://purl.obolibrary.org/obo/ARO_3009057 SHV-238 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase Inhibitor-resistant extended-spectrum class A beta-lactamase SHV-238. http://purl.obolibrary.org/obo/ARO_3009058 SHV-239 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase Inhibitor-resistant class A beta-lactamase SHV-239. http://purl.obolibrary.org/obo/ARO_3009059 SHV-240 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase Inhibitor-resistant class A beta-lactamase SHV-240. http://purl.obolibrary.org/obo/ARO_3009060 SHV-241 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase Inhibitor-resistant class A beta-lactamase SHV-241. http://purl.obolibrary.org/obo/ARO_3009061 SHV-242 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase Inhibitor-resistant class A beta-lactamase SHV-242. http://purl.obolibrary.org/obo/ARO_3009062 SHV-243 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase Class A beta-lactamase SHV-243. http://purl.obolibrary.org/obo/ARO_3009063 SHV-244 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase Class A beta-lactamase SHV-244. http://purl.obolibrary.org/obo/ARO_3009064 SHV-245 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase Class A beta-lactamase SHV-245. http://purl.obolibrary.org/obo/ARO_3009065 SRT-4 http://purl.obolibrary.org/obo/ARO_3000095 SRT beta-lactamase Class C beta-lactamase SRT-4. http://purl.obolibrary.org/obo/ARO_3009066 TEM-239 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase Class A beta-lactamase TEM-239. http://purl.obolibrary.org/obo/ARO_3009067 TEM-248 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase Class A beta-lactamase TEM-248. http://purl.obolibrary.org/obo/ARO_3009068 TEM-249 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase Class A beta-lactamase TEM-249. http://purl.obolibrary.org/obo/ARO_3009069 TEM-250 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase Class A beta-lactamase TEM-250. http://purl.obolibrary.org/obo/ARO_3009070 TEM-251 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase Class A beta-lactamase TEM-251. http://purl.obolibrary.org/obo/ARO_3009071 TEM-252 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase Class A beta-lactamase TEM-252. http://purl.obolibrary.org/obo/ARO_3009072 TEM-253 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase Class A beta-lactamase TEM-253. http://purl.obolibrary.org/obo/ARO_3009073 TEM-254 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase Class A beta-lactamase TEM-254. http://purl.obolibrary.org/obo/ARO_3009074 TEM-255 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase Class A beta-lactamase TEM-255. http://purl.obolibrary.org/obo/ARO_3009075 TEM-256 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase Class A beta-lactamase TEM-256. http://purl.obolibrary.org/obo/ARO_3009076 TEM-257 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase Class A beta-lactamase TEM-257. http://purl.obolibrary.org/obo/ARO_3009077 TEM-258 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase Class A beta-lactamase TEM-258. http://purl.obolibrary.org/obo/ARO_3009078 VEB-16dep http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase Extended-spectrum class A beta-lactamase VEB-16. http://purl.obolibrary.org/obo/ARO_3009079 VEB-18 http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase Extended-spectrum class A beta-lactamase VEB-18. http://purl.obolibrary.org/obo/ARO_3009080 VEB-28 http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase Extended-spectrum class A beta-lactamase VEB-28. http://purl.obolibrary.org/obo/ARO_3009081 VEB-29 http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase Extended-spectrum class A beta-lactamase VEB-29. http://purl.obolibrary.org/obo/ARO_3009082 VEB-30 http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase Extended-spectrum class A beta-lactamase VEB-30. http://purl.obolibrary.org/obo/ARO_3009083 VEB-31 http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase Extended-spectrum class A beta-lactamase VEB-31. http://purl.obolibrary.org/obo/ARO_3009084 VEB-32 http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase Extended-spectrum class A beta-lactamase VEB-32. http://purl.obolibrary.org/obo/ARO_3009085 VEB-33 http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase Extended-spectrum class A beta-lactamase VEB-33. http://purl.obolibrary.org/obo/ARO_3009086 VEB-34 http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase Extended-spectrum class A beta-lactamase VEB-34. http://purl.obolibrary.org/obo/ARO_3009087 VEB-35 http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase Extended-spectrum class A beta-lactamase VEB-35. http://purl.obolibrary.org/obo/ARO_3009088 VEB-36 http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase Extended-spectrum class A beta-lactamase VEB-36. http://purl.obolibrary.org/obo/ARO_3009089 VEB-37 http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase Extended-spectrum class A beta-lactamase VEB-37. http://purl.obolibrary.org/obo/ARO_3009090 VEB-38 http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase Extended-spectrum class A beta-lactamase VEB-38. http://purl.obolibrary.org/obo/ARO_3009091 VEB-39 http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase Extended-spectrum class A beta-lactamase VEB-39. http://purl.obolibrary.org/obo/ARO_3009092 VIM-88 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase Subclass B1 metallo-beta-lactamase VIM-88. http://purl.obolibrary.org/obo/ARO_3009093 VIM-89 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase Subclass B1 metallo-beta-lactamase VIM-89. http://purl.obolibrary.org/obo/ARO_3009094 VIM-90 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase Subclass B1 metallo-beta-lactamase VIM-90. http://purl.obolibrary.org/obo/ARO_3009095 VIM-91 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase Subclass B1 metallo-beta-lactamase VIM-91. http://purl.obolibrary.org/obo/ARO_3009096 YOC-1 http://purl.obolibrary.org/obo/ARO_3007882 YOC beta-lactamase Class C beta-lactamase YOC-1. http://purl.obolibrary.org/obo/ARO_3009098 CfiA28 http://purl.obolibrary.org/obo/ARO_3004200 CfiA beta-lactamase Subclass B1 metallo-beta-lactamase CfiA28. http://purl.obolibrary.org/obo/ARO_3009099 CfiA29 http://purl.obolibrary.org/obo/ARO_3004200 CfiA beta-lactamase Subclass B1 metallo-beta-lactamase CfiA29. http://purl.obolibrary.org/obo/ARO_3009100 CfiA30 http://purl.obolibrary.org/obo/ARO_3004200 CfiA beta-lactamase Subclass B1 metallo-beta-lactamase CfiA30. http://purl.obolibrary.org/obo/ARO_3009101 CfiA31 http://purl.obolibrary.org/obo/ARO_3004200 CfiA beta-lactamase Subclass B1 metallo-beta-lactamase CfiA31. http://purl.obolibrary.org/obo/ARO_3009105 first-generation cephalosporin http://purl.obolibrary.org/obo/ARO_0000032 cephalosporin First-generation cephalosporin antibiotics include those with a relatively narrow spectrum of activity, primarily effective against gram-positive cocci and with minimal coverage against gram-negative bacteria. http://purl.obolibrary.org/obo/ARO_3009106 second-generation cephalosporin http://purl.obolibrary.org/obo/ARO_0000032 cephalosporin Second-generation cephalosporin antibiotics have increased efficacy against gram-negative bacteria compared to first-generation cephalosporins. This subclass also includes cephamycin antibiotics. http://purl.obolibrary.org/obo/ARO_3009107 third-generation cephalosporin http://purl.obolibrary.org/obo/ARO_0000032 cephalosporin Third generation cephalosporin antibiotics have a marked activity against gram-negative bacteria, but diminished activity against gram-positive bacteria. http://purl.obolibrary.org/obo/ARO_3009108 fourth-generation cephalosporin http://purl.obolibrary.org/obo/ARO_0000032 cephalosporin Fourth-generation cephalosporins have activity against gram-positive cocci and a broad array of gram-negative bacteria, including Pseudomonas and many of the Enterobacteriaceae with inducible chromosomal beta-lactamases. http://purl.obolibrary.org/obo/ARO_3009109 other cephalosporins and penems http://purl.obolibrary.org/obo/ARO_0000032 cephalosporin This subfamily includes other penem and cephalosporin antibiotics without defined classification by generation. http://purl.obolibrary.org/obo/ARO_3009110 cefazedone http://purl.obolibrary.org/obo/ARO_3009105 first-generation cephalosporin Cefazedone is a semisynthetic first-generation cephalosporin with antibacterial activity. Cefazedone binds to and inactivates penicillin-binding proteins (PBPs) located on the inner membrane of the bacterial cell wall. http://purl.obolibrary.org/obo/ARO_3009111 cefatrizine http://purl.obolibrary.org/obo/ARO_3009105 first-generation cephalosporin Cefatrizine is a broad-spectrum, semisynthetic, first-generation cephalosporin with antibacterial activity. Cefatrizine binds to and inactivates penicillin-binding proteins located on the inner membrane of the bacterial cell wall causing cell lysis. http://purl.obolibrary.org/obo/ARO_3009112 cefacetrile http://purl.obolibrary.org/obo/ARO_3009105 first-generation cephalosporin Cefacetrile is a broad-spectrum first-generation cephalosporin with antibacterial activity. Cefacetrile binds to and inactivates penicillin-binding proteins located on the inner membrane of the bacterial cell wall causing cell lysis. http://purl.obolibrary.org/obo/ARO_3009113 cefroxadine http://purl.obolibrary.org/obo/ARO_3009105 first-generation cephalosporin Cefroxadine is a semisynthetic first-generation cephalosporin with antibacterial activity. Cefroxadine binds to and inactivates penicillin-binding proteins located on the inner membrane of the bacterial cell wall causing cell lysis. http://purl.obolibrary.org/obo/ARO_3009114 ceftezole http://purl.obolibrary.org/obo/ARO_3009105 first-generation cephalosporin Ceftezole is a first-generation cephalosporin antibiotic with antibacterial activity. Ceftezole binds to and inactivates penicillin-binding proteins located on the inner membrane of the bacterial cell wall causing cell lysis. It is a cephalosporin and a thiadiazole. http://purl.obolibrary.org/obo/ARO_3009115 ceforanide http://purl.obolibrary.org/obo/ARO_3009106 second-generation cephalosporin Ceforanide is a second-generation cephalosporin antibiotic. It is effective against many coliforms, including Escherichia coli, Klebsiella, Enterobacter and Proteus, and most strains of Salmonella, Shigella, Hemophilus, Citrobacter species. http://purl.obolibrary.org/obo/ARO_3009116 cefminox http://purl.obolibrary.org/obo/ARO_3009106 second-generation cephalosporin Cefminox is a second-generation cephalosporin and cephamycin antibiotic. It has broad-spectrum activity, and is especially effective against Gram-negative and anaerobic bacteria. http://purl.obolibrary.org/obo/ARO_3009117 cefbuperazone http://purl.obolibrary.org/obo/ARO_3009106 second-generation cephalosporin Cefbuperazone is a second-generation cephalosporin and cephamycin antibiotic. http://purl.obolibrary.org/obo/ARO_3009118 cefmenoxime http://purl.obolibrary.org/obo/ARO_3009107 third-generation cephalosporin Cefmenoxime is a broad-spectrum and third-generation cephalosporin antibiotic that is typically used in the treatment of female gynecologic and obstetric infections. It is reported to exhibit high activity against a wide variety of gram-positive and gram-negative bacteria. http://purl.obolibrary.org/obo/ARO_3009119 cefodizime http://purl.obolibrary.org/obo/ARO_3009107 third-generation cephalosporin Cefodizime is a third-generation, aminothiazolyl cephalosporin for parenteral use. Cefodizime has broad-spectrum activity and is stable to most beta-lactamases. http://purl.obolibrary.org/obo/ARO_3009120 cefpiramide http://purl.obolibrary.org/obo/ARO_3009107 third-generation cephalosporin Cefpiramide is a third-generation cephalosporin antibiotic. http://purl.obolibrary.org/obo/ARO_3009121 cefteram http://purl.obolibrary.org/obo/ARO_3009107 third-generation cephalosporin Cefteram is a third-generation cephalosporin antibiotic compound. http://purl.obolibrary.org/obo/ARO_3009122 cefozopran http://purl.obolibrary.org/obo/ARO_3009108 fourth-generation cephalosporin Cefozopran is a fourth-generation cephalosporin antibiotic with broad-spectrum activity. http://purl.obolibrary.org/obo/ARO_3009123 penicillin with extended spectrum http://purl.obolibrary.org/obo/ARO_3000008 penicillin beta-lactam Pencillin-like antibiotics with extended spectrum activity gram-negative bacteria, such as ampicillin and similar antibiotic compounds. http://purl.obolibrary.org/obo/ARO_3009124 beta-lactamase sensitive penicillin http://purl.obolibrary.org/obo/ARO_3000008 penicillin beta-lactam Pencillin-like beta-lactam antibiotics with narrow spectrum activity against beta-lactam susceptible bacteria. http://purl.obolibrary.org/obo/ARO_3009125 beta-lactamase resistant penicillin http://purl.obolibrary.org/obo/ARO_3000008 penicillin beta-lactam Penicillin-like antibiotic compounds resistant to penicillinase activity. http://purl.obolibrary.org/obo/ARO_3009126 azidocillin http://purl.obolibrary.org/obo/ARO_3009124 beta-lactamase sensitive penicillin Azidocillin is a narrow-spectrum, semisynthetic penicillin derivative with antibacterial activity. http://purl.obolibrary.org/obo/ARO_3009127 Phenethicillin http://purl.obolibrary.org/obo/ARO_3009124 beta-lactamase sensitive penicillin Phenethicillin is a penicillin in which the substituent at position 6 of the penam ring is a 2-phenoxypropanamido group. It is a penicillin compound with antibacterial activity. http://purl.obolibrary.org/obo/ARO_3009128 penamecillin http://purl.obolibrary.org/obo/ARO_3009124 beta-lactamase sensitive penicillin Penamecillin is a semisynthetic derivative penicillanic acid ester that is the acetoxymethyl ester of benzylpenicillin. It is a prodrug for benzylpenicillin with antibacterial activity. http://purl.obolibrary.org/obo/ARO_3009129 clometocillin http://purl.obolibrary.org/obo/ARO_3009124 beta-lactamase sensitive penicillin Clometocillin is a penicillin that is benzylpenicillin in which the phenylacetyl group has been replaced by a (3,4-dichlorophenyl)(methoxy)acetyl group. It is a semisynthetic penicillin derivative with antibacterial activity. http://purl.obolibrary.org/obo/ARO_3009130 pivampicillin http://purl.obolibrary.org/obo/ARO_3009123 penicillin with extended spectrum Pivampicillin is a semisynthetic, orally active pivalate ester of ampicillin with antibacterial activity. http://purl.obolibrary.org/obo/ARO_3009131 epicillin http://purl.obolibrary.org/obo/ARO_3009123 penicillin with extended spectrum Epicillin is an extended-spectrum, semisynthetic aminopenicillin with antibacterial activity. http://purl.obolibrary.org/obo/ARO_3009132 hetacillin http://purl.obolibrary.org/obo/ARO_3009123 penicillin with extended spectrum Hetacillin is a semi-synthetic penicillin compound with bactericidal properties. Hetacillin is a prodrug that is converted to ampicillin via esterases. http://purl.obolibrary.org/obo/ARO_3009133 aspoxicillin http://purl.obolibrary.org/obo/ARO_3009123 penicillin with extended spectrum Aspoxicillin is a broad-spectrum, semisynthetic penicillin derivative with antibacterial activity. http://purl.obolibrary.org/obo/ARO_3009135 Antibiotic Resistance Platform (ARP) http://purl.obolibrary.org/obo/ARO_3000045 component of AMR genotypic or phenotypic terminology The Antibiotic Resistance Platform (ARP) is a cell-based array of mechanistically distinct individual resistance elements in an identical genetic background. The ARP consists of resistance elements to 18 classes of antibiotics. There are over 100 antibiotic resistance genes currently in the ARP. https://www.thewrightlab.com/antibiotic-resistance-platform. http://purl.obolibrary.org/obo/ARO_3009136 Minimal Antibiotic Resistance Platform (mARP) http://purl.obolibrary.org/obo/ARO_3000045 component of AMR genotypic or phenotypic terminology The Minimal Antibiotic Resistance Platform (mARP) is a tool that can be used for the general dereplication of antibiotics in natural product extracts. This platform consists of fifteen low-copy number plasmids that constitutively express individual resistance genes that target seventeen of the most commonly found antibiotics. This kit is useful for antibiotic dereplication and adjuvant discovery. https://www.thewrightlab.com/antibiotic-resistance-platform. http://purl.obolibrary.org/obo/ARO_3009137 Biocurator http://purl.obolibrary.org/obo/ARO_3000045 component of AMR genotypic or phenotypic terminology A biocurator is a scientist who extracts, interprets, synthesizes and archives data from a variety of sources, including literature, genomes, online materials and author provided biological data, to standardize this data and make it machine readable, more discoverable and accessible to the public. Reproduced from the International Society for Biocuration: https://www.biocuration.org/community/biocuration-generic-job-description/. http://purl.obolibrary.org/obo/ARO_3009139 Mycobacterium tuberculosis mutation catalog http://purl.obolibrary.org/obo/ARO_3000045 component of AMR genotypic or phenotypic terminology Resistance in Mycobacterium tuberculosis is almost exclusively SNVs. Unlike other organisms, culture and antibiotic susceptibility testing for TB is very challenging. The TB community instead developed a likelihood framework, based on statistical association of SNVs with observed phenotypic resistance across a large number of sequenced genomes, organized as mutation catalogs. It is important to note that each catalog may recycle data from earlier catalogs. http://purl.obolibrary.org/obo/ARO_3009140 ReSeqTB http://purl.obolibrary.org/obo/ARO_3009139 Mycobacterium tuberculosis mutation catalog The Relational Sequencing Tuberculosis Data platform (ReSeqTB) is a Mycobacterium tuberculosis AMR mutation catalog published in 2018. Mutation data acquired from the ReSeqTB catalog are evaluated as conferring resistance (Minimal, Moderate, High), not conferring resistance (None), or Indeterminate. http://purl.obolibrary.org/obo/ARO_3009141 CRyPTIC http://purl.obolibrary.org/obo/ARO_3009139 Mycobacterium tuberculosis mutation catalog The Comprehensive Resistance Prediction for Tuberculosis: an International Consortium (CRyPTIC) is a Mycobacterium tuberculosis AMR mutation catalog published in 2022. Mutation data acquired from the CRyPTIC catalog are evaluated as resistant (R), susceptible (S), or undetermined (U). http://purl.obolibrary.org/obo/ARO_3009142 WHO TB mutation catalog, Second Edition http://purl.obolibrary.org/obo/ARO_3009139 Mycobacterium tuberculosis mutation catalog The World Health Organization (WHO) Mutation Catalog, Second Edition is a Mycobacterium tuberculosis AMR mutation catalog published in 2023. https://www.who.int/publications/i/item/9789240082410. Mutation data acquired from the WHO 2023 catalog are evaluated as resistant (R), susceptible (S), or undetermined (U). http://purl.obolibrary.org/obo/ARO_3004357 catV http://purl.obolibrary.org/obo/ARO_3000122 chloramphenicol acetyltransferase (CAT) A chloramphenicol acetyltransferase identified in Brevibacillus brevis and shown to confer resistance to chloramphenicol antibiotics. Described by Pawlowski et al. 2017. http://purl.obolibrary.org/obo/ARO_3004358 ACI beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase A family of class A beta-lactamase enzymes described in the gram-negative cocci Acidaminococcus fermentans. http://purl.obolibrary.org/obo/ARO_3004359 ACI-1 http://purl.obolibrary.org/obo/ARO_3004358 ACI beta-lactamase A class A beta-lactamase described in Acidaminococcus fermentans. ACI-1 was the first description of a beta-lactamase enzyme in a gram-negative anaerobic cocci. Described by Galan et al 2000. http://purl.obolibrary.org/obo/ARO_3004360 antimicrobial resistance testing reference standard http://purl.obolibrary.org/obo/ARO_3000045 component of AMR genotypic or phenotypic terminology Uses breakpoints to create standards for interpreting the clinical outcome of an MIC value for a particular microbial species and antimicrobial agent. http://purl.obolibrary.org/obo/ARO_3004361 sul4 http://purl.obolibrary.org/obo/ARO_3004238 sulfonamide resistant sul sul4 is a dihydropteroate synthase gene and mobile sulfonamide resistance gene shown to confer resistance when expressed in E. coli. http://purl.obolibrary.org/obo/ARO_3004362 OXA-535 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase A chromosome-carried OXA-48-like beta-lactamase, OXA-535, identified in Shewanella spp. JAB-1. Likely the progenitor to the plasmid-carried OXA-436. Expression of OXA-535 in E. coli demonstrated carbapenem-hydrolyzing activity. Described by Jousset et al. 2017. http://purl.obolibrary.org/obo/ARO_3004363 lipid A acyltransferase http://purl.obolibrary.org/obo/ARO_3007429 gene(s) or protein(s) associated with polymyxin resistance operon Lipid A acyltransferase genes confer resistance to certain types of peptide antibiotics such as polymyxins through the aminoacylation of lipopolysaccharide, thereby decreasing the negative charge of the outer membrane surface. http://purl.obolibrary.org/obo/ARO_3004364 almG http://purl.obolibrary.org/obo/ARO_3004363 lipid A acyltransferase A member of the AlmEFG operon, responsible for polymyxin resistance in Vibrio cholerae. AlmG is a glycyltransferase closely related to lipid A acyltransferases. Described by Henderson JC et al. 2017. http://purl.obolibrary.org/obo/ARO_3004365 British Society for Antimicrobial Chemotherapy (BSAC) http://purl.obolibrary.org/obo/ARO_3004360 antimicrobial resistance testing reference standard BSAC is a British inter-professional organisation involved in antibiotic education, research and leadership. Baquero F. found that the BSAC system recommends lower breakpoints than the consensus standard of all systems for antimicrobial susceptibility testing used in Europe (BSAC, DIN, SFM, SIR, NCCLS and WRG). http://purl.obolibrary.org/obo/ARO_3004366 Clinical and Laboratory Standards Institute (CLSI) http://purl.obolibrary.org/obo/ARO_3004360 antimicrobial resistance testing reference standard The Clinical and Laboratory Standards Institute develops and implements clinical laboratory testing standards. http://purl.obolibrary.org/obo/ARO_3004367 Deutsches Institut für Normung (DIN) http://purl.obolibrary.org/obo/ARO_3004360 antimicrobial resistance testing reference standard DIN is recognized by the Federal Government of Germany as the competent standards organization for Germany and as the national standards body representing Germany in non-governmental international standards organizations. Baquero F. found that the DIN system recommends lower breakpoints than the consensus standard of all systems for antimicrobial susceptibility testing used in Europe (BSAC, DIN, SFM, SIR, NCCLS and WRG). http://purl.obolibrary.org/obo/ARO_3004368 European Committee on Antimicrobial Susceptibility Testing (EUCAST) http://purl.obolibrary.org/obo/ARO_3004360 antimicrobial resistance testing reference standard EUCAST is a standing committee jointly organized by ESCMID, ECDC and European national breakpoint committees; it deals with breakpoints and technical aspects of phenotypic in-vitro antimicrobial susceptibility testing. http://purl.obolibrary.org/obo/ARO_3004369 Société Française de Microbiologie (SFM) http://purl.obolibrary.org/obo/ARO_3004360 antimicrobial resistance testing reference standard The French Society of Microbiology (SFM) is a non-profit association which aims to bring together microbiologists from French-speaking countries, working in the domains of bacteria, viruses, Fungi and parasites, and related medical, industrial and environmental microbiology, physiology, genetics, taxonomy, hygiene, and antimicrobial agents. Baquero F. found that the SFM system recommends higher breakpoints than the consensus standard of all systems for antimicrobial susceptibility testing used in Europe (BSAC, DIN, SFM, SIR, NCCLS and WRG). http://purl.obolibrary.org/obo/ARO_3004370 minimum inhibitory concentration (MIC) http://purl.obolibrary.org/obo/ARO_3000045 component of AMR genotypic or phenotypic terminology Minimum inhibitory concentration (MIC), in microbiology, is the lowest concentration of an antimicrobial that will inhibit the visible growth of a microorganism after overnight incubation. http://purl.obolibrary.org/obo/ARO_3004371 MIC value http://purl.obolibrary.org/obo/ARO_3004439 component of AMR phenotype measurement The measured or quantified MIC. http://purl.obolibrary.org/obo/ARO_3004372 MIC unit http://purl.obolibrary.org/obo/ARO_3004439 component of AMR phenotype measurement Unit for measurement of minimum inhibitory concentration (MIC). http://purl.obolibrary.org/obo/ARO_3004374 malacidin A http://purl.obolibrary.org/obo/ARO_3000035 lipopeptide antibiotic A calcium-dependent cyclic lipopeptide found to be effective against multidrug-resistant Staphylococcus aureus in cutaneous wound infections. http://purl.obolibrary.org/obo/ARO_3004375 malacidin biosynthesis http://purl.obolibrary.org/obo/ARO_3000082 antibiotic biosynthesis Biosynthesis of malacidin A and malacidin B calcium-dependent cyclic lipopeptide antibiotics from uncultured soil bacteria. http://purl.obolibrary.org/obo/ARO_3004376 bicyclomycin biosynthesis http://purl.obolibrary.org/obo/ARO_3000082 antibiotic biosynthesis Biosynthesis of the broad-spectrum Rho transcription factor inhibitor bicyclomycin by hydroxylation of a tRNA-dependent cyclodipeptide synthase core. http://purl.obolibrary.org/obo/ARO_3004378 QepA3 http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump A plasmid-mediate quinolone efflux pump described in Klebsiella aerogenes and Escherichia coli. QepA3 confers resistance to fluoroquinolone antibiotics by expelling the antibiotic molecules from the cell. This is distinct from the usual chromosomal mutation mechanism of quinolone resistance. Described by Wang et al. 2017. http://purl.obolibrary.org/obo/ARO_3004379 QepA4 http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump A plasmid-mediated quinolone efflux pump variant described in Escherichia coli. QepA4 confers resistance to quinolone and fluoroquinolone antibiotics by expulsion from the cell. Described by Manageiro et al. 2017. http://purl.obolibrary.org/obo/ARO_3004380 vaborbactam http://purl.obolibrary.org/obo/ARO_3007131 boronic acid beta-lactamase inhibitor Antibiotic adjuvant and serine beta-lactamase inhibitor, often paired with meropenem for clinical use. http://purl.obolibrary.org/obo/ARO_3004387 in-vivo microbial susceptibility test http://purl.obolibrary.org/obo/NCIT_85540 microbial susceptibility test An experimental test conducted inside of a living organism, none of which currently exist for antimicrobial resistance testing. http://purl.obolibrary.org/obo/ARO_3004388 in-vitro microbial susceptibility test http://purl.obolibrary.org/obo/NCIT_85540 microbial susceptibility test An experimental test conducted outside of a living organism, usually in a tube or plate. http://purl.obolibrary.org/obo/ARO_3004389 reagent or protocol used for testing AMR http://purl.obolibrary.org/obo/ARO_3000045 component of AMR genotypic or phenotypic terminology Reagents and procedures used during microbial susceptibility testing. http://purl.obolibrary.org/obo/ARO_3004390 antimicrobial resistance test platform http://purl.obolibrary.org/obo/NCIT_85540 microbial susceptibility test System of analysis for determining antimicrobial susceptibility. http://purl.obolibrary.org/obo/ARO_3004391 diffusion method http://purl.obolibrary.org/obo/ARO_3004388 in-vitro microbial susceptibility test Microbial species are inoculated in a growth medium onto which antimicrobial agents are transferred by diffusion. http://purl.obolibrary.org/obo/ARO_3004392 thin-layer chromatography (TLC)-bioautography http://purl.obolibrary.org/obo/ARO_3004388 in-vitro microbial susceptibility test Components of complex mixtures such as plant extracts are separated across a TLC plate and tested for anti-microbial activity. http://purl.obolibrary.org/obo/ARO_3004393 time-kill test http://purl.obolibrary.org/obo/ARO_3004388 in-vitro microbial susceptibility test Allows for time-dependent or concentration-dependent analysis of antimicrobial effects. Several tubes of broth culture medium containing a suspension of the test microbe are treated with varying concentrations of the antimicrobial agent and the percentage of dead cells determined at various time points. http://purl.obolibrary.org/obo/ARO_3004394 ATP bioluminescence assay http://purl.obolibrary.org/obo/ARO_3004388 in-vitro microbial susceptibility test Relies on the indirect measurement of microbe populations by quantifying microbial ATP production. http://purl.obolibrary.org/obo/ARO_3004395 flow cytofluorometric method http://purl.obolibrary.org/obo/ARO_3004388 in-vitro microbial susceptibility test Microbes exposed to antimicrobial agents are then stained with the intercalating agent propidium iodide. Damaged cells emit a positive signal that is detected by flow cytometry analysis. Flow cytometry can also be used to discriminate between dead, damaged and live cells. http://purl.obolibrary.org/obo/ARO_3004396 mechanism-specific test http://purl.obolibrary.org/obo/ARO_3004388 in-vitro microbial susceptibility test Test that directly detect the presence of a particular resistance mechanism. http://purl.obolibrary.org/obo/ARO_3004397 broth dilution method http://purl.obolibrary.org/obo/ARO_3004388 in-vitro microbial susceptibility test The microbial species are inoculated in liquid growth medium containing incremental dilutions (usually 2-fold) of the antimicrobial agent. http://purl.obolibrary.org/obo/ARO_3004398 automated testing platform http://purl.obolibrary.org/obo/ARO_3004390 antimicrobial resistance test platform Automated system of analysis for determining antimicrobial susceptibility. http://purl.obolibrary.org/obo/ARO_3004399 manual testing platform http://purl.obolibrary.org/obo/ARO_3004390 antimicrobial resistance test platform Non-automated system of analysis for determining antimicrobial susceptibility. http://purl.obolibrary.org/obo/ARO_3004400 MicroScan http://purl.obolibrary.org/obo/ARO_3004398 automated testing platform Specific automated system of analysis for determining antimicrobial susceptibility developed by Omron. http://purl.obolibrary.org/obo/ARO_3004401 Phoenix http://purl.obolibrary.org/obo/ARO_3004398 automated testing platform Specific automated system of analysis for determining antimicrobial susceptibility developed by Becton Dickinson. http://purl.obolibrary.org/obo/ARO_3004402 Sensitire http://purl.obolibrary.org/obo/ARO_3004398 automated testing platform Specific automated system of analysis for determining antimicrobial susceptibility developed by Trek, Thermo Fisher Scientific. http://purl.obolibrary.org/obo/ARO_3004403 Vitek System http://purl.obolibrary.org/obo/ARO_3004398 automated testing platform Specific automated system of analysis for determining antimicrobial susceptibility developed by bioMérieux. http://purl.obolibrary.org/obo/ARO_3004404 automated testing platform vendor http://purl.obolibrary.org/obo/ARO_3004438 AMR testing vendor Vendor of automated system of analysis for determining antimicrobial susceptibility. http://purl.obolibrary.org/obo/ARO_3004405 Becton Dickinson http://purl.obolibrary.org/obo/ARO_3004404 automated testing platform vendor Specific vendor of automated system of analysis for determining antimicrobial susceptibility headquartered in New Jersey, USA. Becton Dickinson is the developer of the Phoenix automated testing platform. http://purl.obolibrary.org/obo/ARO_3004406 bioMérieux http://purl.obolibrary.org/obo/ARO_3004404 automated testing platform vendor Specific vendor of automated system of analysis for determining antimicrobial susceptibility headquartered in France. bioMérieux is the developer of the Vitek automated testing platform. http://purl.obolibrary.org/obo/ARO_3004407 Siemens http://purl.obolibrary.org/obo/ARO_3004404 automated testing platform vendor Specific vendor of automated system of analysis for determining antimicrobial susceptibility headquartered in Berlin and Munich. http://purl.obolibrary.org/obo/ARO_3004408 Omron http://purl.obolibrary.org/obo/ARO_3004404 automated testing platform vendor Specific vendor of automated system of analysis for determining antimicrobial susceptibility based in Japan. Omron is the developer of the MicroScan automated testing platform. http://purl.obolibrary.org/obo/ARO_3004409 Trek http://purl.obolibrary.org/obo/ARO_3004404 automated testing platform vendor Specific vendor of automated system of analysis for determining antimicrobial susceptibility that was acquired by Thermo Fisher Scientific Inc. Thermo Fisher Scienfiic Inc. is headquartered in Massachusetts, USA. Trek is the developer of the Sensitire automated testing platform. http://purl.obolibrary.org/obo/ARO_3004410 micro broth dilution method http://purl.obolibrary.org/obo/ARO_3004397 broth dilution method Broth dilution conducted on 96-well microtiter plates (≤200 µL per well). http://purl.obolibrary.org/obo/ARO_3004411 agar well diffusion method http://purl.obolibrary.org/obo/ARO_3004391 diffusion method This test is a common method of evaluating the antimicrobial activity of plants or microbial extracts. In this method, bacteria are inoculated onto agar plates and the antimicrobial agent is injected into the plate and allowed to diffuse. http://purl.obolibrary.org/obo/ARO_3004412 agar plug diffusion method http://purl.obolibrary.org/obo/ARO_3004391 diffusion method This method is commonly used to study the antagonism between microorganisms. The first bacterial strain is inoculated onto agar plates in tight streaks. The bacteria will secrete molecules that diffuse in the agar medium; this medium is cut and placed on another agar plate inoculated with another microorganism. http://purl.obolibrary.org/obo/ARO_3004413 cross streak method http://purl.obolibrary.org/obo/ARO_3004391 diffusion method This method is commonly used to study the antagonism between microorganisms. The microbial strain of interest is seeded by a single streak in the center of the agar plate. After incubation, the plate is seeded with the second microorganism by single streak perpendicular to the central streak. http://purl.obolibrary.org/obo/ARO_3004414 agar diffusion bioautography http://purl.obolibrary.org/obo/ARO_3004392 thin-layer chromatography (TLC)-bioautography The antimicrobial agent is transferred from a chromatogram to an agar plate previously inoculated with the test microorganism. http://purl.obolibrary.org/obo/ARO_3004415 direct bioautography http://purl.obolibrary.org/obo/ARO_3004392 thin-layer chromatography (TLC)-bioautography A developed TLC plate is dipped into or sprayed with a microbial suspension and then incubated. Live microbial cells are visualized using tetrazolium salts. http://purl.obolibrary.org/obo/ARO_3004416 agar overlay bioautography http://purl.obolibrary.org/obo/ARO_3004392 thin-layer chromatography (TLC)-bioautography The TLC plate is covered with a molten agar medium seeded with the test microbe and the antimicrobial compounds are allowed to diffuse onto the agar medium. Tetrazolium dye staining allows for visualization. http://purl.obolibrary.org/obo/ARO_3004417 inoculum http://purl.obolibrary.org/obo/ARO_3004389 reagent or protocol used for testing AMR Concentration at which bacterial cells in suspension, calculated with respect to final volume (colony forming units/milliliter (cfu/mL)). The standard for broth dilution is 5 x 105cfu/mL. The standard for agar dilution is 104cfu/mL. http://purl.obolibrary.org/obo/ARO_3004418 growth medium http://purl.obolibrary.org/obo/ARO_3004389 reagent or protocol used for testing AMR Medium that supports microorganism growth. http://purl.obolibrary.org/obo/ARO_3004419 chromogenic cephalosporinase test http://purl.obolibrary.org/obo/ARO_3004396 mechanism-specific test Assay for beta lactamase detection. http://purl.obolibrary.org/obo/ARO_3004420 chloramphenicol acetyltransferase assay (CAT) http://purl.obolibrary.org/obo/ARO_3004396 mechanism-specific test Commercial colorimetric assay for detection of chloramphenicol modifying enzyme chloramphenicol acetyltransferase. http://purl.obolibrary.org/obo/ARO_3004421 greater than standard inoculum http://purl.obolibrary.org/obo/ARO_3004417 inoculum Greater than 5 x 105 cfu/mL for broth dilution and 104 cfu/mL for agar dilution. http://purl.obolibrary.org/obo/ARO_3004422 less than standard inoculum http://purl.obolibrary.org/obo/ARO_3004417 inoculum Less than 5 x 105 cfu/mL for broth dilution and 104 cfu/mL for agar dilution. http://purl.obolibrary.org/obo/ARO_3004423 = standard inoculum http://purl.obolibrary.org/obo/ARO_3004417 inoculum Around equal to 5 x 105 cfu/mL for broth dilution and 104 cfu/mL for agar dilution. http://purl.obolibrary.org/obo/ARO_3004424 Mueller-Hinton Broth http://purl.obolibrary.org/obo/ARO_3004418 growth medium General purpose medium used for culture of nonfastidious microorganisms. http://purl.obolibrary.org/obo/ARO_3004425 CO2 supplemented medium http://purl.obolibrary.org/obo/ARO_3004418 growth medium Incubation atmosphere supplemented with CO2. http://purl.obolibrary.org/obo/ARO_3004426 divalent cation supplemented medium http://purl.obolibrary.org/obo/ARO_3004418 growth medium Medium supplementation with 20–25 mg Ca2+ and 10–12.5 mg Mg2+ per liter, which is representative of the divalent cation concentration in blood. Divalent cation supplemented medium is correct to use for susceptibility testing of tetracyclines, daptomycin for gram-positive bacteria and aminoglycosides for Pseudomonas aeruginosarequires. http://purl.obolibrary.org/obo/ARO_3004427 NaCl supplemented medium http://purl.obolibrary.org/obo/ARO_3004418 growth medium Growth medium supplemented with 2% (wt/vol) sodium chloride for testing susceptibility of Staphylococcus aureus to methicillin, oxacillin and nafcillin. http://purl.obolibrary.org/obo/ARO_3004428 Difco Mueller-Hinton Broth http://purl.obolibrary.org/obo/ARO_3004424 Mueller-Hinton Broth Low thymine and thymidine content. http://purl.obolibrary.org/obo/ARO_3004429 BBL Mueller-Hinton Broth http://purl.obolibrary.org/obo/ARO_3004424 Mueller-Hinton Broth High thymine and thymidine content. http://purl.obolibrary.org/obo/ARO_3004430 antimicrobial resistance tissue specificity http://purl.obolibrary.org/obo/ARO_3000045 component of AMR genotypic or phenotypic terminology The tissue type used to select breakpoints from a particular standard, for the interpretation of MIC results. http://purl.obolibrary.org/obo/ARO_3004431 EUCAST antimicrobial phenotype http://purl.obolibrary.org/obo/ARO_3004299 antimicrobial phenotype Qualitative description of a microbial response to antimicrobial agents as described by EUCAST using breakpoints determined through in-vitro testing. These breakpoints are determined irrespective of tissue specificity of infection. http://purl.obolibrary.org/obo/ARO_3004432 wild-type http://purl.obolibrary.org/obo/ARO_3004431 EUCAST antimicrobial phenotype A microbe whose susceptibility to antibiotics is comparable to that of a reference susceptible microbe, meaning that the microbe is sensitive to the particular antibiotic. http://purl.obolibrary.org/obo/ARO_3004433 non wild-type http://purl.obolibrary.org/obo/ARO_3004431 EUCAST antimicrobial phenotype A microbe whose susceptibility to antibiotics differs from that of a reference susceptible microbe, meaning that the microbe is resistant to the particular antibiotic. http://purl.obolibrary.org/obo/ARO_3004438 AMR testing vendor http://purl.obolibrary.org/obo/ARO_3000045 component of AMR genotypic or phenotypic terminology Vendor of AMR testing equipment and reagents. http://purl.obolibrary.org/obo/ARO_3004439 component of AMR phenotype measurement http://purl.obolibrary.org/obo/ARO_3000045 component of AMR genotypic or phenotypic terminology Details required in reporting antimicrobial resistance. http://purl.obolibrary.org/obo/ARO_3004440 CLSI antimicrobial phenotype http://purl.obolibrary.org/obo/ARO_3004299 antimicrobial phenotype Qualitative description of a microbial response to antimicrobial agents as described by CLSI using breakpoints that take into consideration tissue specificity of infection. http://purl.obolibrary.org/obo/ARO_3004441 tet(59) http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump Tet(59) is a chromosome-encoded tetracycline efflux pump described from a Chinese pig manure sample. http://purl.obolibrary.org/obo/ARO_3004442 tet(W/N/W) http://purl.obolibrary.org/obo/ARO_0000002 tetracycline-resistant ribosomal protection protein tet(W/N/W) is a mosaic tetracycline resistance gene and ribosomal protection protein. http://purl.obolibrary.org/obo/ARO_3004443 RSA beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase A family of class A beta-lactamase enzymes, RSA beta-lactamases show carbapenemase and cephalosporinase activity. http://purl.obolibrary.org/obo/ARO_3004444 RSA1-1 http://purl.obolibrary.org/obo/ARO_3004443 RSA beta-lactamase RSA1-1 is a class A beta-lactamase resistance enzyme identified from a functional metagenomic study of contaminated river sediments. http://purl.obolibrary.org/obo/ARO_3004446 Haemophilus influenzae PBP3 conferring resistance to beta-lactam antibiotics http://purl.obolibrary.org/obo/ARO_3003938 Penicillin-binding protein mutations conferring resistance to beta-lactam antibiotics PBP3 is a penicillin-binding protein and beta-lactam resistance enzyme encoded by the ftsI gene in Haemophilus influenzae. Mutations in ftsI confer resistance to beta-lactam antibiotics. http://purl.obolibrary.org/obo/ARO_3004449 TRU beta-lactamase http://purl.obolibrary.org/obo/ARO_3000076 class C beta-lactamase A class C beta-lactamase endogenous to Aeromonas enteropelogenes (tructi). http://purl.obolibrary.org/obo/ARO_3004450 TRU-1 http://purl.obolibrary.org/obo/ARO_3004449 TRU beta-lactamase A class C beta-lactamase enzyme identified from Aeromonas enteropelogenes. TRU-1 confers resistance to penicillin and cephalosporin antibiotics. http://purl.obolibrary.org/obo/NCIT_85540 microbial susceptibility test http://purl.obolibrary.org/obo/ARO_3000045 component of AMR genotypic or phenotypic terminology A method to determine whether microbial growth is affected by an antimicrobial compound. http://purl.obolibrary.org/obo/ARO_3004833 Neisseria gonorrhoeae PBP1 conferring resistance to beta-lactam antibiotics http://purl.obolibrary.org/obo/ARO_3003938 Penicillin-binding protein mutations conferring resistance to beta-lactam antibiotics Point mutation in Neisseria gonorrhoea PBP1 (ponA) decreases affinity between beta-lactam antibiotic molecule and PBP1, thereby conferring resistance to beta-lactam antibiotics. http://purl.obolibrary.org/obo/ARO_3004835 Neisseria gonorrhoeae pilQ gene conferring resistance to beta-lactam http://purl.obolibrary.org/obo/ARO_3003938 Penicillin-binding protein mutations conferring resistance to beta-lactam antibiotics PilQ is an important gonococcal outer membrane component, member of secretin protein family, and involved in Type IV pilus formation. http://purl.obolibrary.org/obo/ARO_3004836 Neisseria gonorrhoeae 23S rRNA with mutation conferring resistance to azithromycin http://purl.obolibrary.org/obo/ARO_3004125 23S rRNA with mutation conferring resistance to macrolide antibiotics Point mutation in the 23S rRNA of Neisseria gonorrhoea shown to confer resistance to azithromycin, a macrolide type antibiotic. http://purl.obolibrary.org/obo/ARO_2000000 confers_resistance_to_antibiotic A relationship ontology term in which the subject (usually an enzyme, protein or other gene product) confers or contributes to clinically relevant resistance to a specific antibiotic drug. An entity is resistant to a chemical compound if and only if x is a pathogen and y is an antibiotic, and the fitness of that pathogen is not decreased when exposed to that antibiotic. http://purl.obolibrary.org/obo/ARO_3009157 Grammar for Antimicrobial Resistance Catalogues (GARC) http://purl.obolibrary.org/obo/ARO_3000045 component of AMR genotypic or phenotypic terminology A proposed grammar to describe genetic changes that is readable by both human and code (https://fowlerlab.org/2018/11/25/goarc-a-general-ontology-for-antimicrobial-resistance-catalogues). http://purl.obolibrary.org/obo/ARO_3009170 myxothiazole http://purl.obolibrary.org/obo/ARO_3009165 antifungal without defined classification This chemical compound is produced by the myxobacterium Myxococcus fulvus. It is an inhibitor of the mitochondrial cytochrome bc1 complex (coenzyme Q - cytochrome c reductase). It is a competitive inhibitor of ubiquinol, and binds at the quinol oxidation (Qo) site of the bc1 complex, blocking electron transfer to the Rieske iron-sulfur protein. http://purl.obolibrary.org/obo/ARO_3009143 Curated-R http://purl.obolibrary.org/obo/ARO_3000045 component of AMR genotypic or phenotypic terminology Mutation data hand curated from the scientific literature, evaluated as conferring resistance (R). http://purl.obolibrary.org/obo/ARO_0000000 macrolide antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule Macrolides are a group of drugs (typically antibiotics) that have a large macrocyclic lactone ring of 12-16 carbons to which one or more deoxy sugars, usually cladinose and desosamine, may be attached. Macrolides bind to the 50S-subunit of bacterial ribosomes, inhibiting the synthesis of vital proteins. http://purl.obolibrary.org/obo/ARO_0000001 fluoroquinolone antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule The fluoroquinolones are a family of synthetic broad-spectrum antibiotics that are 4-quinolone-3-carboxylates. These compounds interact with topoisomerase II (DNA gyrase) to disrupt bacterial DNA replication, damage DNA, and cause cell death. http://purl.obolibrary.org/obo/ARO_0000002 tetracycline-resistant ribosomal protection protein http://purl.obolibrary.org/obo/ARO_3000185 antibiotic target protection protein A family of proteins known to bind to the 30S ribosomal subunit. This interaction prevents tetracycline and tetracycline derivatives from inhibiting ribosomal function. Thus, these proteins confer elevated resistance to tetracycline derivatives as a ribosomal protection protein. http://purl.obolibrary.org/obo/ARO_0000003 astromicin http://purl.obolibrary.org/obo/ARO_0000016 aminoglycoside antibiotic Astromicin is an aminoglycoside antibiotic used to treat different types of bacterial infections. Astromicin works by binding to the bacterial 30S ribosomal subunit, causing misreading of mRNA and leaving the bacterium unable to synthesize proteins vital to its growth. http://purl.obolibrary.org/obo/ARO_0000004 monobactam http://purl.obolibrary.org/obo/ARO_3000007 beta-lactam antibiotic Monobactams are a class of beta-lactam antibiotics with a broad spectrum of antibacterial activity, and have a structure which renders them highly resistant to beta-lactamases. Unlike penams and cephems, monobactams do not have any ring fused to its four-member lactam structure. Monobactam antibiotics are bactericidal, and act by inhibiting the synthesis of the peptidoglycan layer of bacterial cell walls. The peptidoglycan layer is important for cell wall structural integrity, especially in Gram-positive organisms. http://purl.obolibrary.org/obo/ARO_0000005 neomycin http://purl.obolibrary.org/obo/ARO_0000016 aminoglycoside antibiotic Neomycin is an aminoglycoside antibiotic used to treat different types of bacterial infections. Neomycin works by binding to the bacterial 30S ribosomal subunit, causing misreading of mRNA and leaving the bacterium unable to synthesize proteins vital to its growth. http://purl.obolibrary.org/obo/ARO_0000006 erythromycin http://purl.obolibrary.org/obo/ARO_0000000 macrolide antibiotic Erythromycin is a macrolide antibiotic with a 14-carbon ring that has an antimicrobial spectrum similar to or slightly wider than that of penicillin, and is often used for people that have an allergy to penicillins. Erythromycin may possess bacteriocidal activity, particularly at higher concentrations by binding to the 50S subunit of the bacterial 70S rRNA complex, inhibiting peptidyl-tRNA translocation. Thus, protein synthesis and subsequently structure/function processes critical for life or replication are inhibited. http://purl.obolibrary.org/obo/ARO_0000007 dibekacin http://purl.obolibrary.org/obo/ARO_0000016 aminoglycoside antibiotic Dibekacin is an aminoglycoside antibiotic used to treat different types of bacterial infections. Dibekacin works by binding to the bacterial 30S ribosomal subunit, causing misreading of mRNA and leaving the bacterium unable to synthesize proteins vital to its growth. http://purl.obolibrary.org/obo/ARO_0000008 cefoxitin http://purl.obolibrary.org/obo/ARO_3009106 second-generation cephalosporin Cefoxitin is a cephamycin antibiotic often grouped with the second generation cephalosporins. Cefoxitin is bactericidal and acts by inhibiting the synthesis of the peptidoglycan layer of bacterial cell walls. The peptidoglycan layer is important for cell wall structural integrity, especially in Gram-positive organisms. Cefoxitin's 7-alpha-methoxy group and 3' leaving group make it a poor substrate for most beta-lactamases. http://purl.obolibrary.org/obo/ARO_0000009 tunicamycin http://purl.obolibrary.org/obo/ARO_3000707 antibiotic mixture Tunicamycin is mixture of homologous nucleoside antibiotics that block the reaction of UDP-N-acetylglucosamine and dolichyl phosphate in the first step of glycoprotein synthesis. http://purl.obolibrary.org/obo/ARO_0000010 antibiotic resistance gene cluster, cassette, or operon http://purl.obolibrary.org/obo/ARO_3000000 determinant of antibiotic resistance Clusters of antibiotic resistance genes. May be regulated by a shared promoter or repressor. http://purl.obolibrary.org/obo/ARO_0000011 cloxacillin http://purl.obolibrary.org/obo/ARO_3009125 beta-lactamase resistant penicillin Cloxacillin is a semisynthetic, isoxazolyl penicillin derivative in the beta-lactam class of antibiotics. It interferes with peptidogylcan synthesis and is commonly used for treating penicillin-resistant Staphylococcus aureus infections. http://purl.obolibrary.org/obo/ARO_0000012 streptothricin http://purl.obolibrary.org/obo/ARO_3000034 nucleoside antibiotic Streptothricins are a group of N-glycoside antibiotics that include a carbamoylated D-glucosamine to which are attached a series of L-beta-lysine residues at position 2 and a streptolidine at position 1. Streptothricins vary by the number of beta-lysine residues (from 1 (nourseothricin) to 7) and target protein synthesis in bacteria and eukaryotes. http://purl.obolibrary.org/obo/ARO_0000013 amikacin http://purl.obolibrary.org/obo/ARO_0000016 aminoglycoside antibiotic Amikacin is an aminoglycoside antibiotic that works by binding to the bacterial 30S ribosomal subunit, causing misreading of mRNA and leaving the bacterium unable to synthesize proteins vital to its growth. http://purl.obolibrary.org/obo/ARO_0000014 gentamicin C http://purl.obolibrary.org/obo/ARO_3007382 gentamicin Gentamicin C is a mixture of gentamicin C1, gentamicin C1a, and gentamicin C2 (these differ in substituents at position C6'). Gentamicin works by binding to the bacterial 30S ribosomal subunit, causing misreading of mRNA and leaving the bacterium unable to synthesize proteins vital to its growth. http://purl.obolibrary.org/obo/ARO_0000015 methicillin http://purl.obolibrary.org/obo/ARO_3009125 beta-lactamase resistant penicillin Derived from penicillin to combat penicillin-resistance, methicillin is insensitive to beta-lactamases (also known as penicillinases) secreted by many penicillin-resistant bacteria. Methicillin is bactericidal, and acts by inhibiting the synthesis of the peptidoglycan layer of bacterial cell walls. The peptidoglycan layer is important for cell wall structural integrity, especially in Gram-positive organisms. http://purl.obolibrary.org/obo/ARO_0000016 aminoglycoside antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule Aminoglycosides are a group of antibiotics that are mostly effective against Gram-negative bacteria. These molecules consist of aminated sugars attached to a dibasic cyclitol. Aminoglycosides work by binding to the bacterial 30S ribosomal subunit (some work by binding to the 50S subunit), inhibiting the translocation of the peptidyl-tRNA from the A-site to the P-site and also causing misreading of mRNA, leaving the bacterium unable to synthesize proteins vital to its growth. http://purl.obolibrary.org/obo/ARO_0000017 lincosamide antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule Lincosamides (e.g. lincomycin, clindamycin) are a class of drugs which bind to the 23s portion of the 50S subunit of bacterial ribosomes. This interaction inhibits early elongation of peptide chains by inhibiting the transpeptidase reaction, acting similarly to macrolides. http://purl.obolibrary.org/obo/ARO_0000018 viomycin http://purl.obolibrary.org/obo/ARO_3000053 peptide antibiotic Viomycin sulfate (Viocin) is an polypeptide antibiotic used in the treatment of tuberculosis. It is produced by the actinomycete Streptomyces puniceus and binds to the bacterial ribosome, inhibiting prokaryotic protein synthesis and certain forms of RNA splicing. http://purl.obolibrary.org/obo/ARO_0000020 carbapenem http://purl.obolibrary.org/obo/ARO_3000007 beta-lactam antibiotic Carbapenems are a class of beta-lactam antibiotics with a broad spectrum of antibacterial activity, and have a structure which renders them highly resistant to beta-lactamases. Carbapenem antibiotics are bactericidal, and act by inhibiting the synthesis of the peptidoglycan layer of bacterial cell walls. The peptidoglycan layer is important for cell wall structural integrity, especially in Gram-positive organisms. http://purl.obolibrary.org/obo/ARO_0000021 ribostamycin http://purl.obolibrary.org/obo/ARO_0000016 aminoglycoside antibiotic Ribostamycin is an aminoglycoside antibiotic used to treat different types of bacterial infections. Ribostamycin works by binding to the bacterial 30S ribosomal subunit, causing misreading of mRNA and leaving the bacterium unable to synthesize proteins vital to its growth. http://purl.obolibrary.org/obo/ARO_0000022 polymyxin antibiotic http://purl.obolibrary.org/obo/ARO_3000035 lipopeptide antibiotic Polymyxins are cationic detergent antibiotics, with a general structure of a cyclic peptide with a long hydrophobic tail. They disrupt the structure of the bacterial cell membrane by interacting with its phospholipids. Polymyxins have a bactericidal effect on Gram-negative bacilli, especially on Pseudomonas and coliform organisms. http://purl.obolibrary.org/obo/ARO_0000023 enoxacin http://purl.obolibrary.org/obo/ARO_0000001 fluoroquinolone antibiotic Enoxacin belongs to a group called fluoroquinolones. Its mode of action depends upon blocking bacterial DNA replication by binding itself to DNA gyrase and causing double-stranded breaks in the bacterial chromosome. http://purl.obolibrary.org/obo/ARO_0000024 butirosin http://purl.obolibrary.org/obo/ARO_0000016 aminoglycoside antibiotic Butirosin is an aminoglycoside antibiotic used to treat different types of bacterial infections. Butirosin works by binding to the bacterial 30S ribosomal subunit, causing misreading of mRNA and leaving the bacterium unable to synthesize proteins vital to its growth. http://purl.obolibrary.org/obo/ARO_0000025 fosfomycin http://purl.obolibrary.org/obo/ARO_3007149 phosphonic acid antibiotic Fosfomycin (also known as phosphomycin and phosphonomycin) is a broad-spectrum antibiotic produced by certain Streptomyces species. It is effective on gram positive and negative bacteria as it targets the cell wall, an essential feature shared by both bacteria. Its specific target is MurA (MurZ in E.coli), which attaches phosphoenolpyruvate (PEP) to UDP-N-acetylglucosamine, a step of commitment to cell wall synthesis. In the active site of MurA, the active cysteine molecule is alkylated which stops the catalytic reaction. http://purl.obolibrary.org/obo/ARO_0000026 streptogramin antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule Streptogramin antibiotics are natural products produced by various members of the Streptomyces genus. These antibiotics bind to the P site of the 50S subunit of bacterial ribosomes to inhibit protein synthesis. The family consists of two subgroups, type A and type B, which are simultaneously produced by the same bacterial species in a ratio of roughly 70:30. http://purl.obolibrary.org/obo/ARO_0000027 roxithromycin http://purl.obolibrary.org/obo/ARO_0000000 macrolide antibiotic Roxithromycin is a semi-synthetic, 14-carbon ring macrolide antibiotic derived from erythromycin. It is used to treat respiratory tract, urinary and soft tissue infections. Roxithromycin may possess bacteriocidal activity, particularly at higher concentrations by binding to the 50S subunit of the bacterial 70S rRNA complex, protein synthesis and subsequently structure/function processes critical for life or replication are inhibited. http://purl.obolibrary.org/obo/ARO_0000028 vancomycin http://purl.obolibrary.org/obo/ARO_3000081 glycopeptide antibiotic Vancomycin is a glycopeptide antibiotic used in the prophylaxis and treatment of infections caused by Gram-positive bacteria. Vancomycin inhibits the synthesis of peptidoglycan, the major component of the cell wall of gram-positive bacteria. Its mechanism of action is unusual in that it acts by binding precursors of peptidoglycan, rather than by interacting with an enzyme. http://purl.obolibrary.org/obo/ARO_0000029 teicoplanin http://purl.obolibrary.org/obo/ARO_3000081 glycopeptide antibiotic Teicoplanin is a glycopeptide antibiotic used in the prophylaxis and treatment of serious infections caused by Gram-positive bacteria. Teicoplanin has a unique acyl-aliphatic chain, and binds to cell wall precursors to inhibit transglycosylation and transpeptidation. http://purl.obolibrary.org/obo/ARO_0000030 tigecycline http://purl.obolibrary.org/obo/ARO_0000042 glycylcycline Tigecycline is an glycylcycline antibiotic. It works by inhibiting action of the prokaryotic 30S ribosome. http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant http://purl.obolibrary.org/obo/ARO_3000000 determinant of antibiotic resistance Resistance to antibiotics is often conferred by single nucleotide polymorphisms (SNPs) and other mutations in target genes. http://purl.obolibrary.org/obo/ARO_0000032 cephalosporin http://purl.obolibrary.org/obo/ARO_3000007 beta-lactam antibiotic Cephalosporins are a class of beta-lactam antibiotics, containing the beta-lactam ring fused with a dihydrothiazolidine ring. Together with cephamycins they belong to a sub-group called cephems. Cephalosporin are bactericidal, and act by inhibiting the synthesis of the peptidoglycan layer of bacterial cell walls. The peptidoglycan layer is important for cell wall structural integrity, especially in Gram-positive organisms. http://purl.obolibrary.org/obo/ARO_0000034 streptogramin A antibiotic http://purl.obolibrary.org/obo/ARO_0000026 streptogramin antibiotic Streptogramin A antibiotics are cyclic polyketide peptide hybrids that bind to the ribosomal peptidyl transfer centre. Structural variation arises from substituting a proline for its desaturated derivative and by its substitution for Ala or Cys. Used alone, streptogramin A antibiotics are bacteriostatic, but is bactericidal when used with streptogramin B antibiotics. http://purl.obolibrary.org/obo/ARO_0000035 sisomicin http://purl.obolibrary.org/obo/ARO_0000016 aminoglycoside antibiotic Sisomicin is an aminoglycoside antibiotic used to treat different types of bacterial infections. Sisomicin works by binding to the bacterial 30S ribosomal subunit, causing misreading of mRNA and leaving the bacterium unable to synthesize proteins vital to its growth. http://purl.obolibrary.org/obo/ARO_0000036 ciprofloxacin http://purl.obolibrary.org/obo/ARO_0000001 fluoroquinolone antibiotic Ciprofloxacin is a bacteriocidal fluoroquinolone. It blocks bacterial DNA replication by binding to the toposiomerase II or IV-DNA complex (or cleavable complex), thereby causing double-stranded breaks in the bacterial chromosome. http://purl.obolibrary.org/obo/ARO_0000037 apramycin http://purl.obolibrary.org/obo/ARO_0000016 aminoglycoside antibiotic Apramycin is an aminoglycoside antibiotic used to treat different types of bacterial infections in animals. Apramycin works by binding to the bacterial 30S ribosomal subunit, causing misreading of mRNA and leaving the bacterium unable to synthesize proteins vital to its growth. http://purl.obolibrary.org/obo/ARO_0000038 netilmicin http://purl.obolibrary.org/obo/ARO_0000016 aminoglycoside antibiotic Netilmicin is a member of the aminoglycoside family of antibiotics. These antibiotics have the ability to kill a wide variety of bacteria by binding to the bacterial 30S ribosomal subunit, causing misreading of mRNA and leaving the bacterium unable to synthesize proteins vital to its growth. Netilmicin is not absorbed from the gut and is therefore only given by injection or infusion. It is only used in the treatment of serious infections particularly those resistant to gentamicin. http://purl.obolibrary.org/obo/ARO_0000039 spectinomycin http://purl.obolibrary.org/obo/ARO_0000016 aminoglycoside antibiotic Spectinomycin is an aminoglycoside antibiotic used to treat different types of bacterial infections. Spectinomycin works by binding to the bacterial 30S ribosomal subunit inhibiting translation. http://purl.obolibrary.org/obo/ARO_0000040 streptomycin http://purl.obolibrary.org/obo/ARO_0000016 aminoglycoside antibiotic Streptomycin is an aminoglycoside antibiotic used to treat different types of bacterial infections. Streptomycin works by binding to the bacterial 30S ribosomal subunit, causing misreading of mRNA and leaving the bacterium unable to synthesize proteins vital to its growth. http://purl.obolibrary.org/obo/ARO_0000041 bacitracin http://purl.obolibrary.org/obo/ARO_3000707 antibiotic mixture Bacitracin is a mixture of related cyclic polypeptides produced by organisms of the licheniformis group of Bacillus subtilis var Tracy. Bacitracin interferes with the dephosphorylation of the C55-isoprenyl pyrophosphate, a molecule which carries the building blocks of the peptidoglycan bacterial cell wall outside of the inner membrane. http://purl.obolibrary.org/obo/ARO_0000042 glycylcycline http://purl.obolibrary.org/obo/ARO_3000050 tetracycline antibiotic Glycylcyclines are a new class of antibiotics derived from tetracycline. These tetracycline analogues are specifically designed to overcome two common mechanisms of tetracycline resistance. Presently, there is only one glycylcycline antibiotic for clinical use: tigecycline. It works by inhibiting action of the prokaryotic 30S ribosome, preventing the binding of aminoacyl-tRNA. http://purl.obolibrary.org/obo/ARO_0000043 carbenicillin http://purl.obolibrary.org/obo/ARO_3009123 penicillin with extended spectrum Carbenicillin is a semi-synthetic antibiotic belonging to the carboxypenicillin subgroup of the penicillins. It has gram-negative coverage which includes Pseudomonas aeruginosa but limited gram-positive coverage. The carboxypenicillins are susceptible to degradation by beta-lactamase enzymes. Carbenicillin antibiotics are bactericidal, and act by inhibiting the synthesis of the peptidoglycan layer of bacterial cell walls. The peptidoglycan layer is important for cell wall structural integrity, especially in Gram-positive organisms. http://purl.obolibrary.org/obo/ARO_0000045 acriflavine http://purl.obolibrary.org/obo/ARO_3005386 disinfecting agents and antiseptics Acriflavine is a topical antiseptic. It has the form of an orange or brown powder. It may be harmful in the eyes or if inhaled. Acriflavine is also used as treatment for external fungal infections of aquarium fish. http://purl.obolibrary.org/obo/ARO_0000046 lincomycin http://purl.obolibrary.org/obo/ARO_0000017 lincosamide antibiotic Lincomycin is a lincosamide antibiotic that comes from the actinomyces Streptomyces lincolnensis. It binds to the 23s portion of the 50S subunit of bacterial ribosomes and inhibit early elongation of peptide chain by inhibiting transpeptidase reaction. http://purl.obolibrary.org/obo/ARO_0000047 puromycin http://purl.obolibrary.org/obo/ARO_3000080 aminonucleoside antibiotic Puromycin is an aminonucleoside antibiotic, derived from Streptomyces alboniger, that causes premature chain termination during ribosomal protein translation. http://purl.obolibrary.org/obo/ARO_0000049 kanamycin A http://purl.obolibrary.org/obo/ARO_0000016 aminoglycoside antibiotic Kanamycin is an aminoglycoside antibiotic used to treat different types of bacterial infections. Kanamycin works by binding to the bacterial 30S ribosomal subunit, causing misreading of mRNA and leaving the bacterium unable to synthesize proteins vital to its growth. http://purl.obolibrary.org/obo/ARO_0000050 streptogramin B antibiotic http://purl.obolibrary.org/obo/ARO_0000026 streptogramin antibiotic Streptogramin B antibiotics are are cyclic hepta- or hexa-depsipeptides. Type B streptogramins block the peptide exit tunnel of the 50S bacterial ribosome. The general composition of group B streptogramins is 3-hydroxypicolinic acid-L-Thr-D-aminobutyric acid (or D-Ala)-L-Pro-L-Phe (or 4-N-,N-(dimethylamino)-L-Phe)-X-L-phenylglycine. Used alone, streptogramin B antibiotics are bacteriostatic, but is bactericidal when used with streptogramin A antibiotics. http://purl.obolibrary.org/obo/ARO_0000051 tetracycline http://purl.obolibrary.org/obo/ARO_3000050 tetracycline antibiotic Tetracycline is a broad-spectrum polyketide antibiotic produced by many Streptomyces. It works by inhibiting action of the prokaryotic 30S ribosome. http://purl.obolibrary.org/obo/ARO_0000052 tobramycin http://purl.obolibrary.org/obo/ARO_0000016 aminoglycoside antibiotic Tobramycin is an aminoglycoside antibiotic used to treat different types of bacterial infections. Tobramycin works by binding to the bacterial 30S ribosomal subunit, causing misreading of mRNA and leaving the bacterium unable to synthesize proteins vital to its growth. http://purl.obolibrary.org/obo/ARO_0000053 bleomycin http://purl.obolibrary.org/obo/ARO_3000707 antibiotic mixture Bleomycin is a family of glycopeptide antibiotics produced by the bacterium Streptomyces verticillus. Bleomycins, taken as a mixture, act by the induction of DNA and RNA strand breaks. In addition to its antibacterial activity, bleomycin is also used as an anticancer agent. http://purl.obolibrary.org/obo/ARO_0000055 bicyclomycin http://purl.obolibrary.org/obo/ARO_3007150 bicyclomycin-like antibiotic Bicyclomycin represents a unique class of antibiotics, discovered in 1972. It is obtained by the fermentation of Streptomyces sapporonensis. In the crystalline form bicyclomycin is observed to be rhombic or monoclinic, depending on the solvent used. This antibiotic kills bacteria by inhibiting the Rho transcription terminator factor, halting ribonucleic acid (RNA) synthesis. http://purl.obolibrary.org/obo/ARO_0000056 oxacillin http://purl.obolibrary.org/obo/ARO_3009125 beta-lactamase resistant penicillin Oxacillin is a penicillinase-resistant beta-lactam. It is similar to methicillin, and has replaced methicillin in clinical use. Oxacillin, especially in combination with other antibiotics, is effective against many penicillinase-producing strains of Staphylococcus aureus and Staphylococcus epidermidis. http://purl.obolibrary.org/obo/ARO_0000057 telithromycin http://purl.obolibrary.org/obo/ARO_0000000 macrolide antibiotic Telithromycin is a semi-synthetic derivative of erythromycin. It is a 14-membered macrolide and is the first ketolide antibiotic to be used in clinics. Telithromycin binds the 50S subunit of the bacterial ribosome to inhibit protein synthesis. http://purl.obolibrary.org/obo/ARO_0000058 cefazolin http://purl.obolibrary.org/obo/ARO_3009105 first-generation cephalosporin Cefazolin, also known as cefazoline or cephazolin, is a first generation cephalosporin antibiotic. It is administered parenterally, and is active against a broad spectrum of bacteria. http://purl.obolibrary.org/obo/ARO_0000059 cefepime http://purl.obolibrary.org/obo/ARO_3009108 fourth-generation cephalosporin Cefepime (INN) is a fourth-generation cephalosporin antibiotic developed in 1994. It contains an aminothiazolyl group that decreases its affinity with beta-lactamases. Cefepime shows high binding affinity with penicillin-binding proteins and has an extended spectrum of activity against Gram-positive and Gram-negative bacteria, with greater activity against both Gram-negative and Gram-positive organisms than third-generation agents. http://purl.obolibrary.org/obo/ARO_0000060 ceftazidime http://purl.obolibrary.org/obo/ARO_3009107 third-generation cephalosporin Ceftazidime is a third-generation cephalosporin antibiotic. Like other third-generation cephalosporins, it has broad spectrum activity against Gram-positive and Gram-negative bacteria. Unlike most third-generation agents, it is active against Pseudomonas aeruginosa, however it has weaker activity against Gram-positive microorganisms and is not used for such infections. http://purl.obolibrary.org/obo/ARO_0000061 ceftobiprole http://purl.obolibrary.org/obo/ARO_3009109 other cephalosporins and penems Ceftobiprole (Zeftera/Zevtera) is a next generation (5th generation) cephalosporin antibiotic with activity against methicillin-resistant Staphylococcus aureus, penicillin-resistant Streptococcus pneumoniae, Pseudomonas aeruginosa, and Enterococci. Ceftobiprole inhibits transpeptidases essential to building cell walls, and is a poor substrate for most beta-lactamases. http://purl.obolibrary.org/obo/ARO_0000062 ceftriaxone http://purl.obolibrary.org/obo/ARO_3009107 third-generation cephalosporin Ceftriaxone is a third-generation cephalosporin antibiotic. The presence of an aminothiazolyl sidechain increases ceftriazone's resistance to beta-lactamases. Like other third-generation cephalosporins, it has broad spectrum activity against Gram-positive and Gram-negative bacteria. http://purl.obolibrary.org/obo/ARO_0000063 cefuroxime http://purl.obolibrary.org/obo/ARO_3009106 second-generation cephalosporin Cefuroxime is a second-generation cephalosporin antibiotic with increased stability with beta-lactamases than first-generation cephalosporins. Cefuroxime is active against Gram-positive organisms but less active against methicillin-resistant strains. http://purl.obolibrary.org/obo/ARO_0000064 amoxicillin http://purl.obolibrary.org/obo/ARO_3009123 penicillin with extended spectrum Amoxicillin is a moderate-spectrum, bacteriolytic, beta-lactam antibiotic used to treat bacterial infections caused by susceptible microorganisms. A derivative of penicillin, it has a wider range of treatment but remains relatively ineffective against Gram-negative bacteria. It is commonly taken with clavulanic acid, a beta-lactamase inhibitor. Like other beta-lactams, amoxicillin interferes with the synthesis of peptidoglycan. http://purl.obolibrary.org/obo/ARO_0000065 clarithromycin http://purl.obolibrary.org/obo/ARO_0000000 macrolide antibiotic Clarithromycin is a methyl derivative of erythromycin, sharing the 14-carbon macrolide ring. The antibiotic binds to the 50S subunit of the ribosome and is used to treat pharyngitis, tonsillitis, acute maxillary sinusitis, acute bacterial exacerbation of chronic bronchitis, pneumonia (especially atypical pneumonias associated with Chlamydia pneumoniae or TWAR), and skin structure infections. http://purl.obolibrary.org/obo/ARO_0000066 clindamycin http://purl.obolibrary.org/obo/ARO_0000017 lincosamide antibiotic Clindamycin is a lincosamide antibiotic that blocks A-site aminoacyl-tRNA binding. It is usually used to treat infections with anaerobic bacteria but can also be used to treat some protozoal diseases, such as malaria. http://purl.obolibrary.org/obo/ARO_0000067 colistin http://purl.obolibrary.org/obo/ARO_0000022 polymyxin antibiotic Colistins are polymyxin antibiotics produced by certain strains of Bacillus polymyxa var. colistinus. Colistin, also referred to as polymyxin E, is a mixture of cyclic polypeptides colistin A and B which disrupt the bacterial cell membrane and is effective against Gram-negative bacteria. http://purl.obolibrary.org/obo/ARO_0000068 daptomycin http://purl.obolibrary.org/obo/ARO_3000035 lipopeptide antibiotic Daptomycin is a novel lipopeptide antibiotic used in the treatment of certain infections caused by Gram-positive organisms. Daptomycin interferes with the bacterial cell membrane, reducing membrane potential and inhibiting cell wall synthesis. http://purl.obolibrary.org/obo/ARO_0000069 doxycycline http://purl.obolibrary.org/obo/ARO_3000050 tetracycline antibiotic Doxycycline is second generation semi-synthetic derivative of the tetracycline group of antibiotics. It inhibits bacterial protein synthesis by binding to the 30S subunit of the bacterial ribosome and preventing the aminotransferase-tRNA from associating with the ribosome. http://purl.obolibrary.org/obo/ARO_0000070 ertapenem http://purl.obolibrary.org/obo/ARO_0000020 carbapenem Ertapenem is a carbapenem antibiotic and is highly resistant to beta-lactamases like other carbapenems. It inhibits bacterial cell wall synthesis. http://purl.obolibrary.org/obo/ARO_0000071 levofloxacin http://purl.obolibrary.org/obo/ARO_0000001 fluoroquinolone antibiotic Levofloxacin is a synthetic chemotherapeutic antibiotic of the fluoroquinolone drug class. Its main target is topoisomerase IV, inhibiting its function and disrupting DNA replication. http://purl.obolibrary.org/obo/ARO_0000072 linezolid http://purl.obolibrary.org/obo/ARO_3000079 oxazolidinone antibiotic Linezolid is a synthetic antibiotic used for the treatment of serious infections caused by Gram-positive bacteria that are resistant to several other antibiotics. It inhibits protein synthesis by binding to domain V of the 23S rRNA of the 50S subunit of bacterial ribosomes. http://purl.obolibrary.org/obo/ARO_0000073 meropenem http://purl.obolibrary.org/obo/ARO_0000020 carbapenem Meropenem is an ultra-broad spectrum injectable antibiotic used to treat a wide variety of infections, including meningitis and pneumonia. It is a beta-lactam and belongs to the subgroup of carbapenem, similar to imipenem and ertapenem. http://purl.obolibrary.org/obo/ARO_0000074 moxifloxacin http://purl.obolibrary.org/obo/ARO_0000001 fluoroquinolone antibiotic Moxifloxacin is a fourth generation synthetic fluoroquinolone chemotherapeutic agent, and has been shown to be significantly more active than levofloxacin (4 to 8 times more) against Streptococcus pneumoniae. It acts by inhibiting bacterial DNA topoisomerases. http://purl.obolibrary.org/obo/ARO_0000075 nitrofurantoin http://purl.obolibrary.org/obo/ARO_3004116 nitrofuran antibiotic Nitrofurantoin is an antibiotic used to treat urinary tract infections. It inhibits enzyme synthesis by inhibiting essential enzymes involved in the citric acid cycle, as well as those involved in DNA, RNA, and protein synthesis. It is marketed under the following brand names: Furadantin, Macrobid, Macrodantin, Nitro Macro and Urantoin. http://purl.obolibrary.org/obo/ARO_0000076 resistance-modifying agents http://purl.obolibrary.org/obo/ARO_1000001 process or component of antibiotic biology or chemistry Resistance-modifying agents (RMA) include antibiotic adjuvants and other inhibitors of antibiotic resistance, as well as antibiotic potentiators. These are non-antibiotic compounds which act to block resistance mechanisms or enhance antibiotic action. These are often delivered in combination with an antibiotic (e.g. amoxicillin-clavulanic acid) and may either affect the host organism or the pathogen. Adjuvants and potentiators are therefore used to rescue the activity of existing antibiotic drugs, and are researched as an alternative solution to the antibiotic resistance crisis. http://purl.obolibrary.org/obo/ARO_0000077 tazobactam http://purl.obolibrary.org/obo/ARO_3007130 beta-lactam derived beta-lactamase inhibitor Tazobactam is a compound which inhibits the action of bacterial beta-lactamases. http://purl.obolibrary.org/obo/ARO_0000078 piperacillin http://purl.obolibrary.org/obo/ARO_3009123 penicillin with extended spectrum Piperacillin is an acetylureidopenicillin and has an extended spectrum of targets relative to other beta-lactam antibiotics. It inhibits cell wall synthesis in bacteria, and is usually taken with the beta-lactamase inhibitor tazobactam to overcome penicillin-resistant bacteria. http://purl.obolibrary.org/obo/ARO_0000079 clavulanic acid http://purl.obolibrary.org/obo/ARO_3007130 beta-lactam derived beta-lactamase inhibitor Clavulanic acid is a beta-lactamase inhibitor (marketed by GlaxoSmithKline, formerly Beecham) combined with penicillin group antibiotics to overcome certain types of antibiotic resistance. It is used to overcome resistance in bacteria that secrete beta-lactamase, which otherwise inactivates most penicillins. http://purl.obolibrary.org/obo/ARO_0001001 antibiotic target alteration http://purl.obolibrary.org/obo/ARO_1000002 mechanism of antibiotic resistance Mutational alteration or enzymatic modification of antibiotic target which results in antibiotic resistance. http://purl.obolibrary.org/obo/ARO_0001002 antibiotic target replacement http://purl.obolibrary.org/obo/ARO_1000002 mechanism of antibiotic resistance Replacement or substitution of antibiotic action target, which process will result in antibiotic resistance. http://purl.obolibrary.org/obo/ARO_0001003 antibiotic target protection http://purl.obolibrary.org/obo/ARO_1000002 mechanism of antibiotic resistance Protection of antibiotic action target from antibiotic binding, which process will result in antibiotic resistance. http://purl.obolibrary.org/obo/ARO_0001004 antibiotic inactivation http://purl.obolibrary.org/obo/ARO_1000002 mechanism of antibiotic resistance Enzymatic inactivation of antibiotic to confer drug resistance. http://purl.obolibrary.org/obo/ARO_0010000 antibiotic efflux http://purl.obolibrary.org/obo/ARO_1000002 mechanism of antibiotic resistance Antibiotic resistance via the transport of antibiotics out of the cell. http://purl.obolibrary.org/obo/ARO_0010001 ATP-binding cassette (ABC) antibiotic efflux pump http://purl.obolibrary.org/obo/ARO_3000159 efflux pump complex or subunit conferring antibiotic resistance Directed pumping of antibiotic out of a cell to confer resistance. ATP-binding cassette (ABC) transporters are present in all cells of all organisms and use the energy of ATP binding/hydrolysis to transport substrates across cell membranes. http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump http://purl.obolibrary.org/obo/ARO_3000159 efflux pump complex or subunit conferring antibiotic resistance Directed pumping of antibiotic out of a cell to confer resistance. Major facilitator superfamily (MFS) transporters and ABC transporters comprise the two largest and most functionally diverse of the transporter superfamilies. However, MFS transporters are distinct from ABC transporters in both their primary sequence and structure and in the mechanism of energy coupling. As secondary transporters they are, like RND and SMR transporters, energized by the electrochemical proton gradient. http://purl.obolibrary.org/obo/ARO_0010003 small multidrug resistance (SMR) antibiotic efflux pump http://purl.obolibrary.org/obo/ARO_3000159 efflux pump complex or subunit conferring antibiotic resistance Directed pumping of antibiotic out of a cell to confer resistance. Small multidrug resistance (SMR) proteins are a relatively small family of transporters, restricted to prokaryotic cells. They are also the smallest multidrug transporters, with only four transmembrane alpha-helices and no significant extramembrane domain. http://purl.obolibrary.org/obo/ARO_0010004 resistance-nodulation-cell division (RND) antibiotic efflux pump http://purl.obolibrary.org/obo/ARO_3000159 efflux pump complex or subunit conferring antibiotic resistance Directed pumping of antibiotic out of a cell to confer resistance. Resistance-nodulation-division (RND) proteins are found in both prokaryotic and eukaryotic cells and have diverse substrate specificities and physiological roles. However, there are relatively few RND transporters and they are secondary transporters, energized not by ATP binding/hydrolysis but by proton movement down the transmembrane electrochemical gradient. http://purl.obolibrary.org/obo/ARO_1000002 mechanism of antibiotic resistance http://purl.obolibrary.org/obo/ARO_1000001 process or component of antibiotic biology or chemistry Antibiotic resistance mechanisms evolve naturally via natural selection through random mutation, but it could also be engineered by applying an evolutionary stress on a population. http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule http://purl.obolibrary.org/obo/ARO_1000001 process or component of antibiotic biology or chemistry Antibiotics are commonly classified based on their mechanism of action, chemical structure or spectrum of activity. http://purl.obolibrary.org/obo/ARO_3000000 determinant of antibiotic resistance http://purl.obolibrary.org/obo/ARO_1000001 process or component of antibiotic biology or chemistry A mutation, single nucleotide polymorphism, gene, or gene product that confers antibiotic resistance. http://purl.obolibrary.org/obo/ARO_3000001 beta-lactamase http://purl.obolibrary.org/obo/ARO_3000557 antibiotic inactivation enzyme Beta-lactamases are enzymes (EC 3.5.2.6) produced by some bacteria and are responsible for their resistance to beta-lactam antibiotics like penicillins, cephalosporins (are relatively resistant to beta-lactamase), cephamycins, and carbapenems (ertapenem). These antibiotics have a common element in their molecular structure: a four-atom ring known as a beta-lactam. The lactamase enzyme breaks that ring open, deactivating the molecule's antibacterial properties. Beta-lactam antibiotics are typically used to treat a broad spectrum of gram-positive and gram-negative bacteria. Beta-lactamases produced by gram-negative organisms are usually secreted. http://purl.obolibrary.org/obo/ARO_3000002 vanW http://purl.obolibrary.org/obo/ARO_3002976 gene(s) or protein(s) associated with a glycopeptide resistance cluster vanW is an accessory gene, with unknown function, found on vancomycin resistance operons. http://purl.obolibrary.org/obo/ARO_3000003 antibiotic without defined classification http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule These compounds are antibiotics of unique structure or origin, without a defined classification. http://purl.obolibrary.org/obo/ARO_3000004 class B (metallo-) beta-lactamase http://purl.obolibrary.org/obo/ARO_3000001 beta-lactamase Ambler Class B beta-lactamases are the metallo-beta-lactamases. These enzymes possess one or two zinc ions in the active site, which are used to orient a hydroxide nucleophile to attack the carbonyl on a beta-lactam ring. There are currently no inhibitors in late-stage development for these relatively new beta-lactamases. http://purl.obolibrary.org/obo/ARO_3000005 vanD http://purl.obolibrary.org/obo/ARO_3002978 D-Ala-D-Lac ligase VanD is a D-Ala-D-Ala ligase homolog similar to VanA, and can synthesize D-Ala-D-Lac, an alternative substrate for peptidoglycan synthesis that reduces vancomycin binding affinity. It is associated with both vancomycin and teicoplanin resistance. http://purl.obolibrary.org/obo/ARO_3000006 vanH http://purl.obolibrary.org/obo/ARO_3002976 gene(s) or protein(s) associated with a glycopeptide resistance cluster VanH is a D-specific alpha-ketoacid dehydrogenase that synthesizes D-lactate. D-lactate is incorporated into the end of the peptidoglycan subunits, decreasing vancomycin binding affinity. http://purl.obolibrary.org/obo/ARO_3000007 beta-lactam antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule Beta-lactam antibiotics are a broad class of antibiotics that include penams (penicillin derivatives), cephems (cephalosporins), monobactams, and carbapenems. These antibiotic agents contain a beta-lactam nucleus in its molecular structure. They are the most widely-used group of antibiotics. http://purl.obolibrary.org/obo/ARO_3000008 penicillin beta-lactam http://purl.obolibrary.org/obo/ARO_3000007 beta-lactam antibiotic Penicilins (Penams) are a group of antibiotics derived from Penicillium fungi that share a skeleton beta-lactam moiety fused with a thiazolidine ring. Penicillin-like antibiotics are historically significant because they are the first drugs that were effective against many previously serious diseases such as syphilis and Staphylococcus infections. Penicillins are still widely used today, though many types of bacteria are now resistant. All penicillins are beta-lactam antibiotics in the penam sub-group, and are used in the treatment of bacterial infections caused by susceptible, usually Gram-positive, organisms. http://purl.obolibrary.org/obo/ARO_3000010 vanA http://purl.obolibrary.org/obo/ARO_3002978 D-Ala-D-Lac ligase VanA is a D-Ala-D-Ala ligase homolog that synthesizes D-Ala-D-Lac, an alternative substrate for peptidoglycan synthesis that reduces vancomycin binding affinity. It has been isolated from VREs. It is associated with both vancomycin and teicoplanin resistance. http://purl.obolibrary.org/obo/ARO_3000011 vanX http://purl.obolibrary.org/obo/ARO_3002976 gene(s) or protein(s) associated with a glycopeptide resistance cluster VanX is a D,D-dipeptidase that cleaves D-Ala-D-Ala but not D-Ala-D-Lac, ensuring that the latter dipeptide that has reduced binding affinity with vancomycin is used to synthesize peptidoglycan substrate. http://purl.obolibrary.org/obo/ARO_3000012 protein(s) conferring antibiotic resistance via molecular bypass http://purl.obolibrary.org/obo/ARO_3000000 determinant of antibiotic resistance Proteins involved in restructuring of the cell wall, causing antibiotic resistance. http://purl.obolibrary.org/obo/ARO_3000013 vanB http://purl.obolibrary.org/obo/ARO_3002978 D-Ala-D-Lac ligase VanB is a D-Ala-D-Ala ligase homolog similar to VanA, and can synthesize D-Ala-D-Lac, an alternative substrate for peptidoglycan synthesis that reduces vancomycin binding affinity. It has been isolated from VREs. It is associated with vancomycin resistance, but not teicoplanin resistance. http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase TEM-1 is the most commonly-encountered beta-lactamase in gram-negative bacteria. Up to 90% of ampicillin resistance in E. coli is due to the production of TEM-1. Also responsible for the ampicillin and penicillin resistance that is seen in H. influenzae and N. gonorrhoeae in increasing numbers. Although TEM-type beta-lactamases are most often found in E. coli and K. pneumoniae, they are also found in other species of gram-negative bacteria with increasing frequency. The amino acid substitutions responsible for the ESBL phenotype cluster around the active site of the enzyme and change its configuration, allowing access to oxyimino-beta-lactam substrates. Opening the active site to beta-lactam substrates also typically enhances the susceptibility of the enzyme to b-lactamase inhibitors, such as clavulanic acid. Although the inhibitor-resistant beta-lactamases are not ESBLs, they are often discussed with ESBLs because they are also derivatives of the classical TEM- or SHV-type enzymes. These enzymes were at first given the designation IRT for inhibitor-resistant TEM beta-lactamase; however, all have subsequently been renamed with numerical TEM designations. There are at least 19 distinct inhibitor-resistant TEM beta-lactamases. Inhibitor-resistant TEM beta-lactamases have been found mainly in clinical isolates of E. coli, but also some strains of K. pneumoniae, Klebsiella oxytoca, P. mirabilis, and Citrobacter freundii. Although the inhibitor-resistant TEM variants are resistant to inhibition by clavulanic acid and sulbactam, thereby showing clinical resistance to the beta-lactam-lactamase inhibitor combinations of amoxicillin-clavulanate (Co-amoxiclav), ticarcillin-clavulanate, and ampicillin/sulbactam, they normally remain susceptible to inhibition by tazobactam and subsequently the combination of piperacillin/tazobactam, although resistance has been described. http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase http://purl.obolibrary.org/obo/ARO_3000096 SHV-LEN beta-lactamase SHV-1 shares 68 percent of its amino acids with TEM-1 and has a similar overall structure. The SHV-1 beta-lactamase is most commonly found in K. pneumoniae and is responsible for up to 20% of the plasmid-mediated ampicillin resistance in this species. ESBLs in this family also have amino acid changes around the active site, most commonly at positions 238 or 238 and 240. More than 60 SHV varieties are known. http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase These enzymes were named for their greater activity against cefotaxime than other oxyimino-beta-lactam substrates (eg, ceftazidime, ceftriaxone, or cefepime). Rather than arising by mutation, they represent examples of plasmid acquisition of beta-lactamase genes normally found on the chromosome of Kluyvera species, a group of rarely pathogenic commensal organisms. These enzymes are not very closely related to TEM or SHV beta-lactamases in that they show only approximately 40% identity with these two commonly isolated beta-lactamases. Despite their name, a few are more active on ceftazidime than cefotaxime. CTX-M-15 was recently found in bacterial strains expressing NDM-1 and were responsible for resistance to aztreonam. http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase http://purl.obolibrary.org/obo/ARO_3000075 class D beta-lactamase OXA beta-lactamases were long recognized as a less common but also plasmid-mediated beta-lactamase variety that could hydrolyze oxacillin and related anti-staphylococcal penicillins. These beta-lactamases differ from the TEM and SHV enzymes in that they belong to molecular class D and functional group 2d. The OXA-type beta-lactamases confer resistance to ampicillin and cephalothin and are characterized by their high hydrolytic activity against oxacillin and cloxacillin and the fact that they are poorly inhibited by clavulanic acid. Amino acid substitutions in OXA enzymes can also give the ESBL phenotype. The OXA beta-lactamase family was originally created as a phenotypic rather than a genotypic group for a few beta-lactamases that had a specific hydrolysis profile. Therefore, there is as little as 20% sequence homology among some of the members of this family. However, recent additions to this family show some degree of homology to one or more of the existing members of the OXA beta-lactamase family. Some confer resistance predominantly to ceftazidime, but OXA-17 confers greater resistance to cefotaxime and cefepime than it does resistance to ceftazidime. http://purl.obolibrary.org/obo/ARO_3000018 IMI beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase IMI beta-lactamases are a group of TEM-1-like beta-lactamase that are known to hydrolyze imipenem. IMI beta-lactamases are inhibited by clavulanic acid and tazobactam. http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase Plasmid mediated IMP-type carbapenemases, of which at least 26 varieties are currently known, became established in Japan in the 1990s in enteric gram-negative organisms, Pseudomonas and Acinetobacter species. Integron-associated, sometimes within plasmids. Hydrolyses all beta-lactams except monobactams, and evades all beta-lactam inhibitors. http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase The Verone integron-encoded metallo-beta-lactamase (VIM) family was reported from Italy in 1999. There are, to date, 23 reported variants. VIM enzymes mostly occur in P. aeruginosa, also P. putida and, very rarely, Enterobacteriaceae. Integron-associated, sometimes within plasmids. Hydrolyses all beta-lactams except monobactams, and evades all beta-lactam inhibitors. There is a strong incidence of these in East Asia. http://purl.obolibrary.org/obo/ARO_3000022 ristocetin http://purl.obolibrary.org/obo/ARO_3000081 glycopeptide antibiotic Ristocetin is a glycopeptide antibiotic similar to vancomycin but positively charged. It is not used clinically because it induces platelet agglutination. http://purl.obolibrary.org/obo/ARO_3000023 aminocoumarin sensitive parE http://purl.obolibrary.org/obo/ARO_3003259 antibiotic sensitive DNA topoisomerase subunit parE Subunit of the topoisomerase IV sensitive to aminocoumarins. http://purl.obolibrary.org/obo/ARO_3000024 patA http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance PatA is an ABC transporter of Streptococcus pneumoniae that interacts with PatB to confer fluoroquinolone resistance. http://purl.obolibrary.org/obo/ARO_3000025 patB http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance PatB is an ABC transporter of Streptococcus pneumoniae that interacts with PatA to confer fluoroquinolone resistance.. http://purl.obolibrary.org/obo/ARO_3000026 mepA http://purl.obolibrary.org/obo/ARO_3000112 multidrug and toxic compound extrusion (MATE) transporter MepA is an efflux protein regulated by MepR and part of the MepRAB cluster. Its presence in Staphylococcus aureus led to multidrug resistance, while it has also been shown to decrease tigecycline susceptibility. http://purl.obolibrary.org/obo/ARO_3000027 emrA http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance EmrA is a membrane fusion protein, providing an efflux pathway with EmrB and TolC between the inner and outer membranes of E. coli, a Gram-negative bacterium. http://purl.obolibrary.org/obo/ARO_3000034 nucleoside antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule Nucleoside antibiotics are made of modified nucleosides and nucleotides with wide-ranging activities and means of antibacterial effects. This drug class includes aminonucleoside antibiotics, which contain an amino group. http://purl.obolibrary.org/obo/ARO_3000035 lipopeptide antibiotic http://purl.obolibrary.org/obo/ARO_3000053 peptide antibiotic Lipopeptide antibiotics are aliphatic, with their hydrophobic components interacting with the bacterial cell membrane. http://purl.obolibrary.org/obo/ARO_3000036 tetracycline inactivation enzyme http://purl.obolibrary.org/obo/ARO_3000557 antibiotic inactivation enzyme Enzymes or other gene products which hydroxylate tetracycline and other tetracycline derivatives. Hydroxylation inactivates tetracycline-like antibiotics, thus conferring resistance to these compounds. http://purl.obolibrary.org/obo/ARO_3000040 hydrolysis of antibiotic conferring resistance http://purl.obolibrary.org/obo/ARO_0001004 antibiotic inactivation Hydrolysis of an antibiotic molecule to confer resistance. http://purl.obolibrary.org/obo/ARO_3000042 beta-lactamase inhibitor http://purl.obolibrary.org/obo/ARO_3007222 inhibitor of antibiotic resistance mechanism Antibiotic adjuvants shown to inhibit the action of a beta-lactamase enzyme or enhance the ability of a beta-lactam antibiotic. These compounds are used along with antibiotics to treat beta-lactam-resistant infectious pathogens. http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase VEB beta-lactamases or Vietnamese extended-spectrum beta-lactamases are class A beta-lactamases that confer high-level resistance to oxyimino cephalosporins and to aztreonam. http://purl.obolibrary.org/obo/ARO_3000050 tetracycline antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule These antibiotics are derived from tetracycline, a polyketide antibiotic that inhibits the 30S subunit of bacterial ribosomes. http://purl.obolibrary.org/obo/ARO_3000053 peptide antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule Peptide antibiotics have a wide range of antibacterial mechanisms, depending on the amino acids that make up the antibiotic, although most act to disrupt the cell membrane in some manner. Subclasses of peptide antibiotics can include additional sidechains of other types, such as lipids in the case of the lipopeptide antibiotics. http://purl.obolibrary.org/obo/ARO_3000055 SME beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase SME beta-lactamases are chromosome-mediated class A beta-lactamases that hydrolyze carbapenems in Serratia marcescens. http://purl.obolibrary.org/obo/ARO_3000056 PER beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase PER beta-lactamases are plasmid-mediated extended spectrum beta-lactamases found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase NDM beta-lactamases or New Delhi metallo-beta-lactamases are class B beta-lactamases that confer resistance to a broad range of antibiotics including carbapenems, cephalosporins and penicillins. http://purl.obolibrary.org/obo/ARO_3000058 MIR beta-lactamase http://purl.obolibrary.org/obo/ARO_3000076 class C beta-lactamase MIR beta-lactamases are plasmid-mediated beta-lactamases that confer resistance to oxyimino- and alpha-methoxy beta-lactams. http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase Klebsiella pneumoniae carbapenem resistant (KPC) beta-lactamases are notorious for their ability to efficiently hydrolyze carbapenems, unlike other Ambler Class A beta-lactamases. There are currently 9 variants reported worldwide. These enzymes were first isolated from Klebsiella pneumoniae strains in 2001 in the United States. Hospital outbreaks have since been reported in Greece and Israel and KPC carrying strains are now endemic to New York facilities. KPC-1 and KPC-2 have been shown to be identical and are now referred to as KPC-2. http://purl.obolibrary.org/obo/ARO_3000060 IND beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase IND beta-lactamases are class B carbapenem-hydrolyzing beta-lactamases. http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase GES beta-lactamases or Guiana extended-spectrum beta-lactamases are related to the other plasmid-located class A beta-lactamases. http://purl.obolibrary.org/obo/ARO_3000067 FOX beta-lactamase http://purl.obolibrary.org/obo/ARO_3000076 class C beta-lactamase FOX beta-lactamases are plasmid-encoded AmpC-type beta-lactamase which conferred resistance to broad-spectrum cephalosporins and cephamycins. http://purl.obolibrary.org/obo/ARO_3000068 DHA beta-lactamase http://purl.obolibrary.org/obo/ARO_3000076 class C beta-lactamase DHA beta-lactamases are plasmid-mediated AmpC β-lactamases that confer resistance to cephamycins and oxyimino-cephalosporins. http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase http://purl.obolibrary.org/obo/ARO_3000087 CMY-MOX beta-lactamase CMY beta-lactamases are plasmid-mediated class C beta-lactamases that encodes for resistance to cephamycins. http://purl.obolibrary.org/obo/ARO_3000071 vanS http://purl.obolibrary.org/obo/ARO_3002905 VanS-VanR two-component regulatory system VanS is similar to histidine protein kinases like EnvZ and acts as a response regulator by activating VanR. VanS is required for high level transcription of other van glycopeptide resistance genes. http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase http://purl.obolibrary.org/obo/ARO_3000076 class C beta-lactamase ACT beta-lactamases, also known as AmpC beta-lactamases, are cephalosporinases that cannot be inhibited by clavulanate. These enzymes are encoded by genes located on the chromosome and can be induced by the presence of beta-lactam antibiotics. However recently, these genes have been found on plasmids and expressed at high constitutive levels in Escherichia coli and Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3000073 ACC beta-lactamase http://purl.obolibrary.org/obo/ARO_3000076 class C beta-lactamase ACC beta-lactamases or Ambler class C beta-lactamases are AmpC beta-lactamases. They possess an interesting resistance phenotype due to their low activity against cephamycins. http://purl.obolibrary.org/obo/ARO_3000074 emrB http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance emrB is a translocase in the emrB -TolC efflux protein in E. coli. It recognizes substrates including carbonyl cyanide m-chlorophenylhydrazone (CCCP), nalidixic acid, and thioloactomycin. http://purl.obolibrary.org/obo/ARO_3000075 class D beta-lactamase http://purl.obolibrary.org/obo/ARO_3000001 beta-lactamase Class D beta-lactamases are one of the subgroups of beta-lactamases that are classified as serine enzymes. http://purl.obolibrary.org/obo/ARO_3000076 class C beta-lactamase http://purl.obolibrary.org/obo/ARO_3000001 beta-lactamase AmpC type beta-lactamases are commonly isolated from extended-spectrum cephalosporin-resistant Gram-negative bacteria. AmpC beta-lactamases (also termed class C or group 1) are typically encoded on the chromosome of many Gram-negative bacteria including Citrobacter, Serratia, Enterobacter species, and P. aeruginosa where its expression is usually inducible; it may also occur on Escherichia coli but is not usually inducible, although it can be hyperexpressed. AmpC type beta-lactamases may also be carried on plasmids. AmpC beta-lactamases, in contrast to ESBLs, hydrolyse broad and extended-spectrum cephalosporins (cephamycins as well as to oxyimino-beta-lactams) but are not inhibited by beta-lactamase inhibitors such as clavulanic acid. http://purl.obolibrary.org/obo/ARO_3000077 vanY http://purl.obolibrary.org/obo/ARO_3002976 gene(s) or protein(s) associated with a glycopeptide resistance cluster VanY is a D,D-carboxypeptidase that cleaves removes the terminal D-Ala from peptidoglycan for the addition of D-Lactate. The D-Ala-D-Lac peptidoglycan subunits have reduced binding affinity with vancomycin compared to D-Ala-D-Ala. http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase http://purl.obolibrary.org/obo/ARO_3000001 beta-lactamase The Class A beta-lactamases are one of the subgroups of beta-lactamases that are classified as serine enzymes. Class A beta-lactamases exhibit a large degree of variability and are known to hydrolyze penicillins. http://purl.obolibrary.org/obo/ARO_3000079 oxazolidinone antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule Oxazolidinones are a class of synthetic antibiotics discovered the the 1980's. They inhibit protein synthesis by binding to domain V of the 23S rRNA of the 50S subunit of bacterial ribosomes. Linezolid is the only member of this class currently in clinical use. http://purl.obolibrary.org/obo/ARO_3000080 aminonucleoside antibiotic http://purl.obolibrary.org/obo/ARO_3000034 nucleoside antibiotic Aminonucleoside antibiotics are nucleoside antibiotics that contain an amino group. This amino group is often acylated, e.g. puromycin. http://purl.obolibrary.org/obo/ARO_3000081 glycopeptide antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule Glycopeptide antibiotics are natural products produced non-ribosomally by Actinomycetales bacteria. With the exception of bleomycins, they act by binding the terminal D-Ala-D-Ala in peptidoglycan precursors of the growing bacterial cell wall and are generally active against Gram-positive bacteria. This inhibits transglycosylation leading to cell death due to osmotic stress. http://purl.obolibrary.org/obo/ARO_3000082 antibiotic biosynthesis http://purl.obolibrary.org/obo/ARO_1000001 process or component of antibiotic biology or chemistry The biological synthesis of antibiotics. http://purl.obolibrary.org/obo/ARO_3000083 MOX beta-lactamase http://purl.obolibrary.org/obo/ARO_3000087 CMY-MOX beta-lactamase MOX beta-lactamases are plasmid-mediated AmpC-type beta-lactamases. http://purl.obolibrary.org/obo/ARO_3000085 CMY-LAT-MOX beta-lactamase http://purl.obolibrary.org/obo/ARO_3000076 class C beta-lactamase A grouping of the related CMY, LAT, and MOX beta-lactamases. http://purl.obolibrary.org/obo/ARO_3000086 CMY-LAT beta-lactamase http://purl.obolibrary.org/obo/ARO_3000085 CMY-LAT-MOX beta-lactamase A grouping of the related CMY and LAT beta-lactamases. http://purl.obolibrary.org/obo/ARO_3000087 CMY-MOX beta-lactamase http://purl.obolibrary.org/obo/ARO_3000085 CMY-LAT-MOX beta-lactamase A grouping of the related CMY and MOX beta-lactamases. http://purl.obolibrary.org/obo/ARO_3000089 AER beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase AER beta-lactamases are capable of hydrolyzing arbenicillin. http://purl.obolibrary.org/obo/ARO_3000090 Bla1 http://purl.obolibrary.org/obo/ARO_3004229 class A Bacillus anthracis Bla beta-lactamase Bla1 is a chromosomal-encoded beta-lactamase, found in Bacillus anthracis, which hydrolyzes penicillins. http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase CARB beta-lactamases are class A lactamases that can hydrolyze carbenicillin. Many of the PSE beta-lactamases have been renamed as CARB-lactamases with the notable exception of PSE-2 which is now OXA-10. http://purl.obolibrary.org/obo/ARO_3000094 OCH beta-lactamase http://purl.obolibrary.org/obo/ARO_3000076 class C beta-lactamase OCH beta-lactamases are Ambler class C chromosomal-encoded beta-lactamases in Brucella anthropi. http://purl.obolibrary.org/obo/ARO_3000095 SRT beta-lactamase http://purl.obolibrary.org/obo/ARO_3000076 class C beta-lactamase SRT beta-lactamases. http://purl.obolibrary.org/obo/ARO_3000096 SHV-LEN beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase A grouping of the related SHV and LEN beta-lactamases. http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase http://purl.obolibrary.org/obo/ARO_3000096 SHV-LEN beta-lactamase LEN beta-lactamases are chromosomal class A beta-lactamases that confer resistance to ampicillin, amoxicillin, carbenicillin, and ticarcillin but not to extended-spectrum beta-lactams. http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase http://purl.obolibrary.org/obo/ARO_3000076 class C beta-lactamase PDC beta-lactamases are class C beta-lactamases that are found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3000100 gene modulating beta-lactam resistance http://purl.obolibrary.org/obo/ARO_3000000 determinant of antibiotic resistance Genes that directly or indirectly modulate beta-lactam resistance. http://purl.obolibrary.org/obo/ARO_3000103 aminocoumarin antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule Aminocoumarin antibiotics bind DNA gyrase subunit B to inhibit ATP-dependent DNA supercoiling. http://purl.obolibrary.org/obo/ARO_3000105 phosphorylation of antibiotic conferring resistance http://purl.obolibrary.org/obo/ARO_0001004 antibiotic inactivation Phosphorylation of antibiotic usually by ATP, sometimes GTP. http://purl.obolibrary.org/obo/ARO_3000106 acylation of antibiotic conferring resistance http://purl.obolibrary.org/obo/ARO_0001004 antibiotic inactivation Addition of an acyl group to an antibiotic, often via acetylation by acetylCoA. http://purl.obolibrary.org/obo/ARO_3000107 nucleotidylation of antibiotic conferring resistance http://purl.obolibrary.org/obo/ARO_0001004 antibiotic inactivation Modification by NMP, usually AMP. http://purl.obolibrary.org/obo/ARO_3000111 novobiocin http://purl.obolibrary.org/obo/ARO_3000103 aminocoumarin antibiotic Novobiocin is an aminocoumarin antibiotic produced by Streptomyces spheroides and Streptomyces niveus, and binds DNA gyrase subunit B inhibiting ATP-dependent DNA supercoiling. http://purl.obolibrary.org/obo/ARO_3000112 multidrug and toxic compound extrusion (MATE) transporter http://purl.obolibrary.org/obo/ARO_3000159 efflux pump complex or subunit conferring antibiotic resistance Directed pumping of antibiotic out of a cell to confer resistance. Multidrug and toxic compound extrusion (MATE) transporters utilize the cationic gradient across the membrane as an energy source. Although there is a diverse substrate specificity, almost all MATE transporters recognize fluoroquinolones. Arciflavine, ethidium and aminoglycosides are also good substrates. http://purl.obolibrary.org/obo/ARO_3000113 vga-type ABC-F protein http://purl.obolibrary.org/obo/ARO_3004469 ABC-F ATP-binding cassette ribosomal protection protein Vga-type plasmid-borne ABC-F proteins, expressed in staphylococci that confer resistance to streptogramin A antibiotics through ribosomal protection. http://purl.obolibrary.org/obo/ARO_3000114 aminoglycoside phosphotransferase (APH) http://purl.obolibrary.org/obo/ARO_3007380 aminoglycoside modifying enzyme Kinases that modify aminoglycoside antibiotics by phosphorylation using NTPs as cofactor. http://purl.obolibrary.org/obo/ARO_3000115 antibiotic resistant DNA topoisomerase subunit parE http://purl.obolibrary.org/obo/ARO_3000370 antibiotic resistant DNA topoisomerase subunit ParE is a subunit of topoisomerase IV, which decatenates and relaxes DNA to allow access to genes for transcription or translation. Mutations in ParE prevents antibiotics from inhibiting DNA synthesis, thus conferring resistance. http://purl.obolibrary.org/obo/ARO_3000116 vanZ http://purl.obolibrary.org/obo/ARO_3002976 gene(s) or protein(s) associated with a glycopeptide resistance cluster VanZ is a teicoplanin resistance gene that is an accessory protein. VanZ prevents the incorporation of the terminal D-Ala into peptidoglycan subunits. http://purl.obolibrary.org/obo/ARO_3000117 antibiotic A47934 http://purl.obolibrary.org/obo/ARO_3000081 glycopeptide antibiotic A47934 is an 'aglycone' glycopeptide antibiotic produced by Streptomyces toyocaensis. It is a teicoplanin-like glycopeptide. http://purl.obolibrary.org/obo/ARO_3000118 vgaB http://purl.obolibrary.org/obo/ARO_3000113 vga-type ABC-F protein Vga(B) is an ABC-F protein expressed in staphylococci that confers resistance to streptogramin A antibiotics and related compounds. It is associated with plasmid DNA. http://purl.obolibrary.org/obo/ARO_3000119 edeine http://purl.obolibrary.org/obo/ARO_3000053 peptide antibiotic Edeines are basic linear peptides produced by Bacillus brevis Vm4. They have antibacterial as well as antifungal, antiviral, and anticancer properties. Edeines are bacteriostatic and bacteriocidal at low and high concentrations, respectively. They are able to inhibit DNA synthesis and protein translation. These compounds are synthesized by nonribosomal peptide synthetases and contain numerous unusual amino acids. http://purl.obolibrary.org/obo/ARO_3000120 balhimycin http://purl.obolibrary.org/obo/ARO_3000081 glycopeptide antibiotic Balhimycin is a vancomycin-like glycopeptide antibiotic produced by Amycolatopsis balhimycina. It binds to the terminal Lys-D-Ala-D-Ala of peptidoglycan precursors. http://purl.obolibrary.org/obo/ARO_3000121 aminoglycoside acetyltransferase (AAC) http://purl.obolibrary.org/obo/ARO_3007380 aminoglycoside modifying enzyme Aminoglycoside acetyltransferase enzymes modify aminoglycoside antibiotics by catalyzing the transfer of an acetyl group to one of the amino groups present in aminoglycosides, using acetyl coenzyme A as a donor substrate. http://purl.obolibrary.org/obo/ARO_3000122 chloramphenicol acetyltransferase (CAT) http://purl.obolibrary.org/obo/ARO_3000557 antibiotic inactivation enzyme Inactivates chloramphenicol by addition of an acyl group. CAT is used to describe many variants of the chloramphenicol acetyltransferase gene in a range of organisms including Acinetobacter calcoaceticus, Agrobacterium tumefaciens, Alkalihalobacillus clausii, Bacillus subtilis, Campylobacter coli, Enterococcus faecalis, Enterococcus faecium, Lactococcus lactis, Listeria monocytogenes, Listonella anguillarum, Morganella morganii, Photobacterium damselae subsp. piscicida, Proteus mirabilis, Salmonella typhi, Serratia marcescens, Shigella flexneri, Staphylococcus aureus, Staphylococcus haemolyticus, Staphylococcus intermedius, Streptococcus agalactiae, Streptococcus suis and Streptomyces acrimycini. http://purl.obolibrary.org/obo/ARO_3000123 gramicidin http://purl.obolibrary.org/obo/ARO_3000053 peptide antibiotic Gramicidins are a family of antibiotics synthesized by Bacillus brevis. It includes the linear pentadecapeptides gramicidin A, B and C that make up the mixture gramicidin D. Gramicidin S is a cyclic peptide chain. Gramicidins are also components of tyrothricins, another mixture of antibiotics produced by Bacillus brevis. http://purl.obolibrary.org/obo/ARO_3000124 mecI http://purl.obolibrary.org/obo/ARO_3000100 gene modulating beta-lactam resistance mecI acts as a repressor of transcription of the mecA/mecR1/mecI operon. http://purl.obolibrary.org/obo/ARO_3000125 hydrolysis of fosfomycin epoxide ring http://purl.obolibrary.org/obo/ARO_3000040 hydrolysis of antibiotic conferring resistance The use of different nucleophilic molecules by enzymes can break up the epoxide ring of fosfomycin and render the molecule ineffective. http://purl.obolibrary.org/obo/ARO_3000126 APH(3') http://purl.obolibrary.org/obo/ARO_3000114 aminoglycoside phosphotransferase (APH) A category of aminoglycoside O-phosphotransferase enzymes with modification regiospecificity based at the 3'-hydroxyl group of the respective antibiotic. These enzymes inactivate aminoglycoside antibiotics, specifically kanamycin and neomycin, by the ATP-dependent phosphorylation of the 3'-hydroxyl group of the compound. http://purl.obolibrary.org/obo/ARO_3000127 APH(3'') http://purl.obolibrary.org/obo/ARO_3000114 aminoglycoside phosphotransferase (APH) A category of aminoglycoside O-phosphotransferase enzymes with modification regiospecificity based at the 3''-hydroxyl group of the respective antibiotic. These enzymes are characterized by enzymatic antibiotic inactivation, specifically of streptomycin, by the ATP-dependent phosphorylation of the 3''-hydroxyl group of the compound. http://purl.obolibrary.org/obo/ARO_3000128 APH(2'') http://purl.obolibrary.org/obo/ARO_3000114 aminoglycoside phosphotransferase (APH) A category of aminoglycoside O-phosphotransferase enzymes with modification regiospecificity based at the 2''-hydroxyl group of the respective antibiotic. These enzymes inactivate aminoglycoside antibiotics, specifically kanamycin, tobramycin and amikacin, by the ATP-dependent phosphorylation of the 3'-hydroxyl group of the compound. http://purl.obolibrary.org/obo/ARO_3000130 edeine A http://purl.obolibrary.org/obo/ARO_3000119 edeine Edeine A is a subtype of the peptide antibiotic edeine, composed of beta-tyr, beta-ser, diaminopropionic acid, diaminohydroxyazelaic acid, glycine, and spermidine. Edeine A is a mixture of edeine A1 and its inactive isomer, edeine A2. Edeines bind to the 30S subunit to block fMet-tRNA interaction at the P site, inhibiting protein synthesis and subsequent structure/function processes critical for life or replication. http://purl.obolibrary.org/obo/ARO_3000132 clorobiocin http://purl.obolibrary.org/obo/ARO_3000103 aminocoumarin antibiotic Clorobiocin is an aminocoumarin antibiotic produced by Streptomyces roseochromogenes, and binds DNA gyrase subunit B to inhibit ATP-dependent DNA supercoiling. http://purl.obolibrary.org/obo/ARO_3000133 fosfomycin thiol transferase http://purl.obolibrary.org/obo/ARO_3000342 fosfomycin inactivation enzyme Catalyzes the addition of a thiol group from a nucleophilic molecule to fosfomycin. http://purl.obolibrary.org/obo/ARO_3000134 edeine B http://purl.obolibrary.org/obo/ARO_3000119 edeine Edeine B is a subtype of the peptide antibiotic edeine, composed of beta-tyr, beta-ser, diaminopropionic acid, diaminohydroxyazelaic acid, glycine, and guanylspermidine. Edeine B is a mixture of edeine B1 and its inactive isomer, edeine B2. Edeines bind to the 30S subunit to block fMet-tRNA interaction at the P site, inhibiting protein synthesis and subsequent structure/function processes critical for life or replication. Edeine B has also been shown to inhibit septation and cause filamentous morphology, also leading to cell death. http://purl.obolibrary.org/obo/ARO_3000135 edeine D http://purl.obolibrary.org/obo/ARO_3000119 edeine Edeine D is a subtype of edeine similar to edeine A with the beta-tyr replaced by beta-phe-beta-ala. Edeines bind to the 30S subunit to block fMet-tRNA interaction at the P site, inhibiting protein synthesis and subsequent structure/function processes critical for life or replication. http://purl.obolibrary.org/obo/ARO_3000136 edeine F http://purl.obolibrary.org/obo/ARO_3000119 edeine Edeine F is a subtype of edeine similar to edeine B with beta-tyr replaced by beta-phe-beta-ala. Edeines bind to the 30S subunit to block fMet-tRNA interaction at the P site, inhibiting protein synthesis and subsequent structure/function processes critical for life or replication. http://purl.obolibrary.org/obo/ARO_3000145 tylosin http://purl.obolibrary.org/obo/ARO_0000000 macrolide antibiotic Tylosin is a 16-membered macrolide, naturally produced by Streptomyces fradiae. It interacts with the bacterial ribosome 50S subunit to inhibit protein synthesis. http://purl.obolibrary.org/obo/ARO_3000149 FosA http://purl.obolibrary.org/obo/ARO_3000133 fosfomycin thiol transferase An enzyme that confers resistance to fosfomycin in Serratia marcescens by breaking the epoxide ring of the molecule. It depends on the cofactors Manganese (II) and Potassium and uses Glutathione (GSH) as the nucleophilic molecule. In Pseudomonas aeruginosa, FosA catalyzes the conjugation of glutathione to carbon-1 of fosfomycin, rendering it ineffective as an antibacterial drug. http://purl.obolibrary.org/obo/ARO_3000150 coumermycin A1 http://purl.obolibrary.org/obo/ARO_3000103 aminocoumarin antibiotic Coumermycin A1 is an antibiotic produced by Streptomyces rishiriensis, and binds DNA gyrase subunit B to inhibit ATP-dependent DNA supercoiling. http://purl.obolibrary.org/obo/ARO_3000151 APH(6) http://purl.obolibrary.org/obo/ARO_3000114 aminoglycoside phosphotransferase (APH) A category of aminoglycoside O-phosphotransferase enzymes with modification regiospecificity based at the 6-hydroxyl group of the respective antibiotic. These enzymes are characterized by enzymatic antibiotic inactivation, specifically of streptomycin, by the ATP-dependent phosphorylation of the 6-hydroxyl group of the compound. http://purl.obolibrary.org/obo/ARO_3000152 minocycline http://purl.obolibrary.org/obo/ARO_3000050 tetracycline antibiotic Minocycline is second generation semi-synthetic derivative of the tetracycline group of antibiotics. It inhibits bacterial protein synthesis by binding to the 30S subunit of the bacterial ribosome and preventing the aminotransferase-tRNA from associating with the ribosome. http://purl.obolibrary.org/obo/ARO_3000153 APH(9) http://purl.obolibrary.org/obo/ARO_3000114 aminoglycoside phosphotransferase (APH) A category of aminoglycoside O-phosphotransferase enzymes with modification regiospecificity based at the 9-hydroxyl group of the respective antibiotic. These enzymes are characterized by enzymatic antibiotic inactivation, specifically of spectinomycin, by the ATP-dependent phosphorylation of the 9-hydroxyl group of the compound. http://purl.obolibrary.org/obo/ARO_3000154 APH(7'') http://purl.obolibrary.org/obo/ARO_3000114 aminoglycoside phosphotransferase (APH) A category of aminoglycoside O-phosphotransferase enzymes with modification regiospecificity based at the 7''-hydroxyl group of the respective antibiotic. These enzymes are characterized by enzymatic antibiotic inactivation, specifically of hygromycin, by the ATP-dependent phosphorylation of the 7''-hydroxyl group of the compound. http://purl.obolibrary.org/obo/ARO_3000155 APH(4) http://purl.obolibrary.org/obo/ARO_3000114 aminoglycoside phosphotransferase (APH) A category of aminoglycoside O-phosphotransferase enzymes with modification regiospecificity based at the 4-hydroxyl group of the respective antibiotic. These enzymes are characterized by enzymatic antibiotic inactivation, specifically of hygromycin, by the ATP-dependent phosphorylation of the 4-hydroxyl group of the compound. http://purl.obolibrary.org/obo/ARO_3000156 spiramycin http://purl.obolibrary.org/obo/ARO_0000000 macrolide antibiotic Spiramycin is a 16-membered macrolide and is natural product produced by Streptomyces ambofaciens. It binds to the 50S subunit of bacterial ribosomes and inhibits peptidyl transfer activity to disrupt protein synthesis. http://purl.obolibrary.org/obo/ARO_3000157 rifamycin antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule Rifamycin antibiotics are a group of broad-spectrum ansamycin antibiotics that inhibit bacterial RNA polymerase by binding to a highly conserved region, blocking the oligonucleotide exit tunnel, and preventing the extension of nascent mRNAs. http://purl.obolibrary.org/obo/ARO_3000158 azithromycin http://purl.obolibrary.org/obo/ARO_0000000 macrolide antibiotic Azithromycin is a 15-membered macrolide and falls under the subclass of azalide. Like other macrolides, azithromycin binds bacterial ribosomes to inhibit protein synthesis. The nitrogen substitution at the C-9a position prevents its degradation. http://purl.obolibrary.org/obo/ARO_3000159 efflux pump complex or subunit conferring antibiotic resistance http://purl.obolibrary.org/obo/ARO_3000000 determinant of antibiotic resistance Efflux proteins that pump antibiotic out of a cell to confer resistance. http://purl.obolibrary.org/obo/ARO_3000160 blaI http://purl.obolibrary.org/obo/ARO_3000100 gene modulating beta-lactam resistance blaI acts as a repressor of transcription of the blaZ/blaR1/blaI operon. http://purl.obolibrary.org/obo/ARO_3000164 rRNA methyltransferase conferring antibiotic resistance http://purl.obolibrary.org/obo/ARO_3000519 antibiotic target modifying enzyme Catalyzes methylation of rRNA. http://purl.obolibrary.org/obo/ARO_3000165 tet(A) http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump TetA is a tetracycline efflux pump found in many species of Gram-negative bacteria. http://purl.obolibrary.org/obo/ARO_3000166 tet(B) http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump Tet(B) is a tetracycline efflux protein expressed in many Gram-negative bacteria. It confers resistance to tetracycline, doxycycline, and minocycline, but not tigecycline. http://purl.obolibrary.org/obo/ARO_3000167 tet(C) http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump Tet(C) is a tetracycline efflux pump found in many species of Gram-negative bacteria. It is typically found in plasmid DNA. http://purl.obolibrary.org/obo/ARO_3000168 tet(D) http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump TetD is a tetracycline efflux pump found exclusively in Gram-negative bacteria. http://purl.obolibrary.org/obo/ARO_3000169 rifampin http://purl.obolibrary.org/obo/ARO_3000157 rifamycin antibiotic Rifampin is a semi-synthetic rifamycin, and inhibits RNA synthesis by binding to RNA polymerase. Rifampin is the mainstay agent for the treatment of tuberculosis, leprosy and complicated Gram-positive infections. http://purl.obolibrary.org/obo/ARO_3000170 imipenem http://purl.obolibrary.org/obo/ARO_0000020 carbapenem Imipenem is a broad-spectrum antibiotic and is usually taken with cilastatin, which prevents hydrolysis of imipenem by renal dehydropeptidase-I. It is resistant to hydrolysis by most other beta-lactamases. Notable exceptions are the KPC beta-lactamases and Ambler Class B enzymes. http://purl.obolibrary.org/obo/ARO_3000171 diaminopyrimidine antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule Diaminopyrimidines are a class of organic compounds containing a pyrimidine ring substituted by two amine groups. They are inhibitors of dihydrofolate reductase, an enzyme critical for DNA synthesis. http://purl.obolibrary.org/obo/ARO_3000172 FosB http://purl.obolibrary.org/obo/ARO_3000133 fosfomycin thiol transferase A thiol transferase that leads to the resistance of fosfomycin. Contrasting FosA, FosB is dependent on the cofactor Magnesium (II) and uses either bacillithiol or L-cysteine to open up the epoxide ring of fosfomycin. http://purl.obolibrary.org/obo/ARO_3000173 tet(E) http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump TetE is a tetracycline efflux pump found in many Gram-negative bacteria, especially those in water environments. The gene is found on large plasmids. http://purl.obolibrary.org/obo/ARO_3000174 tet(G) http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump TetG is a tetracycline efflux protein found in Gram-negative bacteria. The encoding gene is found in both chromosomal and plasmid DNA where it is frequently linked to the floR, sul1, and cmlA9 genes which encode proteins that can confer florfenicol/chloramphenicol, sulfamethoxazole, and chloramphenicol resistance, respectively. http://purl.obolibrary.org/obo/ARO_3000175 tet(H) http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump TetH is a tetracycline efflux protein expressed in Gram-negative bacteria (Actinobacillus, Acinetobacter, Gallibacterium, Histophilus, Mannheimia, Moraxella, Pasteurella, and Psychrobacter). Its gene is linked to the resistance genes sul2, and strA, which confer resistance to sulfamethoxazole and streptomycin, respectively. http://purl.obolibrary.org/obo/ARO_3000176 dirithromycin http://purl.obolibrary.org/obo/ARO_0000000 macrolide antibiotic Dirithromycin is an oxazine derivative of erythromycin, sharing the 14-carbon macrolide ring. The antibiotic binds to the 50S subunit of the ribosome to inhibit bacterial protein synthesis. http://purl.obolibrary.org/obo/ARO_3000177 tet(J) http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump TetJ is a tetracycline efflux protein expressed in Gram-negative bacteria (Escherichia, Morganella, and Proteus). http://purl.obolibrary.org/obo/ARO_3000178 tet(K) http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump TetK is a tetracycline efflux protein found in both Gram-negative (Haemophilus and Gallibacterium) and Gram-positive (many species, including mycobacteria) bacteria. http://purl.obolibrary.org/obo/ARO_3000179 tet(L) http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump TetL is a tetracycline efflux protein found in many species of Gram-negative and Gram-positive bacteria. http://purl.obolibrary.org/obo/ARO_3000180 tetA(P) http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump TetA(P) is a inner membrane tetracycline efflux protein found on the same operon as the ribosomal protection protein TetB(P). It is found in Clostridium, a Gram-positive bacterium. http://purl.obolibrary.org/obo/ARO_3000181 tet(V) http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump TetV is a tetracycline efflux protein that has been found in Mycolicibacterium smegmatis and Mycolicibacterium fortuitum. http://purl.obolibrary.org/obo/ARO_3000182 tet(Y) http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump TetY is a tetracycline efflux pump found in Gram-negative bacteria (Aeromonas and Escherichia). It is associated with plasmid DNA. http://purl.obolibrary.org/obo/ARO_3000183 tet(Z) http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump TetZ is a tetracycline efflux protein found in Gram-positive bacteria (Corynebacterium and Lactobacillus). It is associated with plasmid DNA. http://purl.obolibrary.org/obo/ARO_3000184 chloroeremomycin http://purl.obolibrary.org/obo/ARO_3000081 glycopeptide antibiotic Chloroeremomycin is a vancomycin-like glycopeptide, with three sugars instead of two in vancomycin and balhimycin. Chloroeremomycin dimerizes and binds to the terminus of peptidoglycan precursors. http://purl.obolibrary.org/obo/ARO_3000185 antibiotic target protection protein http://purl.obolibrary.org/obo/ARO_3000000 determinant of antibiotic resistance These proteins confer antibiotic resistance by bind the antibiotic target to prevent antibiotic binding. http://purl.obolibrary.org/obo/ARO_3000186 tet(M) http://purl.obolibrary.org/obo/ARO_0000002 tetracycline-resistant ribosomal protection protein Tet(M) is a ribosomal protection protein that confers tetracycline resistance. It is found on transposable DNA elements and its horizontal transfer between bacterial species has been documented. http://purl.obolibrary.org/obo/ARO_3000187 hydrolysis of beta-lactam antibiotic by serine beta-lactamase http://purl.obolibrary.org/obo/ARO_3000040 hydrolysis of antibiotic conferring resistance Mechanism of enzymatic degradation common to Ambler Class A, C and D beta-lactamases. A serine residue located in the active site is used to form an acyl-enzyme intermediate and subsequent hydrolysis renders the beta-lactam inactive. http://purl.obolibrary.org/obo/ARO_3000188 trimethoprim http://purl.obolibrary.org/obo/ARO_3000171 diaminopyrimidine antibiotic Trimethoprim is a synthetic 5-(3,4,5- trimethoxybenzyl) pyrimidine inhibitor of dihydrofolate reductase, inhibiting synthesis of tetrahydrofolic acid. Tetrahydrofolic acid is an essential precursor in the de novo synthesis of the DNA nucleotide thymidine. Trimethoprim is a bacteriostatic antibiotic mainly used in the prophylaxis and treatment of urinary tract infections in combination with sulfamethoxazole, a sulfonamide antibiotic. http://purl.obolibrary.org/obo/ARO_3000189 oritavancin http://purl.obolibrary.org/obo/ARO_3000081 glycopeptide antibiotic Oritavancin is a semi-synthetic derivative of chloroeremomycin, a vancomycin-like glycopeptide. Oritavancin inhibits both transglycosylation and transpeptidation, by binding both the D-Ala-D-Ala and pentaglycine bridge segments of peptidoglycan to inhibit cell wall formation. http://purl.obolibrary.org/obo/ARO_3000190 tet(O) http://purl.obolibrary.org/obo/ARO_0000002 tetracycline-resistant ribosomal protection protein Tet(O) is a ribosomal protection protein. It is associated with conjugative plasmids. http://purl.obolibrary.org/obo/ARO_3000191 tet(Q) http://purl.obolibrary.org/obo/ARO_0000002 tetracycline-resistant ribosomal protection protein Tet(Q) is a ribosomal protection protein. Its gene is associated with a conjugative transposon and has been found in both Gram-positive and Gram-negative bacteria. http://purl.obolibrary.org/obo/ARO_3000192 tet(S) http://purl.obolibrary.org/obo/ARO_0000002 tetracycline-resistant ribosomal protection protein Tet(S) is a ribosomal protection protein found in Gram-positive and Gram-negative strains. It is similar to tet(M) and tet(O). http://purl.obolibrary.org/obo/ARO_3000193 tet(T) http://purl.obolibrary.org/obo/ARO_0000002 tetracycline-resistant ribosomal protection protein Tet(T) is a ribosomal protection protein of streptococci. It is similar to Tet(Q). http://purl.obolibrary.org/obo/ARO_3000194 tet(W) http://purl.obolibrary.org/obo/ARO_0000002 tetracycline-resistant ribosomal protection protein Tet(W) is a ribosomal protection protein. It is associated with both conjugative and non conjugative DNA and has been found strains of Clostridioides difficile. http://purl.obolibrary.org/obo/ARO_3000195 tetB(P) http://purl.obolibrary.org/obo/ARO_0000002 tetracycline-resistant ribosomal protection protein TetB(P) is a tetracycline ribosomal protection protein found on the same operon as tetA(P), a tetracycline efflux protein. http://purl.obolibrary.org/obo/ARO_3000196 tet(32) http://purl.obolibrary.org/obo/ARO_0000002 tetracycline-resistant ribosomal protection protein Tet(32) is a tetracycline resistance gene similar to Tet(O), and binds to the ribosome to confer tetracycline resistance as a ribosomal protection protein. http://purl.obolibrary.org/obo/ARO_3000197 tet(36) http://purl.obolibrary.org/obo/ARO_0000002 tetracycline-resistant ribosomal protection protein Tet(36) is a tetracycline resistance gene found in Bacteroides similar to Tet(Q), and binds to the ribosome to confer antibiotic resistance as a ribosomal protection protein. http://purl.obolibrary.org/obo/ARO_3000198 FosX http://purl.obolibrary.org/obo/ARO_3000133 fosfomycin thiol transferase FosX is an enzyme used to confer resistance to fosfomycin. It's dependent on the cofactor, manganese (II), and uses water to generate a vicinal diol. http://purl.obolibrary.org/obo/ARO_3000199 gramicidin D http://purl.obolibrary.org/obo/ARO_3000707 antibiotic mixture Gramicidin D is a mixture of the linear peptides gramicidin A, B, and C, each with 15 alternating L- and D-amino acids. They are active against most gram-positive bacteria and select gram-negative bacteria. These compounds create channels in the bacterial membrane and increase the permeability to cations. http://purl.obolibrary.org/obo/ARO_3000200 gramicidin S http://purl.obolibrary.org/obo/ARO_3000123 gramicidin Gramicidin S is a cyclical decapeptide with two pentapeptides (Val-Orn-Leu-D-Phe-Pro) joined head to tail. Like other gramicidins, Gramicidin S disrupts membrane permeability of cations while also destabilizing the membrane at higher concentrations. http://purl.obolibrary.org/obo/ARO_3000201 macrolide inactivation enzyme http://purl.obolibrary.org/obo/ARO_3000557 antibiotic inactivation enzyme Enzymes shown to inactivate macrolide antibiotics by chemical modification, thereby conferring resistance to macrolides. http://purl.obolibrary.org/obo/ARO_3000202 Cfr 23S ribosomal RNA methyltransferase http://purl.obolibrary.org/obo/ARO_3004575 S-adenosylmethionine (SAM) superfamily Cfr genes produce enzymes which catalyze the methylation of the 23S rRNA subunit at position 8 of adenine-2503. Methylation of 23S rRNA at this site confers resistance to some classes of antibiotics, including streptogramins, chloramphenicols, florfenicols, linezolids and clindamycin. http://purl.obolibrary.org/obo/ARO_3000203 hydrolysis of beta-lactam antibiotic by metallo-beta-lactamase http://purl.obolibrary.org/obo/ARO_3000040 hydrolysis of antibiotic conferring resistance Mechanism of enzymatic degradation common to Ambler Class B beta-lactamases. One or two zinc atoms are used to orient a hydroxide nucleophile for attack of the beta-lactam ring. In contrast to serine beta-lactamases, no acyl-enzyme intermediate is formed. http://purl.obolibrary.org/obo/ARO_3000205 tet(X) http://purl.obolibrary.org/obo/ARO_3000036 tetracycline inactivation enzyme Tet(X) is a flavin-dependent monooxygenase conferring resistance to tetracycline antibiotics. Tet(X) hydroxylates position 11a of the tetraketide group thus inactivating the antibiotic. http://purl.obolibrary.org/obo/ARO_3000206 emrK http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance emrK is a membrane fusion protein that is a homolog of EmrA. Together with the inner membrane transporter EmrY and the outer membrane channel TolC, it mediates multidrug efflux. http://purl.obolibrary.org/obo/ARO_3000207 acrA http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance Protein subunit of AcrA-AcrB-TolC multidrug efflux complex. AcrA represents the periplasmic portion of the transport protein. http://purl.obolibrary.org/obo/ARO_3000208 glycosylation of antibiotic conferring resistance http://purl.obolibrary.org/obo/ARO_0001004 antibiotic inactivation Addition of glycosyl moiety to antibiotics thereby inactivating them. http://purl.obolibrary.org/obo/ARO_3000209 antibiotic resistant DNA topoisomerase subunit parY http://purl.obolibrary.org/obo/ARO_3000370 antibiotic resistant DNA topoisomerase subunit ParY is part of a topoisomerase IV that is resistant to antibiotics that affect other topoisomerases. http://purl.obolibrary.org/obo/ARO_3000210 rifamycin-resistant beta-subunit of RNA polymerase (rpoB) http://purl.obolibrary.org/obo/ARO_3003276 antibiotic resistant rpoB Rifampin resistant RNA polymerases include amino acids substitutions which disrupt the affinity of rifampin for its binding site. These mutations are frequently concentrated in the rif I region of the beta-subunit and most often involve amino acids which make direct interactions with rifampin. However, mutations which also confer resistance can occur outside this region and may involve amino acids which do not directly make contact with rifampin. http://purl.obolibrary.org/obo/ARO_3000211 ribosomal alteration conferring antibiotic resistance http://purl.obolibrary.org/obo/ARO_0001001 antibiotic target alteration Chemical alteration of the ribosome results in modification of an antibiotic's target leading to resistance. http://purl.obolibrary.org/obo/ARO_3000212 mutation conferring antibiotic resistance http://purl.obolibrary.org/obo/ARO_0001001 antibiotic target alteration Point mutations in the DNA may lead to an altered gene product that may result in antibiotic resistance. Examples included modified antibiotic targets with lower binding affinities and the deactivation of repressors that result in increased expression of genes that inactivate or pump out antibiotics. http://purl.obolibrary.org/obo/ARO_3000213 restructuring of bacterial cell wall conferring antibiotic resistance http://purl.obolibrary.org/obo/ARO_0001001 antibiotic target alteration Peptidoglycan precursors ending in D-Ala-D-Lac or D-Ala-D-Ser instead of D-Ala-D-Ala conferring high level glycopeptide resistance. http://purl.obolibrary.org/obo/ARO_3000214 hygromycin B http://purl.obolibrary.org/obo/ARO_0000016 aminoglycoside antibiotic Hygromycin B is an aminoglycoside antibiotic used to treat different types of bacterial infections. Hygromycin B works by binding to the bacterial 30S ribosomal subunit, causing misreading of mRNA and leaving the bacterium unable to synthesize proteins vital to its growth. Hygromycin B has also been shown to interact with eukaryotic cells. http://purl.obolibrary.org/obo/ARO_3000215 mecR1 http://purl.obolibrary.org/obo/ARO_3000100 gene modulating beta-lactam resistance mecR1 is a transmembrane spanning and signal transducing protein which in response to interaction with beta-lactam antibiotics results in upregulation of the mecA/mecR1/mecI operon. http://purl.obolibrary.org/obo/ARO_3000216 acrB http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance Protein subunit of AcrA-AcrB-TolC multidrug efflux complex. AcrB functions as a herterotrimer which forms the inner membrane component and is primarily responsible for substrate recognition and energy transduction by acting as a drug/proton antiporter. http://purl.obolibrary.org/obo/ARO_3000217 blaR1 http://purl.obolibrary.org/obo/ARO_3000100 gene modulating beta-lactam resistance blaR1 is a transmembrane spanning and signal transducing protein which in response to interaction with beta-lactam antibiotics results in upregulation of the blaZ/blaR1/blaI operon. http://purl.obolibrary.org/obo/ARO_3000218 aminoglycoside nucleotidyltransferase (ANT) http://purl.obolibrary.org/obo/ARO_3007380 aminoglycoside modifying enzyme Covalent modification of aminoglycoside antibiotic hydroxyl group by ATP-dependent transfer of AMP. http://purl.obolibrary.org/obo/ARO_3000219 mutant efflux regulatory protein conferring antibiotic resistance http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Efflux regulatory proteins with mutations that result in increased expression of efflux proteins. http://purl.obolibrary.org/obo/ARO_3000220 antibiotic resistant DNA topoisomerase subunit gyrB http://purl.obolibrary.org/obo/ARO_3000370 antibiotic resistant DNA topoisomerase subunit Point mutations in gyrB confer antibiotic resistance by preventing drugs from binding the beta-subunit of gyrase, essential for DNA supercoiling. http://purl.obolibrary.org/obo/ARO_3000221 lincosamide nucleotidyltransferase (LNU) http://purl.obolibrary.org/obo/ARO_3000557 antibiotic inactivation enzyme Resistance to the lincosamide antibiotic by ATP-dependent modification of the 3' and/or 4'-hydroxyl groups of the methylthiolincosamide sugar. http://purl.obolibrary.org/obo/ARO_3000222 gramicidin A http://purl.obolibrary.org/obo/ARO_3000123 gramicidin Gramicidin A is the most abundant (more than 80%) of the three gramicidins in gramicidin D, with a tryptophan in position 11. Gramicidins form dimers in the bacterial membrane that increase the permeability of cations. http://purl.obolibrary.org/obo/ARO_3000223 gramicidin B http://purl.obolibrary.org/obo/ARO_3000123 gramicidin Gramicidin B is one of the three gramicidins in gramicidin D, with a phenylalanine in position 11. It is structurally similar to gramicidin A, but its ability to induce the assembly of bilayers is reduced. Gramicidins form dimers in the bacterial membrane that increase the permeability of cations. http://purl.obolibrary.org/obo/ARO_3000224 gramicidin C http://purl.obolibrary.org/obo/ARO_3000123 gramicidin Gramicidin C is one of the three gramicidins in gramicidin D, with a tyrosine in position 11. It is structurally similar to gramicidin A, but its ability to induce the assembly of bilayers is reduced. Gramicidins form dimers in the bacterial membrane that increase the permeability of cations. http://purl.obolibrary.org/obo/ARO_3000225 ANT(6) http://purl.obolibrary.org/obo/ARO_3000218 aminoglycoside nucleotidyltransferase (ANT) A category of aminoglycoside O-nucleotidyltransferase enzymes with modification regiospecificity based at the 6-hydroxyl group of the respective antibiotic. These enzymes inactivate aminoglycoside antibiotics, specifically streptomycin, by transfer of an AMP group from an ATP substrate to the 6-hydroxyl group of the compound. http://purl.obolibrary.org/obo/ARO_3000226 antibiotic resistant folP http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Point mutations in dihydropteroate synthase folP prevent sulfonamide antibiotics from inhibiting its role in folate synthesis, thus conferring sulfonamide resistance. http://purl.obolibrary.org/obo/ARO_3000227 tyrothricin http://purl.obolibrary.org/obo/ARO_3000707 antibiotic mixture Tyrothricin is a mixture of antibiotics including tyrocidines and gramicidins, isolated from Bacillus brevis. http://purl.obolibrary.org/obo/ARO_3000228 ANT(9) http://purl.obolibrary.org/obo/ARO_3000218 aminoglycoside nucleotidyltransferase (ANT) A category of aminoglycoside O-nucleotidyltransferase enzymes with modification regiospecificity based at the 9-hydroxyl group of the respective antibiotic. These enzymes inactivate aminoglycoside antibiotics, specifically streptomycin, by transfer of an AMP group from an ATP substrate to the 9-hydroxyl group of the compound. http://purl.obolibrary.org/obo/ARO_3000229 ANT(4') http://purl.obolibrary.org/obo/ARO_3000218 aminoglycoside nucleotidyltransferase (ANT) A category of aminoglycoside O-nucleotidyltransferase enzymes with modification regiospecificity based at the 4'-hydroxyl group of the respective antibiotic. These enzymes inactivate aminoglycoside antibiotics by transfer of an AMP group from an ATP substrate to the 4-hydroxyl group of the compound. http://purl.obolibrary.org/obo/ARO_3000230 ANT(2'')-Ia http://purl.obolibrary.org/obo/ARO_3007405 ANT(2'')-I Plasmid or integron-encoded nucleotidylylation of 2-deoxystreptamine aminoglycosides at the hydroxyl group at position 2'' in P. aeruginosa, K. pneumoniae, Morganella morganii, E. coli, S. typhimurium, C. freundii and A. baumannii. http://purl.obolibrary.org/obo/ARO_3000231 beta-lactam resistance operon http://purl.obolibrary.org/obo/ARO_0000010 antibiotic resistance gene cluster, cassette, or operon An operon conferring resistance to beta-lactam antibiotics. http://purl.obolibrary.org/obo/ARO_3000232 ANT(3'')-Ia http://purl.obolibrary.org/obo/ARO_3007407 ANT(3'')-I Nucleotidylylation of streptomycin at the hydroxyl group at position 3''. http://purl.obolibrary.org/obo/ARO_3000233 streptogramin inactivation enzyme http://purl.obolibrary.org/obo/ARO_3000557 antibiotic inactivation enzyme Resistance to streptogramin antibiotics may be conferred through enzymatic inactivation. There are two known mechanisms of streptogramin inactivation shown clinically to confer resistance: 1) vgB lyase enzymes linearize type B streptogramin antibiotics by breaking the ester linkage; 2) vat acetyltransferase enzymes modify type A streptogramin antibiotics by transferring an acetyl group from acetyl-CoA to the secondary streptogramin hydroxyl. Both mechanisms result in antibiotic inactivation thus conferring resistance. http://purl.obolibrary.org/obo/ARO_3000234 glycopeptide resistance gene cluster http://purl.obolibrary.org/obo/ARO_0000010 antibiotic resistance gene cluster, cassette, or operon Genes that when expressed confer resistance to vancomycin and teicoplanin type antibiotics. http://purl.obolibrary.org/obo/ARO_3000235 ethambutol resistant embB http://purl.obolibrary.org/obo/ARO_3005005 antibiotic-resistant emb arabinosyltransferase embB gene encodes for an arabinosyl transferase in the arabinogalactan synthesis pathway. It is inhibited by ethambutol. Mutations within the ERDR region of embB confers resistance to ethambutol. http://purl.obolibrary.org/obo/ARO_3000236 glycopeptide resistance gene cluster VanA http://purl.obolibrary.org/obo/ARO_3000234 glycopeptide resistance gene cluster This inducible cluster confers high resistance to both vancomycin and teicoplanin by allowing restructuring of peptidoglycan precursors to end in D-Ala-D-Lac. The vanA gene cluster can be located either on plasmids or on the chromosome. Gene orientation: vanRSHAXYZ. http://purl.obolibrary.org/obo/ARO_3000237 TolC http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance TolC is a protein subunit of many multidrug efflux complexes in Gram negative bacteria. It is an outer membrane efflux protein and is constitutively open. Regulation of efflux activity is often at its periplasmic entrance by other components of the efflux complex. http://purl.obolibrary.org/obo/ARO_3000238 glycopeptide resistance gene cluster VanB http://purl.obolibrary.org/obo/ARO_3000234 glycopeptide resistance gene cluster This inducible cluster confers resistance to vancomycin but organisms remain sensitive to teicoplanin by allowing restructuring of peptidoglycan precursors to end in D-Ala-D-Lac. Sensitivity to teicoplanin is due to lack of binding to the sensor kinase VanS. The vanB gene cluster can be located either on plasmids or on the chromosome. Gene orientation: vanRSYWHBX. http://purl.obolibrary.org/obo/ARO_3000244 reduced permeability to antibiotic http://purl.obolibrary.org/obo/ARO_1000002 mechanism of antibiotic resistance Reduction in permeability to antibiotic, generally through reduced production of porins, can provide resistance. http://purl.obolibrary.org/obo/ARO_3000245 RbpA http://purl.obolibrary.org/obo/ARO_3004243 RbpA bacterial RNA polymerase-binding protein RNA-polymerase binding protein which confers resistance to rifampin. http://purl.obolibrary.org/obo/ARO_3000246 glycopeptide resistance gene cluster VanC http://purl.obolibrary.org/obo/ARO_3000234 glycopeptide resistance gene cluster Confers low vancomycin resistance by engineering peptidoglycan precursors ending in D-Ala-D-Ser in an inducible or constitutive manner. The vanC cluster is intrinsic to the Enterococcus gallinarum chromosome. vanC organisms remain susceptible to teicoplanin. Gene orientation: vanC(XY)TRS. http://purl.obolibrary.org/obo/ARO_3000247 phosphoenolpyruvate (PEP) mutase http://purl.obolibrary.org/obo/ARO_3000082 antibiotic biosynthesis A tetrameric protein that converts phosphoenolpyruvate (PEP) to phosponopyruvate (Ppyr). http://purl.obolibrary.org/obo/ARO_3000248 DnaA http://purl.obolibrary.org/obo/ARO_3004244 DnaA chromosomal replication initiation protein DnaA is a chromosomal replication initiation protein which binds and interacts with RNA polymerase in Escherichia coli. A surplus of DnaA present in a cell has been shown to confer resistance to the antibiotic Rifampicin. Normally, rifampicin inhibits initiation of transcription by RNA polymerase, but a surplus of DnaA available at the origin has been shown to disrupt Rifampicin activity and confer resistance. http://purl.obolibrary.org/obo/ARO_3000249 chloramphenicol phosphotransferase http://purl.obolibrary.org/obo/ARO_3000557 antibiotic inactivation enzyme ATP-dependent kinase modifies the C-3 hydroxyl group of chloramphenicol. Source is the chloramphenicol producer Streptomyces venezuelae. http://purl.obolibrary.org/obo/ARO_3000250 ErmC http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase ErmC is a methyltransferase that catalyzes the methylation of A2058 of the 23S ribosomal RNA in two steps. Expression of ErmC is inducible by erythromycin. The leader peptide causes attenuation of the mRNA and stabilizes the structure preventing further translation. When erythromycin is present, it binds the leader peptide causing a change in conformation allowing for the expression of ErmC. http://purl.obolibrary.org/obo/ARO_3000251 msrA http://purl.obolibrary.org/obo/ARO_3004471 msr-type ABC-F protein MsrA is an ABC-F subfamily ribosomal protection protein expressed in Staphylococcus species which confers resistance to erythromycin and streptogramin B antibiotics through antibiotic target protection mechanisms. It is associated with plasmid DNA. http://purl.obolibrary.org/obo/ARO_3000253 glycopeptide resistance gene cluster VanD http://purl.obolibrary.org/obo/ARO_3000234 glycopeptide resistance gene cluster Homologous to vanA, contains a D-Ala-D-Lac ligase. This cluster is constitutively expressed in the chromosome due to a dysfunctional D-ala-D-ala ligase and confers moderate resistance to both vancomycin and teicoplanin. Gene orientation: vanRSYHDX. http://purl.obolibrary.org/obo/ARO_3000254 emrY http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance emrY is a multidrug transport that moves substrates across the inner membrane of the Gram-negative E. coli. It is a homolog of emrB. http://purl.obolibrary.org/obo/ARO_3000255 glycopeptide resistance gene cluster VanF http://purl.obolibrary.org/obo/ARO_3000234 glycopeptide resistance gene cluster Homologous to vanA, contains a D-Ala-D-Lac ligase. The vanF gene cluster is inducible and confers high resistance to vancomycin in Paenibacillus popilliae. vanF organisms remain susceptible to teicoplanin. Gene orientation: RSYZHFX. http://purl.obolibrary.org/obo/ARO_3000256 glycopeptide resistance gene cluster VanM http://purl.obolibrary.org/obo/ARO_3000234 glycopeptide resistance gene cluster Homologous to vanA, contains a D-Ala-D-Lac ligase. The plasmid-located vanM gene cluster is inducible and confers high resistance to vancomycin and teicoplanin. Gene orientation: RSYHMX. http://purl.obolibrary.org/obo/ARO_3000257 glycopeptide resistance gene cluster VanG http://purl.obolibrary.org/obo/ARO_3000234 glycopeptide resistance gene cluster Contains a D-Ala-D-Ser ligase. The vanG gene cluster is inducible and confers low resistance to vancomycin. vanG organisms remain susceptible to teicoplanin. It is the only van gene cluster that contains two vanY genes. Gene orientation: vanRSYWGYT. http://purl.obolibrary.org/obo/ARO_3000259 glycopeptide resistance gene cluster VanE http://purl.obolibrary.org/obo/ARO_3000234 glycopeptide resistance gene cluster Homologous to VanC, contains a D-Ala-D-Ser ligase. The chromosome-located vanE gene cluster is inducible and confers low resistance to vancomycin. vanE organisms remain susceptible to teicoplanin. Gene orientation: E(XY)TRS. http://purl.obolibrary.org/obo/ARO_3000260 glycopeptide resistance gene cluster VanL http://purl.obolibrary.org/obo/ARO_3000234 glycopeptide resistance gene cluster Homologous to VanC, contains a D-Ala-D-Ser ligase. The chromosome-located vanL gene cluster is inducible and confers low resistance to vancomycin. vanL organisms remain susceptible to teicoplanin. It is the only van gene cluster with two vanT genes. Gene orientation: vanL(XY)TmTrRS. http://purl.obolibrary.org/obo/ARO_3000261 sigma factor conferring resistance to rifampin http://purl.obolibrary.org/obo/ARO_3000507 rifampin-resistant RNA polymerase-binding protein When bound to different sigma factors, RNA-polymerase may possess an altered sensitivity to rifampin-mediated inhibition. Sequence data unavailable. http://purl.obolibrary.org/obo/ARO_3000262 bla operon http://purl.obolibrary.org/obo/ARO_3000231 beta-lactam resistance operon The bla operon is composed of blaZ/blaR1/blaI. http://purl.obolibrary.org/obo/ARO_3000263 marA http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux In the presence of antibiotic stress, E. coli overexpresses the global activator protein MarA, which besides inducing MDR efflux pump AcrAB, also down- regulates synthesis of the porin OmpF. http://purl.obolibrary.org/obo/ARO_3000264 emrE http://purl.obolibrary.org/obo/ARO_0010003 small multidrug resistance (SMR) antibiotic efflux pump EmrE is a small multidrug transporter that functions as a homodimer and that couples the efflux of small polyaromatic cations from the cell with the import of protons down an electrochemical gradient. EmrE is found in E. coli and P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3000265 porin OmpF http://purl.obolibrary.org/obo/ARO_3004281 General Bacterial Porin with reduced permeability to beta-lactams In the presence of antibiotic stress, E. coli overexpresses the global activator protein MarA, which besides inducing MDR efflux pump AcrAB, also down- regulates synthesis of the porin OmpF. http://purl.obolibrary.org/obo/ARO_3000266 ADP-ribosylation of antibiotic conferring resistance http://purl.obolibrary.org/obo/ARO_0001004 antibiotic inactivation The inactivation of antibiotics by the enzymatic addition of ADP-ribose from NAD+. http://purl.obolibrary.org/obo/ARO_3000268 mec operon http://purl.obolibrary.org/obo/ARO_3000231 beta-lactam resistance operon The mec operon is composed of mecA/mecR1/mecI. http://purl.obolibrary.org/obo/ARO_3000269 brodimoprim http://purl.obolibrary.org/obo/ARO_3000171 diaminopyrimidine antibiotic Brodimoprim is a structural derivative of trimethoprim and an inhibitor of bacterial dihydrofolate reductase. The 4-methoxy group of trimethoprim is replaced with a bromine atom. http://purl.obolibrary.org/obo/ARO_3000270 protein modulating permeability to antibiotic http://purl.obolibrary.org/obo/ARO_3000000 determinant of antibiotic resistance Enzymes or other proteins either directly or indirectly reducing overall permeability to antibiotics. http://purl.obolibrary.org/obo/ARO_3000273 antibiotic resistant DNA topoisomerase subunit gyrA http://purl.obolibrary.org/obo/ARO_3000370 antibiotic resistant DNA topoisomerase subunit Point mutations in gyrA confer antibiotic resistance by preventing drugs from binding the alpha-subunit of gyrase, essential for DNA supercoiling. http://purl.obolibrary.org/obo/ARO_3000274 antibiotic resistant DNA topoisomerase subunit parC http://purl.obolibrary.org/obo/ARO_3000370 antibiotic resistant DNA topoisomerase subunit Point mutations in parC confer antibiotic resistance by preventing drugs from binding the parC subunit of topoisomerase IV, essential for DNA decatanation and relaxation. http://purl.obolibrary.org/obo/ARO_3000282 sulfonamide antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule Sulfonamides are broad spectrum, synthetic antibiotics that contain the sulfonamide group. Sulfonamides inhibit dihydropteroate synthase, which catalyzes the conversion of p-aminobenzoic acid to dihydropteroic acid as part of the tetrahydrofolic acid biosynthetic pathway. Tetrahydrofolic acid is essential for folate synthesis, a precursor of many nucleotides and amino acids. Many sulfamides are taken with trimethoprim, an inhibitor of dihydrofolate reductase, also disturbing the trihydrofolic acid synthesis pathway. http://purl.obolibrary.org/obo/ARO_3000284 tetroxoprim http://purl.obolibrary.org/obo/ARO_3000171 diaminopyrimidine antibiotic Tetroxoprim is a trimethoprim derivative that inhibits bacterial dihydrofolate reductase. http://purl.obolibrary.org/obo/ARO_3000299 phosphonopyruvate decarboxylase http://purl.obolibrary.org/obo/ARO_3000082 antibiotic biosynthesis Stabilizes the C-P bond in phosphonopyruvate formed by phophoenolpyruvate mutase by catalyzing the self-removal of the carboxyl group. http://purl.obolibrary.org/obo/ARO_3000300 lsaA http://purl.obolibrary.org/obo/ARO_3004472 lsa-type ABC-F protein LsaA is an ABC-F subfamily protein expressed in Enterococcus faecalis. It confers resistance to clindamycin, quinupristin-dalfopristin, and dalfopristin. http://purl.obolibrary.org/obo/ARO_3000309 emrD http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump EmrD is a multidrug transporter from the Major Facilitator Superfamily (MFS) primarily found in Escherichia coli. EmrD couples efflux of amphipathic compounds with proton import across the plasma membrane. http://purl.obolibrary.org/obo/ARO_3000316 mphA http://purl.obolibrary.org/obo/ARO_3000333 macrolide phosphotransferase (MPH) The mphA gene encodes for resistance enzyme MPH(2')-I which preferentially inactivate 14-membered macrolides (e.g.erythromycin, telithromycin, roxithromycin) over 16-membered macrolides (e.g.tylosin, spiramycin). It phosphorylates macrolides at 2'-OH hydroxyl of desosamine sugar of macrolides in a GTP-dependent manner. http://purl.obolibrary.org/obo/ARO_3000318 mphB http://purl.obolibrary.org/obo/ARO_3000333 macrolide phosphotransferase (MPH) The mphB gene encodes for MPH(2')-II. This enzymes phosphorylates 14-membered and 16-membered macrolides. It phosphorylates macrolides in GTP- dependent manner at 2'-OH hydroxyl of desosamine sugar of macrolides. http://purl.obolibrary.org/obo/ARO_3000319 mphC http://purl.obolibrary.org/obo/ARO_3000333 macrolide phosphotransferase (MPH) The mphC gene was identified from Staphylococcus aureus. This gene shows similarity to mphB gene from Escherchia coli. http://purl.obolibrary.org/obo/ARO_3000320 macrolide esterase http://purl.obolibrary.org/obo/ARO_3000201 macrolide inactivation enzyme Hydrolytic enzymes that cleave the macrocycle lactone ring of macrolide antibiotics. http://purl.obolibrary.org/obo/ARO_3000321 hydrolysis of macrolide macrocycle lactone ring http://purl.obolibrary.org/obo/ARO_3000040 hydrolysis of antibiotic conferring resistance Hydrolysis of the the macrocycle lactone ring of macrolide antibiotics. http://purl.obolibrary.org/obo/ARO_3000322 AAC(3) http://purl.obolibrary.org/obo/ARO_3000121 aminoglycoside acetyltransferase (AAC) A category of aminoglycoside N-acetyltransferase enzymes with modification regiospecificity based at the 3-amino group of the respective antibiotic. These enzymes inactivate aminoglycoside antibiotics through acetylation of the 3-amino group of the compound. http://purl.obolibrary.org/obo/ARO_3000324 sulfadiazine http://purl.obolibrary.org/obo/ARO_3000282 sulfonamide antibiotic Sulfadiazine is a potent inhibitor of dihydropteroate synthase, interfering with the tetrahydrofolic biosynthesis pathway. Tetrahydrofolic acid is essential for folate synthesis, a precursor to many nucleotides and amino acids. http://purl.obolibrary.org/obo/ARO_3000325 sulfadimidine http://purl.obolibrary.org/obo/ARO_3000282 sulfonamide antibiotic Sulfadimidine is an alkaline sulfonamide antibiotic that inhibits dihydropteroate synthase, and enzyme in the tetrahydrofolic acid biosynthesis pathway. This interferes with the production of folate, which is a precursor to many amino acids and nucleotides. http://purl.obolibrary.org/obo/ARO_3000326 ErmE http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase ErmE is a methyltransferase found in the erythromycin producer Saccharopolyspora erythraea. Like other Erm enzymes, it catalyzes the methylation of A2058 of the 23S ribosomal RNA. The gene is found within the erythromycin biosynthetic cluster and is responsible for self-resistance. http://purl.obolibrary.org/obo/ARO_3000327 sulfadoxine http://purl.obolibrary.org/obo/ARO_3000282 sulfonamide antibiotic Sulfadoxine is an inhibitor of dihydropteroate synthase, interfering with the tetrahydrofolic biosynthesis pathway. Tetrahydrofolic acid is essential for folate synthesis, a precursor to many nucleotides and amino acids. http://purl.obolibrary.org/obo/ARO_3000328 rRNA with mutation conferring antibiotic resistance http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Single nucleotide polymorphisms (SNPs) in rRNA can confer antibiotic resistance to drugs that target the bacterial ribosome. http://purl.obolibrary.org/obo/ARO_3000329 sulfamethoxazole http://purl.obolibrary.org/obo/ARO_3000282 sulfonamide antibiotic Sulfamethoxazole is a sulfonamide antibiotic usually taken with trimethoprim, a diaminopyrimidine antibiotic. Sulfamethoxazole inhibits dihydropteroate synthase, essential to tetrahydrofolic acid biosynthesis. This pathway generates compounds used in the synthesis of many amino acids and nucleotides. http://purl.obolibrary.org/obo/ARO_3000330 sulfisoxazole http://purl.obolibrary.org/obo/ARO_3000282 sulfonamide antibiotic Sulfisoxazole is an inhibitor of dihydropteroate synthase, interfering with the tetrahydrofolic biosynthesis pathway. Tetrahydrofolic acid is essential for folate synthesis, a precursor to many nucleotides and amino acids. http://purl.obolibrary.org/obo/ARO_3000333 macrolide phosphotransferase (MPH) http://purl.obolibrary.org/obo/ARO_3000201 macrolide inactivation enzyme Macrolide phosphotransferases (MPH) are enzymes encoded by macrolide phosphotransferase genes (mph genes). These enzymes phosphorylate macrolides in GTP dependent manner at 2'-OH of desosamine sugar thereby inactivating them. Characterized MPH's are differentiated based on their substrate specificity. http://purl.obolibrary.org/obo/ARO_3000336 23S rRNA with mutation conferring antibiotic resistance http://purl.obolibrary.org/obo/ARO_3000328 rRNA with mutation conferring antibiotic resistance Point mutations in bacterial 23S rRNA from the large ribosomal subunit that confer resistance to antibiotics. Antibiotics such as linezolid block peptide synthesis through peptidyl transferase activity. Mutations in the 23S rRNA subunit reduce antibiotic binding affinity at specific sites, conferring resistance. http://purl.obolibrary.org/obo/ARO_3000337 iclaprim http://purl.obolibrary.org/obo/ARO_3000171 diaminopyrimidine antibiotic Iclaprim is a bactericidal compound that inhibits dihydrofolate reductase. It is used against clinically important Gram-positive pathogens, including methicillin-sensitive Staphylococcus aureus and methicillin-resistant S. aureus. http://purl.obolibrary.org/obo/ARO_3000338 linearization of antibiotic conferring resistance http://purl.obolibrary.org/obo/ARO_0001004 antibiotic inactivation Genes that confer antibiotic resistance by hydrolyzing bonds to linearize and deactivate antibiotics. http://purl.obolibrary.org/obo/ARO_3000341 AAC(2') http://purl.obolibrary.org/obo/ARO_3000121 aminoglycoside acetyltransferase (AAC) A category of aminoglycoside N-acetyltransferase enzymes with modification regiospecificity based at the 2'-amino group of the respective antibiotic. These enzymes inactivate aminoglycoside antibiotics through acetylation of the 2-amino group of the compound. http://purl.obolibrary.org/obo/ARO_3000342 fosfomycin inactivation enzyme http://purl.obolibrary.org/obo/ARO_3000557 antibiotic inactivation enzyme Enzymes that inactivate fosfomycin by chemical modification. http://purl.obolibrary.org/obo/ARO_3000343 tap http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump Efflux pump proteins contained within Mycobacterial genomes which confer resistance to a number of different antibiotics including aminoglycosides, and tetracyclines. http://purl.obolibrary.org/obo/ARO_3000344 EmrAB-TolC http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump EmrAB-TolC is a multidrug efflux system found in E. coli. EmrB is the electrochemical-gradient powered transporter; EmrA is the linker; and TolC is the outer membrane channel. It confers resistance to nalidixic acid and thiolactomycin. http://purl.obolibrary.org/obo/ARO_3000345 AAC(6') http://purl.obolibrary.org/obo/ARO_3000121 aminoglycoside acetyltransferase (AAC) A category of aminoglycoside N-acetyltransferase enzymes with modification regiospecificity based at the 6'-amino group of the respective antibiotic. These enzymes inactivate aminoglycoside antibiotics through acetylation of the 6-amino group of the compound. http://purl.obolibrary.org/obo/ARO_3000347 ErmA http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase ErmA confers the MLSb phenotype. Similar to ErmC, Expression of ErmA is inducible by erythromycin. The leader peptide causes attenuation of the mRNA and stabilizes the structure preventing further translation. When erythromycin is present, it binds the leader peptide causing a change in conformation allowing for the expression of ErmA. http://purl.obolibrary.org/obo/ARO_3000359 fosfomycin phosphotransferase http://purl.obolibrary.org/obo/ARO_3000342 fosfomycin inactivation enzyme In the presence of ATP and magnesium (II), fosfomycin gets phosphorylated at the phosphate group resulting in a diphosphate group which inactivates the antibiotic. http://purl.obolibrary.org/obo/ARO_3000361 EreA http://purl.obolibrary.org/obo/ARO_3000320 macrolide esterase EreA is an erythromycin esterase that hydrolyses the drug's lactone ring. http://purl.obolibrary.org/obo/ARO_3000363 EreB http://purl.obolibrary.org/obo/ARO_3000320 macrolide esterase EreB is an erythromycin esterase-like protein that hydrolyses the drug's lactone ring. http://purl.obolibrary.org/obo/ARO_3000368 vanC http://purl.obolibrary.org/obo/ARO_3002979 D-Ala-D-Ser ligase VanC is a D-Ala-D-Ala ligase homolog that synthesizes D-Ala-D-Ser, an alternative substrate for peptidoglycan synthesis that reduces vancomycin binding affinity. It is specific to Enterococcus gallinarum and E. casseliflavus, providing intrinsic resistance. http://purl.obolibrary.org/obo/ARO_3000369 MtrCDE http://purl.obolibrary.org/obo/ARO_0010004 resistance-nodulation-cell division (RND) antibiotic efflux pump The mtr (multiple transferable resistance) system of Neisseria gonorrhoeae confers resistance to many hydrophobic agents including antibiotics, fatty-acids and detergents. MtrCDE is homologous to AcrAB-TolC, where MtrC is the membrane fusion protein, MtrD is the inner membrane transporter, and MtrE is the outer membrane channel protein. http://purl.obolibrary.org/obo/ARO_3000370 antibiotic resistant DNA topoisomerase subunit http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Many drugs target topoisomerases to inhibit DNA synthesis. Resistant DNA topoisomerase subunits prevent antibiotic binding and thus confer resistance. http://purl.obolibrary.org/obo/ARO_3000372 vanT http://purl.obolibrary.org/obo/ARO_3002976 gene(s) or protein(s) associated with a glycopeptide resistance cluster VanT is a membrane bound serine racemase, converting L-serine to D-serine. It is associated with VanC, which incorporated D-serine into D-Ala-D-Ser terminal end of peptidoglycan subunits that have a decreased binding affinity with vancomycin. It was isolated from Enterococcus gallinarum. http://purl.obolibrary.org/obo/ARO_3000373 EmrKY-TolC http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump EmrKY is a homolog of EmrAB found in E. coli. Together with TolC, it is a tripartite multidrug transporter. http://purl.obolibrary.org/obo/ARO_3000375 ErmB http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase ErmB confers the MLSb phenotype. Similar to ErmC, expression of ErmB is inducible by erythromycin. The leader peptide causes attenuation of the mRNA and stabilizes the structure preventing further translation. When erythromycin is present, it binds the leader peptide causing a change in conformation allowing for the expression of ErmB. http://purl.obolibrary.org/obo/ARO_3000376 streptogramin vgb lyase http://purl.obolibrary.org/obo/ARO_3000233 streptogramin inactivation enzyme vgb (Virginiamycin B) lyase inactivates type B streptogramin antibiotics by linearizing the streptogramin lactone ring at the ester linkage through an elimination mechanism, thus conferring resistance to these compounds. http://purl.obolibrary.org/obo/ARO_3000377 MexA http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MexA is the membrane fusion protein of the MexAB-OprM multidrug efflux complex. http://purl.obolibrary.org/obo/ARO_3000378 MexB http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MexB is the inner membrane multidrug exporter of the efflux complex MexAB-OprM. http://purl.obolibrary.org/obo/ARO_3000379 OprM http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance OprM is an outer membrane factor protein found in Pseudomonas aeruginosa and Burkholderia vietnamiensis. It is part of the MexAB-OprM, MexVW-OprM, MexXY-OprM and the AmrAB-OprM complex. http://purl.obolibrary.org/obo/ARO_3000380 FosC http://purl.obolibrary.org/obo/ARO_3004245 fosC phosphotransferase family FosC is an enzyme that phosphorylates fosfomycin to confer resistance. http://purl.obolibrary.org/obo/ARO_3000381 antibiotic target replacement protein http://purl.obolibrary.org/obo/ARO_3000000 determinant of antibiotic resistance Alternate proteins that have the same functions as other antibiotic target proteins, but are structurally different and thus resistant to antibiotics. These can replace the activity of other antibiotic-sensitive proteins in the presence of antibiotics. http://purl.obolibrary.org/obo/ARO_3000382 azidamfenicol http://purl.obolibrary.org/obo/ARO_3000387 phenicol antibiotic Azidamfenicol is a water soluble derivative of chloramphenicol, sharing the same mode of action of inhibiting peptide synthesis by interacting with the 23S RNA of the 50S ribosomal subunit. http://purl.obolibrary.org/obo/ARO_3000384 AcrAB-TolC http://purl.obolibrary.org/obo/ARO_0010004 resistance-nodulation-cell division (RND) antibiotic efflux pump AcrAB-TolC is a tripartite RND efflux system that confers resistance to tetracycline, chloramphenicol, ampicillin, nalidixic acid, and rifampin in Gram-negative bacteria. The system spans the cell membrane (AcrB) and the outer-membrane (TolC), and is linked together in the periplasm by AcrA. http://purl.obolibrary.org/obo/ARO_3000385 chloramphenicol http://purl.obolibrary.org/obo/ARO_3000387 phenicol antibiotic Chloramphenicol is a bacteriostatic antimicrobial originally derived from the bacterium Streptomyces venezuelae. It was the first antibiotic to be manufactured synthetically on a large scale. It functions by inhibiting peptidyl transferase activity of the bacterial ribosome, binding to A2451 and A2452 residues in the 23S rRNA of the 50S ribosomal subunit and preventing peptide bond formation. http://purl.obolibrary.org/obo/ARO_3000386 MexAB-OprM http://purl.obolibrary.org/obo/ARO_0010004 resistance-nodulation-cell division (RND) antibiotic efflux pump MexAB-OprM is a multidrug efflux protein expressed in the Gram-negative Pseudomonas aeruginosa. MexA is the membrane fusion protein; MexB is the inner membrane transporter; and OprM is the outer membrane channel. MexAB-OprM is associated with resistance to fluoroquinolones, chloramphenicol, erythromycin, azithromycin, novobiocin, and certain β-lactams and lastly over-expression is linked to colistin resistance. http://purl.obolibrary.org/obo/ARO_3000387 phenicol antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule Phenicols are broad spectrum bacteriostatic antibiotics acting on bacterial protein synthesis. More specifically, the phenicols block peptide elongation by binding to the peptidyltansferase centre of the 70S ribosome. http://purl.obolibrary.org/obo/ARO_3000388 streptogramin biosynthesis http://purl.obolibrary.org/obo/ARO_3000082 antibiotic biosynthesis Biosynthesis of streptoramin antibiotics. http://purl.obolibrary.org/obo/ARO_3000389 streptogramin B biosynthesis http://purl.obolibrary.org/obo/ARO_3000388 streptogramin biosynthesis Type B streptogramins are cyclic hexa- or hepta-depsipeptides produced by NRPSs in Streptomyces. The NRPS contains 6 or 7 modules arranged on one or more genes. SnbA catalyzes the activation of the first residue, 3-hydroxypicolynic acid. SnbC then activates and incorporates threonine and aminobutyric acid. Lastly, SnbDE activates and incoporates the last four amino acids. The thioesterase domain is responsible for peptide cyclization, and it is located at the end of the assembly line. http://purl.obolibrary.org/obo/ARO_3000390 rifampin ADP-ribosyltransferase (Arr) http://purl.obolibrary.org/obo/ARO_3000576 rifampin inactivation enzyme Enzyme responsible for the ADP-ribosylative inactivation of rifampin at the 23-OH position using NAD+. http://purl.obolibrary.org/obo/ARO_3000391 norA http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump NorA is a multidrug efflux pump in Staphylococcus aureus that confers resistance to fluoroquinolones and other structurally unrelated antibiotics like acriflavine. It shares 30% similarity with NorA, and is a structural homolog of Bmr of Bacillus subtilis. It is regulated by arlRS and mgrA, the latter also known as NorR. http://purl.obolibrary.org/obo/ARO_3000392 Erm(37) http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase Erm(37) is found in Mycobacterium species and confers the MLSb phenotype. In addition to methylation of A2058 this Erm methylates adjacent adenosines (A2057 and A2059) as well. http://purl.obolibrary.org/obo/ARO_3000393 glycopeptide biosynthesis http://purl.obolibrary.org/obo/ARO_3000082 antibiotic biosynthesis Synthesis of glycopeptide antibiotics. http://purl.obolibrary.org/obo/ARO_3000394 Actinoplanes teichomyceticus teicoplanin gene cluster http://purl.obolibrary.org/obo/ARO_3000393 glycopeptide biosynthesis Biosynthesis of teicoplanin by Actinoplanes teichomyceticus. http://purl.obolibrary.org/obo/ARO_3000410 sul1 http://purl.obolibrary.org/obo/ARO_3004238 sulfonamide resistant sul Sul1 is a sulfonamide resistant dihydropteroate synthase of Gram-negative bacteria. It is linked to other resistance genes of class 1 integrons. http://purl.obolibrary.org/obo/ARO_3000412 sul2 http://purl.obolibrary.org/obo/ARO_3004238 sulfonamide resistant sul Sul2 is a sulfonamide resistant dihydropteroate synthase of Gram-negative bacteria, usually found on small plasmids. http://purl.obolibrary.org/obo/ARO_3000413 sul3 http://purl.obolibrary.org/obo/ARO_3004238 sulfonamide resistant sul Sul3 is a sulfonamide resistant dihydropteroate synthase similar to Sul1 and Sul2. Its resistance gene was found encoded in E. coli plasmid DNA of sulfonamide resistant isolates. http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) http://purl.obolibrary.org/obo/ARO_3000185 antibiotic target protection protein Qnr proteins are pentapeptide repeat proteins that mimic DNA and protect the cell from the activity of fluoroquinolone antibiotics. http://purl.obolibrary.org/obo/ARO_3000421 norB http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump NorB is a multidrug efflux pump in Staphylococcus aureus that confers resistance to fluoroquinolones and other structurally unrelated antibiotics like tetracycline. It shares 30% similarity with NorB, and is a structural homolog of Blt of Bacillus subtilis. It is regulated by mgrA, also known as NorR. http://purl.obolibrary.org/obo/ARO_3000423 FomA http://purl.obolibrary.org/obo/ARO_3004246 Fom phosphotransferase family In the presence of ATP and magnesium (II), fosfomycin gets phosphorylated at the phosphate group resulting in a diphosphate group which inactivates the antibiotic. http://purl.obolibrary.org/obo/ARO_3000443 rifampin glycosyltransferase http://purl.obolibrary.org/obo/ARO_3000576 rifampin inactivation enzyme The enzymatic inactivation of rifampin by glycosylation at the 23-OH position. http://purl.obolibrary.org/obo/ARO_3000444 rphA http://purl.obolibrary.org/obo/ARO_3004040 rifampin phosphotransferase The enzymatic inactivation of rifampin by phosphorylation at the 21-OH position. http://purl.obolibrary.org/obo/ARO_3000445 rifampin monooxygenase http://purl.obolibrary.org/obo/ARO_3000576 rifampin inactivation enzyme Enzyme responsible for the decolorization of rifampin by monoxygenation. http://purl.obolibrary.org/obo/ARO_3000446 antibiotic-resistant isoleucyl-tRNA synthetase (ileS) http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mupirocin inhibits protein synthesis by interfering with isoleucyl-tRNA synthetase (ileS). Mutations in ileS can confer low-level mupirocin resistance. http://purl.obolibrary.org/obo/ARO_3000448 QepA1 http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump QepA1 is a plasmid-mediated efflux pump in E. coli, shown to contribute to fluoroquinolone resistance. It is regulated by sox genes, also known as global stress regulators. http://purl.obolibrary.org/obo/ARO_3000449 FomB http://purl.obolibrary.org/obo/ARO_3004246 Fom phosphotransferase family An enzyme which on its own cannot provide fosfomycin resistance, however in conjunction with FomA, it leads to the formation of fosfomycin with three phosphates total, which makes it inactive. http://purl.obolibrary.org/obo/ARO_3000450 hydroxylation of antibiotic conferring resistance http://purl.obolibrary.org/obo/ARO_0001004 antibiotic inactivation Inactivation of an antibiotic via introduction a hydroxyl group (-OH). http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux http://purl.obolibrary.org/obo/ARO_3000000 determinant of antibiotic resistance Protein(s) and two component regulatory systems that directly or indirectly change rates of antibiotic efflux. http://purl.obolibrary.org/obo/ARO_3000452 fluoroquinolone resistant DNA topoisomerase http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Fluoroquinolones inhibit type II and type IV topoisomerases (2 strand breaking enzymes) such as GyrA/GyrB and ParC/ParE. Point mutations in the associated gyrA and parC genes, in particular in the 'quinolone resistance determining region' (QRDR), give rise to resistance to the class. http://purl.obolibrary.org/obo/ARO_3000453 streptogramin vat acetyltransferase http://purl.obolibrary.org/obo/ARO_3000233 streptogramin inactivation enzyme vat (Virginiamycin acetyltransferases) enzymes catalyze the transfer of an acetyl group from acetyl-CoA to the secondary alcohol of streptogramin A compounds, thus inactivating virginiamycin-like antibiotics and conferring resistance to these compounds. http://purl.obolibrary.org/obo/ARO_3000454 polymyxin B http://purl.obolibrary.org/obo/ARO_3000707 antibiotic mixture Polymyxin B is mixture of mostly polymyxins B1 and B2, mainly used for resistant gram-negative infections. They are polypeptides with cationic detergent action on cell membranes. http://purl.obolibrary.org/obo/ARO_3000455 streptogramin A biosynthesis http://purl.obolibrary.org/obo/ARO_3000388 streptogramin biosynthesis Type A streptogramins are produced by a hybrid NRPS/PKS composed of 8 NRPS modules and 2 PKS modules. http://purl.obolibrary.org/obo/ARO_3000456 thiamphenicol http://purl.obolibrary.org/obo/ARO_3000387 phenicol antibiotic Derivative of Chloramphenicol. The nitro group (-NO2) is substituted by a sulfomethyl group (-SO2CH3). http://purl.obolibrary.org/obo/ARO_3000457 aminocoumarin resistant parE http://purl.obolibrary.org/obo/ARO_3000115 antibiotic resistant DNA topoisomerase subunit parE ParE is a subunit of topoisomerase IV, which decatenates and relaxes DNA to allow access to genes for transcription or translation. Point mutations in ParE prevent anticoumarin antibiotics from inhibiting DNA synthesis, thus conferring resistance. http://purl.obolibrary.org/obo/ARO_3000458 macrolide glycosyltransferase http://purl.obolibrary.org/obo/ARO_3000201 macrolide inactivation enzyme Macrolide glycosyltransferases are enzymes encoded by macrolide glycosyltransferase genes and inactivate macrolides by glycosylating them at 2'-OH of desosamine sugar moiety. They are predominantly found in macrolide producers and are also found in non-producers and are used as a resistance mechanism. Different variants of this enzyme has been reported. http://purl.obolibrary.org/obo/ARO_3000459 fosfomycin biosynthesis http://purl.obolibrary.org/obo/ARO_3000082 antibiotic biosynthesis Biosynthesis of fosfomycin. http://purl.obolibrary.org/obo/ARO_3000461 florfenicol http://purl.obolibrary.org/obo/ARO_3000387 phenicol antibiotic Florfenicol is a fluorine derivative of chloramphenicol, where the nitro group (-NO2) is substituted by a sulfomethyl group (-SO2CH3) and the hydroxyl group (-OH), by a fluorine group (-F). The action mechanism is the same as chloramphenicol's, where the antibiotic binds to the 23S RNA of the 50S subunit of bacterial ribosomes to inhibit protein synthesis. http://purl.obolibrary.org/obo/ARO_3000462 mgtA http://purl.obolibrary.org/obo/ARO_3004237 mgt macrolide glycotransferase A macrolide glycosyltransferase encoded by the mgtA gene in Streptomyces lividans. This enzyme inactivates macrolides using UDP-glucose as a cofactor. Its optimal substrates are lankamycin, calcomycin, rosaramicin, methymycin, and pikromycin, while interactions with erythomycin, oldeandomycin, azithromycin, and tylosin were weaker. It is inactive against spiramycin and carbomycin. Mechanism first described by Cundliffe, 1992. http://purl.obolibrary.org/obo/ARO_3000463 gimA http://purl.obolibrary.org/obo/ARO_3004236 gimA family macrolide glycosyltransferase A macrolide glycosyltransferase encoded by the gimA gene in Streptomyces ambofaciens, a natural producer of the macrolide antibiotic spiramycin. Chalcomycin, methymycin, tylosin, pikromycin, rosaramicin, oleandomycin, josamycin, and carbomycin are preferred substrates of gimA glycosyltransferase, while erythromycin and spiramycin have notably low binding affinities. GimA may be able to inactivate spiramycin precursors. Described by Gourmelen et al. 1998. http://purl.obolibrary.org/obo/ARO_3000464 Neisseria gonorrhoeae porin PIB (por) http://purl.obolibrary.org/obo/ARO_3004281 General Bacterial Porin with reduced permeability to beta-lactams Mutant forms of the porin Por result in reduced permeability to antibiotics, particularly tetracyclines and beta-lactams. http://purl.obolibrary.org/obo/ARO_3000465 ole glycosyltransferase http://purl.obolibrary.org/obo/ARO_3000458 macrolide glycosyltransferase OleI and OleD are glycosyltransferases found in Streptomyces antibioticus which is a natural producer of antibiotic oleandomycin. OleI glycosylates antibiotic oleandomycin whereas OleD can glycosylate a wide variety of macrolides. http://purl.obolibrary.org/obo/ARO_3000466 dalbavancin http://purl.obolibrary.org/obo/ARO_3000081 glycopeptide antibiotic Dalbavancin is a semisynthetic second-generation lipoglycopeptide derived from teicoplanin. It binds to the D-Ala-D-Ala terminus of peptidoglycan precursors. It is used to treat Gram-positive bacteria and can be used to treat methicillin-resistant Staphylococcus aureus and vancomycin-resistant enterococci. http://purl.obolibrary.org/obo/ARO_3000467 NDM-5 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase New Delhi beta-lactamase NDM-5. http://purl.obolibrary.org/obo/ARO_3000469 hydroxypropylphosphonic acid epoxidase http://purl.obolibrary.org/obo/ARO_3000459 fosfomycin biosynthesis The enzyme responsible for the final step of fosfomycin biosynthesis. It converts S-2-hydroxypropylphosphonic acid (S-HPP) into fosfomycin via an oxidative cyclalization reaction. It uses Iron (II) or Zinc (II) as cofactors. http://purl.obolibrary.org/obo/ARO_3000476 tet(31) http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump Tet31 is a tetracycline efflux pump found in Aeromonas salmonicida, a Gram-negative bacteria. It has also been shown to be expressed in Gallibacterium anatis. http://purl.obolibrary.org/obo/ARO_3000478 tet(33) http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump Tet33 is a tetracycline efflux pump found in Gram-positive bacteria, including Arthrobacter and Corynebacterium. http://purl.obolibrary.org/obo/ARO_3000479 aminocoumarin resistant gyrB http://purl.obolibrary.org/obo/ARO_3000220 antibiotic resistant DNA topoisomerase subunit gyrB Point mutations in DNA gyrase subunit B (gyrB) can result in resistance to aminocoumarins. These mutations usually involve arginine residues in organisms. http://purl.obolibrary.org/obo/ARO_3000480 aminocoumarin resistant parY http://purl.obolibrary.org/obo/ARO_3000209 antibiotic resistant DNA topoisomerase subunit parY Expression of parY(R), which encodes an aminocoumarin resistant topoisomerase IV, can confer aminocoumarin resistance. http://purl.obolibrary.org/obo/ARO_3000481 tet(35) http://purl.obolibrary.org/obo/ARO_0010001 ATP-binding cassette (ABC) antibiotic efflux pump Tet35 is a tetracycline efflux pump found in the Gram-negative Vibrio and Stenotrophomonas. It is unrelated to other tet resistance genes. http://purl.obolibrary.org/obo/ARO_3000488 telavancin http://purl.obolibrary.org/obo/ARO_3000081 glycopeptide antibiotic Telavancin is a semi-synthetic derivative of vancomycin and is a second-generation lipoglycopeptide antibiotic. Telavancin inhibits cell wall synthesis by forming a complex with the D-Ala-D-Ala terminus of peptidoglycan precursors and preventing transglycosylation. http://purl.obolibrary.org/obo/ARO_3000489 sav1866 http://purl.obolibrary.org/obo/ARO_0010001 ATP-binding cassette (ABC) antibiotic efflux pump Sav1866 is a multidrug efflux pump in the Gram-positive Staphylococcus aureus. It is a homolog of the human ABC transporter Mdr1 and pumps out toxic compounds including verapamil, tetraphenylphosphorchloride, and Hoechst 33342. http://purl.obolibrary.org/obo/ARO_3000490 tuberactinomycin http://purl.obolibrary.org/obo/ARO_3000053 peptide antibiotic Tuberactinomycins are a family of cyclic peptide antibiotics that are important in the treatment of tuberculosis. Tuberactinomycins contain nonproteinogenic amino acids and inhibit group I self-splicing RNA to disrupt prokaryotic protein synthesis. http://purl.obolibrary.org/obo/ARO_3000491 acrD http://purl.obolibrary.org/obo/ARO_0010004 resistance-nodulation-cell division (RND) antibiotic efflux pump AcrD is an aminoglycoside efflux pump expressed in E. coli. Its expression can be induced by indole, and is regulated by baeRS and cpxAR. http://purl.obolibrary.org/obo/ARO_3000492 gene involved in self-resistance to antibiotic http://purl.obolibrary.org/obo/ARO_3000000 determinant of antibiotic resistance Genes that are involved in conferring self resistance to antibiotic. http://purl.obolibrary.org/obo/ARO_3000495 ErmD http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase ErmD confers MLSb phenotype. http://purl.obolibrary.org/obo/ARO_3000496 vanXY http://purl.obolibrary.org/obo/ARO_3002976 gene(s) or protein(s) associated with a glycopeptide resistance cluster VanXY is a protein with both D,D-carboxypeptidase and D,D-dipeptidase activity, found in Enterococcus gallinarum. It cleaves and removes the terminal D-Ala of peptidoglycan subunits for the incorporation of D-Ser by VanC. D-Ala-D-Ser has low binding affinity with vancomycin. http://purl.obolibrary.org/obo/ARO_3000497 ethambutol http://purl.obolibrary.org/obo/ARO_3000527 polyamine antibiotic Ethambutol is an antimycobacterial drug prescribed to treat tuberculosis. It is usually given in combination with other tuberculosis drugs, such as isoniazid, rifampicin, and pyrazinamide. Ethambutol inhibits arabinosyl biosynthesis, disrupting mycobacterial cell wall formation. http://purl.obolibrary.org/obo/ARO_3000498 ErmF http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase ErmF confers the MLSb phenotype. http://purl.obolibrary.org/obo/ARO_3000499 AcrE http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance AcrE is a membrane fusion protein, similar to AcrA. http://purl.obolibrary.org/obo/ARO_3000500 phosphonoacetaldehyde methyltransfererase http://purl.obolibrary.org/obo/ARO_3000082 antibiotic biosynthesis The enzyme responsible for converting phosphonoacetaldehyde to (S)-2-/nhydroxypropylphosphonic acid (S-HPP) via an anionic methyl attack, which also reduces the aldehyde to an alcohol. http://purl.obolibrary.org/obo/ARO_3000501 rpoB2 http://purl.obolibrary.org/obo/ARO_3000210 rifamycin-resistant beta-subunit of RNA polymerase (rpoB) Due to gene duplication, the genomes of Nocardia species include both rifampin-sensitive beta-subunit of RNA polymerase (rpoB) and rifampin-resistant beta-subunit of RNA polymerase (rpoB2) genes, with ~88% similarity between the two gene products. Expression of the rpoB2 variant results in replacement of rifampin sensitivity with rifampin resistance. http://purl.obolibrary.org/obo/ARO_3000502 AcrF http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance AcrF is a inner membrane transporter, similar to AcrB. http://purl.obolibrary.org/obo/ARO_3000503 AcrEF-TolC http://purl.obolibrary.org/obo/ARO_0010004 resistance-nodulation-cell division (RND) antibiotic efflux pump AcrEF-TolC is a tripartite multidrug efflux system similar to AcrAB-TolC and found in Gram-negative bacteria. AcrE is the membrane fusion protein, AcrF is the inner membrane transporter, and TolC is the outer membrane channel protein. http://purl.obolibrary.org/obo/ARO_3000504 golS http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux GolS is a regulator activated by the presence of golD, and promotes the expression of the MdsABC efflux pump. http://purl.obolibrary.org/obo/ARO_3000506 MexR http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux MexR is the repressor of the MexRAB-OprM operon. Mutant forms of mexR result in up-regulation of efflux pump system MexAB-OprM. http://purl.obolibrary.org/obo/ARO_3000507 rifampin-resistant RNA polymerase-binding protein http://purl.obolibrary.org/obo/ARO_3000185 antibiotic target protection protein Proteins which have been experimentally shown to protect RNA-polymerase from rifampin inhibition. http://purl.obolibrary.org/obo/ARO_3000508 gadX http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux GadX is an AraC-family regulator that promotes mdtEF expression to confer multidrug resistance. http://purl.obolibrary.org/obo/ARO_3000510 Staphylococcus aureus mupB conferring resistance to mupirocin http://purl.obolibrary.org/obo/ARO_3000446 antibiotic-resistant isoleucyl-tRNA synthetase (ileS) An alternative isoleucyl-tRNA synthetase conferring resistance to mupirocin. http://purl.obolibrary.org/obo/ARO_3000515 evgSA http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux EvgSA is a two-component regulatory system that regulates MdtEF and EmrKY expression for multidrug resistance. EvgS is a sensor protein that phosphorylates the regulatory protein EvgA, though EvgA can be phosphorylated by other methods when it is overexpressed. http://purl.obolibrary.org/obo/ARO_3000516 emrR http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux EmrR is a negative regulator for the EmrAB-TolC multidrug efflux pump in E. coli. Mutations lead to EmrAB-TolC overexpression. http://purl.obolibrary.org/obo/ARO_3000517 rifaximin http://purl.obolibrary.org/obo/ARO_3000157 rifamycin antibiotic Rifaximin is a semi-synthetic rifamycin used to treat traveller's diarrhea. Rifaximin inhibits RNA synthesis by binding to the beta subunit of bacterial RNA polymerase. http://purl.obolibrary.org/obo/ARO_3000518 CRP http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux CRP is a global regulator that represses MdtEF multidrug efflux pump expression. http://purl.obolibrary.org/obo/ARO_3000519 antibiotic target modifying enzyme http://purl.obolibrary.org/obo/ARO_3000000 determinant of antibiotic resistance Enzymes that confer resistance by modifying antibiotic targets. http://purl.obolibrary.org/obo/ARO_3000520 isoniazid http://purl.obolibrary.org/obo/ARO_3007152 isoniazid-like antibiotic Isoniazid is an organic compound that is the first-line anti tuberculosis medication in prevention and treatment. As a prodrug, it is activated by mycobacterial catalase-peroxidases such as M. tuberculosis KatG. Isoniazid inhibits mycolic acid synthesis, which prevents cell wall synthesis in mycobacteria. http://purl.obolibrary.org/obo/ARO_3000521 Staphylococcus aureus mupA conferring resistance to mupirocin http://purl.obolibrary.org/obo/ARO_3000446 antibiotic-resistant isoleucyl-tRNA synthetase (ileS) An alternative isoleucyl-tRNA synthetase conferring resistance to mupirocin. http://purl.obolibrary.org/obo/ARO_3000522 ErmG http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase ErmG is a rRNA adenine N-6-methyltransferase that protects the ribosome from inactivation due to antibiotic binding. http://purl.obolibrary.org/obo/ARO_3000524 cpxAR http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux CpxAR is a two-component regulatory system that involves a sensor kinase, CpxA, and the regulator CpxR. When the membrane envelope is stressed, CpxAR promotes acrD and mdtABC expression to confer multidrug resistance through efflux. http://purl.obolibrary.org/obo/ARO_3000525 antibiotic A40926 http://purl.obolibrary.org/obo/ARO_3000081 glycopeptide antibiotic A40926 is a glycopeptide antibiotic produced by Nonomuraea sp. ATCC 39727. It is precusor of the second-generation glycopeptide antibiotic dalbavancin. http://purl.obolibrary.org/obo/ARO_3000526 cmeR http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux CmeR is a repressor for the CmeABC multidrug efflux pump, binding to the cmeABC promoter region. http://purl.obolibrary.org/obo/ARO_3000527 polyamine antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule Polyamine antibiotics are organic compounds having two or more primary amino groups. http://purl.obolibrary.org/obo/ARO_3000528 chlortetracycline http://purl.obolibrary.org/obo/ARO_3000050 tetracycline antibiotic Chlortetracycline was an early, first-generation tetracycline antibiotic developed in the 1940's. It inhibits bacterial protein synthesis by binding to the 30S subunit of bacterial ribosomes, preventing the aminoacyl-tRNA from binding to the ribosome. http://purl.obolibrary.org/obo/ARO_3000530 rifabutin http://purl.obolibrary.org/obo/ARO_3000157 rifamycin antibiotic Rifabutin is a semisynthetic rifamycin used in tuberculosis therapy. It inhibits DNA-dependent RNA synthesis. http://purl.obolibrary.org/obo/ARO_3000531 baeSR http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux BaeSR is a two component regulatory system for efflux proteins in Gram-negative bacteria. BaeR is a response regulator, while BaeS is a sensor kinase. http://purl.obolibrary.org/obo/ARO_3000532 aminocoumarin biosynthesis http://purl.obolibrary.org/obo/ARO_3000082 antibiotic biosynthesis Biosynthesis of aminocoumarin antibiotics. http://purl.obolibrary.org/obo/ARO_3000533 macA http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MacA is a membrane fusion protein that forms an antibiotic efflux complex with MacB and TolC. macA corresponds to 1 locus in Pseudomonas aeruginosa PAO1 and 1 locus in Pseudomonas aeruginosa LESB58. http://purl.obolibrary.org/obo/ARO_3000534 rifapentine http://purl.obolibrary.org/obo/ARO_3000157 rifamycin antibiotic Rifapentine is a semisynthetic rifamycin that inhibits DNA-dependent RNA synthesis. It is often used in the treatment of tuberculosis and leprosy. http://purl.obolibrary.org/obo/ARO_3000535 macB http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MacB is an ATP-binding cassette (ABC) transporter that exports macrolides with 14- or 15- membered lactones. It forms an antibiotic efflux complex with MacA and TolC. macB corresponds to 1 locus in Pseudomonas aeruginosa PAO1 and 1 locus in Pseudomonas aeruginosa LESB58. http://purl.obolibrary.org/obo/ARO_3000536 Streptomyces spheroides novobiocin biosynthetic gene cluster http://purl.obolibrary.org/obo/ARO_3000532 aminocoumarin biosynthesis Novobiocin is produced from biosynthetic clusters in Streptomyces spheroides and Streptomyces niveus. http://purl.obolibrary.org/obo/ARO_3000545 MacAB-TolC http://purl.obolibrary.org/obo/ARO_0010001 ATP-binding cassette (ABC) antibiotic efflux pump MacAB-TolC is an ABC efflux pump complex expressed in E. coli and Salmonella enterica. It confers resistance to macrolides, including erythromycin. http://purl.obolibrary.org/obo/ARO_3000546 Streptomyces roseochromogenus subsp. oscitans clorobiocin biosynthetic gene cluster http://purl.obolibrary.org/obo/ARO_3000532 aminocoumarin biosynthesis Clorobiocin is produced by a biosynthetic cluster in Streptomyces roseochromogenus subsp. oscitans. http://purl.obolibrary.org/obo/ARO_3000547 arlRS http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux ArlRS is a two-component regulatory system for NorA. ArlS phosphorylates ArlR to promote NorA expression. http://purl.obolibrary.org/obo/ARO_3000548 Streptomyces rishiriensis strain DSM 40489 coumermycin A1 biosynthetic gene cluster http://purl.obolibrary.org/obo/ARO_3000532 aminocoumarin biosynthesis Coumermycin A1 is produced by a biosynthetic cluster in Streptomyces rishiriensis. http://purl.obolibrary.org/obo/ARO_3000549 adeS http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux AdeS is a sensor kinase in the AdeRS regulatory system of AdeABC. It is essential for AdeABC expression. http://purl.obolibrary.org/obo/ARO_3000550 aztreonam http://purl.obolibrary.org/obo/ARO_0000004 monobactam Aztreonam was the first monobactam discovered, and is greatly effective against Gram-negative bacteria while inactive against Gram-positive bacteria. Artreonam is a poor substrate for beta-lactamases, and may even act as an inhibitor. In Gram-negative bacteria, Aztreonam interferes with filamentation, inhibiting cell division and leading to cell death. http://purl.obolibrary.org/obo/ARO_3000551 organoarsenic antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule Organoarsenic antibiotics are arsenic-containing compounds with antibacterial effects. The organoarsenic antibiotic arsphenamine and its derivatives were developed in the 1910s as the first modern chemotherapeutic agents. http://purl.obolibrary.org/obo/ARO_3000552 arsphenamine http://purl.obolibrary.org/obo/ARO_3000551 organoarsenic antibiotic Arsphenamine, also known as Salvarsan and 606, is a drug that was used beginning in the 1910s to treat syphilis and trypanosomiasis. It is an organoarsenic compound and was the first modern chemotherapeutic agent. http://purl.obolibrary.org/obo/ARO_3000553 adeR http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux AdeR is a positive regulator of AdeABC efflux system. AdeR inactivation leads to susceptibility to aminoglycoside antibiotics. http://purl.obolibrary.org/obo/ARO_3000554 mupirocin http://purl.obolibrary.org/obo/ARO_3007151 mupirocin-like antibiotic Mupirocin, also known as pseudomonic acid, is a bacteriostatic polyketide antibiotic from Pseudomonas fluorescens used to treat S. aureus and MRSA. It inhibits Ile tRNA synthetase. http://purl.obolibrary.org/obo/ARO_3000555 macrolide biosynthesis http://purl.obolibrary.org/obo/ARO_3000082 antibiotic biosynthesis Biosynthesis of macrolide antibiotics. http://purl.obolibrary.org/obo/ARO_3000556 tet(44) http://purl.obolibrary.org/obo/ARO_0000002 tetracycline-resistant ribosomal protection protein Tet44 is a tetracycline resistance gene found in Campylobacter fetus, and binds to the ribosome to confer antibiotic resistance as a ribosomal protection protein. http://purl.obolibrary.org/obo/ARO_3000557 antibiotic inactivation enzyme http://purl.obolibrary.org/obo/ARO_3000000 determinant of antibiotic resistance Enzyme that catalyzes the inactivation of an antibiotic resulting in resistance. Inactivation includes chemical modification, destruction, etc. http://purl.obolibrary.org/obo/ARO_3000559 adeN http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux AdeN is a repressor of AdeIJK, a RND-type efflux pump in Acinetobacter baumannii. Its inactivation increases expression of AdeJ. http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase http://purl.obolibrary.org/obo/ARO_3004274 23S ribosomal RNA methyltransferase Erm proteins are part of the RNA methyltransferase family and methylate A2058 (E. coli nomenclature) of the 23S ribosomal RNA conferring degrees of resistance to Macrolides, Lincosamides and Streptogramin b. This is called the MLSb phenotype. http://purl.obolibrary.org/obo/ARO_3000561 tet(30) http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump Tet30 is a tetracycline efflux pump found in agrobacterium, a Gram-negative bacterium. http://purl.obolibrary.org/obo/ARO_3000565 tet(38) http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump Tet38 is a tetracycline efflux pump found in the Gram-positive Staphylococcus aureus. It is regulated by mgrA, which also regulates NorB. http://purl.obolibrary.org/obo/ARO_3000566 tet(39) http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump Tet39 is a tetracycline efflux pump found in Gram-negative bacteria, including Brevundimonas, Stenotrophomonas, Enterobacter, Alcaligenes, Acinetobacter, and Providencia. http://purl.obolibrary.org/obo/ARO_3000567 tet(40) http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump Tet40 is a tetracycline efflux pump found in the Gram-positive Clostridium. It is similar to tetA(P). http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase http://purl.obolibrary.org/obo/ARO_3000004 class B (metallo-) beta-lactamase Subclass B1 possess a binuclear active site. Within this active site can be either one or two Zn(II) ions. This subclass is able to hydrolyze penicillins, cephalosporins and carbapenems. This is the most clinically relevant subclass of MBLs. http://purl.obolibrary.org/obo/ARO_3000569 tet(41) http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump Tet41 is a tetracycline efflux pump found in Serratia, a Gram-negative bacterium. It is related to Acinetobacter Tet(39). http://purl.obolibrary.org/obo/ARO_3000570 subclass B2 (metallo-) beta-lactamase http://purl.obolibrary.org/obo/ARO_3000004 class B (metallo-) beta-lactamase Metallo-beta-lactmases of subclass B2 contain only one Zn ion in their active site and selectively hydrolyze carbapenems. http://purl.obolibrary.org/obo/ARO_3000571 subclass B3 (metallo-) beta-lactamase http://purl.obolibrary.org/obo/ARO_3000004 class B (metallo-) beta-lactamase Metallo-beta-lactamases of subclass B3 are similar to B1 in that they have activity against penicillins, cephalosporins and carbapenems; however, the are only active with two Zn(II) ions in the active site. http://purl.obolibrary.org/obo/ARO_3000572 tet(42) http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump Tet42 is a tetracycline efflux pump found in both Gram-negative (Pseudomonas) and Gram-positive (Microbacterium, Bacillus, Staphylococcus, Paenibacillus) bacteria. http://purl.obolibrary.org/obo/ARO_3000573 tet(43) http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump Tet(43) is a tetracycline resistance gene with unknown origins, isolated from metagenomic DNA. http://purl.obolibrary.org/obo/ARO_3000574 vanR http://purl.obolibrary.org/obo/ARO_3002905 VanS-VanR two-component regulatory system VanR is a OmpR-family transcriptional activator in the VanSR regulatory system. When activated by VanS, it promotes cotranscription of VanA, VanH, and VanX. http://purl.obolibrary.org/obo/ARO_3000575 vanU http://purl.obolibrary.org/obo/ARO_3002976 gene(s) or protein(s) associated with a glycopeptide resistance cluster VanU is a transcriptional activator of vancomycin resistance genes. http://purl.obolibrary.org/obo/ARO_3000576 rifampin inactivation enzyme http://purl.obolibrary.org/obo/ARO_3000557 antibiotic inactivation enzyme Enzymes that inactivate rifampin antibiotics by chemical modification. http://purl.obolibrary.org/obo/ARO_3000577 subclass B1 Bacillus cereus Bc beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase Subclass B1 Bacillus cereus Bc beta-lactamases are zinc metallo-beta-lactamases that hydrolyze a large number of penicillins and cephalosporins. http://purl.obolibrary.org/obo/ARO_3000578 CcrA http://purl.obolibrary.org/obo/ARO_3004200 CfiA beta-lactamase CcrA is a CfiA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3000579 Chryseobacterium meningosepticum BlaB http://purl.obolibrary.org/obo/ARO_3004201 BlaB beta-lactamase This BlaB specific to Chryseobacterium meningosepticum mediates resistance against many beta-lactam antibiotics, notably penams and carbapenems. http://purl.obolibrary.org/obo/ARO_3000580 SPM beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase Sao Paulo metallo-beta-lactamase (SPM-1) confers resistance to carbapenem in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3000581 CphA beta-lactamase http://purl.obolibrary.org/obo/ARO_3000570 subclass B2 (metallo-) beta-lactamase CphA is an Ambler Class B MBL; subclass B2 originally isolated from Aeromonas hydrophilia. This enzyme has specific activity against carbapenems and is active as a mono-zinc protein. http://purl.obolibrary.org/obo/ARO_3000582 L1 beta-lactamase http://purl.obolibrary.org/obo/ARO_3004215 L1 family beta-lactamase L1 is an Ambler class B MBL; subclass B3 originally isolated from Stenotrophomonas maltophilia. It has activity against a broad range of beta-lactams and is only active with two Zn(II) ions in the active site. http://purl.obolibrary.org/obo/ARO_3000583 pristinamycin IA http://purl.obolibrary.org/obo/ARO_0000050 streptogramin B antibiotic Pristinamycin IA is a type B streptogramin antibiotic produced by Streptomyces pristinaespiralis. It binds to the P site of the 50S subunit of the bacterial ribosome, preventing the extension of protein chains. http://purl.obolibrary.org/obo/ARO_3000584 quinupristin http://purl.obolibrary.org/obo/ARO_0000050 streptogramin B antibiotic Quinupristin is a type B streptogramin and a semisynthetic derivative of pristinamycin 1A. It is a component of the drug Synercid and interacts with the 50S subunit of the bacterial ribosome to inhibit protein synthesis. http://purl.obolibrary.org/obo/ARO_3000586 pulvomycin http://purl.obolibrary.org/obo/ARO_3001219 elfamycin antibiotic Pulvomycin is a polyketide antibiotic that binds elongation factor Tu (EF-Tu) to inhibit protein biosynthesis by preventing the formation of the ternary complex (EF-Tu*GTP*aa-tRNA). Phenotypically, it was shown that pulvomycin sensitivity is dominant over resistance. http://purl.obolibrary.org/obo/ARO_3000587 sulbactam http://purl.obolibrary.org/obo/ARO_3007130 beta-lactam derived beta-lactamase inhibitor Sulbactam is an inhibitor of non-AmpC serine beta-lactamases. http://purl.obolibrary.org/obo/ARO_3000588 avibactam http://purl.obolibrary.org/obo/ARO_3007008 diazabicyclooctane Serine beta-lactamase inhibitor targeting class A, class C, and some class D enzymes. http://purl.obolibrary.org/obo/ARO_3000589 NDM-1 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase NDM-1 is a metallo-beta-lactamase isolated from Klebsiella pneumoniae with nearly complete resistance to all beta-lactam antibiotics. http://purl.obolibrary.org/obo/ARO_3000590 NDM-2 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase NDM-2 was isolated from a strain of Acinetobacter baumannii in Germany from a patient hospitalized in Cairo. A single amino acid substitution (P28R) differentiates this gene from NDM-1 and the two enzymes appear to have an identical spectrum of hydrolysis. http://purl.obolibrary.org/obo/ARO_3000592 ErmN http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase ErmN is a methyltransferase found in the tylosin producer Streptomyces fradiae. Like other Erm enzymes, it catalyzes the methylation of A2058 of the 23S ribosomal RNA. Specifically, this enzyme transfers only one methyl group. The gene is found in the tylosin biosynthetic cluster and is responsible for self-resistance to tylosin. http://purl.obolibrary.org/obo/ARO_3000593 ErmQ http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase ErmQ confers MLSb phenotype. http://purl.obolibrary.org/obo/ARO_3000594 ErmR http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase ErmR is a methyltransferase found in the erythromycin producer Aeromicrobium erythreum. Like other Erm enzymes, it catalyzes the methylation of A2058 of the 23S ribosomal RNA. The gene is found within the erythromycin biosynthetic cluster and is responsible for self-resistance. http://purl.obolibrary.org/obo/ARO_3000595 ErmT http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase ErmT confers MLSb phenotype. http://purl.obolibrary.org/obo/ARO_3000596 ErmX http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase ErmX is a rRNA methyltransferase that protects the ribosome from inactivation due to antibiotic binding. http://purl.obolibrary.org/obo/ARO_3000598 Erm(31) http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase Erm(31) confers a MLSb resistant phenotype. Along with erm(30), these genes are responsible for self-resistance in the pikromycin/narbomycin/methymycin/neomethymycin producer, Streptomyces venezuelae. http://purl.obolibrary.org/obo/ARO_3000599 Erm(33) http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase ErmD confers MLSb phenotype. http://purl.obolibrary.org/obo/ARO_3000600 Erm(34) http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase ErmD confers MLSb phenotype. http://purl.obolibrary.org/obo/ARO_3000601 Erm(38) http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase ErmD confers MLSb phenotype. http://purl.obolibrary.org/obo/ARO_3000602 Erm(39) http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase ErmD confers MLSb phenotype. http://purl.obolibrary.org/obo/ARO_3000603 Erm(41) http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase Erm41 confers MLSb phenotype. http://purl.obolibrary.org/obo/ARO_3000604 Erm(35) http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase ErmD confers MLSb phenotype. http://purl.obolibrary.org/obo/ARO_3000605 Erm(36) http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase ErmD confers MLSb phenotype. http://purl.obolibrary.org/obo/ARO_3000606 FEZ-1 http://purl.obolibrary.org/obo/ARO_3004211 FEZ beta-lactamase FEZ-1 is an Ambler class B MBL; subclass B3 first isolated from Legionella gormanii. It has activity against a broad range of beta-lactams and is only active with two Zn(II) ions in the active site. http://purl.obolibrary.org/obo/ARO_3000610 gene detected by antibiotic resistance screening microarray http://purl.obolibrary.org/obo/ARO_3000000 determinant of antibiotic resistance Many genes involved in antibiotic resistance are mobile and microarray probes for these genes can thus provide positive results for any number of organisms. CARD stores the coding sequences of genes targeted by the probe sets of available antibiotic resistance microarrays. http://purl.obolibrary.org/obo/ARO_3000614 mef(E) http://purl.obolibrary.org/obo/ARO_3000747 mef mef(E) is a proton motive efflux pump in Streptococcus pneumoniae that confers resistance to macrolides. It is found on the same operon as mefA and the ABC-efflux pump mel. http://purl.obolibrary.org/obo/ARO_3000616 mel http://purl.obolibrary.org/obo/ARO_3004471 msr-type ABC-F protein Mel, a homolog of MsrA, is an ABC-F subfamily protein associated with macrolide resistance. It is expressed on the same operon as mefA and mefE, both MFS-type efflux proteins that confer macrolide resistance. http://purl.obolibrary.org/obo/ARO_3000617 mecA http://purl.obolibrary.org/obo/ARO_3001208 methicillin resistant PBP2 A foreign PBP2a acquired by lateral gene transfer that is able to perform peptidoglycan synthesis in the presence of beta-lactams. http://purl.obolibrary.org/obo/ARO_3000619 fluoroquinolone resistant parC http://purl.obolibrary.org/obo/ARO_3000452 fluoroquinolone resistant DNA topoisomerase ParC is a subunit of topoisomerase IV, which decatenates and relaxes DNA to allow access to genes for transcription or translation. Point mutations in ParC prevent fluoroquinolone antibiotics from inhibiting DNA synthesis, and confer low-level resistance. Higher-level resistance results from both gyrA and parC mutations. http://purl.obolibrary.org/obo/ARO_3000620 adeL http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux AdeL is a regulator of AdeFGH in Acinetobacter baumannii. AdeL mutations are associated with AdeFGH overexpression and multidrug resistance. http://purl.obolibrary.org/obo/ARO_3000621 PC1 beta-lactamase (blaZ) http://purl.obolibrary.org/obo/ARO_3004197 BlaZ beta-lactamase The blaZ beta-lactamase is found in Bacillus subtilis and Staphylococcus aureus. http://purl.obolibrary.org/obo/ARO_3000622 colistin A http://purl.obolibrary.org/obo/ARO_0000067 colistin Colistin A, or polymyxin E1, has a 6-octanoic acid lipid tail. Polymyxins disrupt the cell membrane of Gram-negative bacteria. http://purl.obolibrary.org/obo/ARO_3000624 colistin B http://purl.obolibrary.org/obo/ARO_0000067 colistin Colistin B, or polymyxin E2, has a 6-heptanoic acid lipid tail. Polymyxins disrupt the cell membrane of Gram-negative bacteria. http://purl.obolibrary.org/obo/ARO_3000625 polymyxin B1 http://purl.obolibrary.org/obo/ARO_3000454 polymyxin B Polymyxin B1 is in the family of polymyxin lipopeptides with a 6-methyloctanoic acid acyl group. These antibiotics disrupt the cell membrane of Gram-negative bacteria. http://purl.obolibrary.org/obo/ARO_3000626 polymyxin B2 http://purl.obolibrary.org/obo/ARO_3000454 polymyxin B Polymyxin B2 is in the family of polymyxin lipopeptides with a 6-methylheptanoic acid acyl group. These antibiotics disrupt the cell membrane of Gram-negative bacteria. http://purl.obolibrary.org/obo/ARO_3000627 polymyxin B3 http://purl.obolibrary.org/obo/ARO_3000454 polymyxin B Polymyxin B3 is in the family of polymyxin lipopeptides with an octanoic acid acyl group. These antibiotics disrupt the cell membrane of Gram-negative bacteria. http://purl.obolibrary.org/obo/ARO_3000628 polymyxin B4 http://purl.obolibrary.org/obo/ARO_3000454 polymyxin B Polymyxin B4 is in the family of polymyxin lipopeptides with a heptanoic acid acyl group. These antibiotics disrupt the cell membrane of Gram-negative bacteria. http://purl.obolibrary.org/obo/ARO_3000629 bacitracin A http://purl.obolibrary.org/obo/ARO_0000041 bacitracin Bacitracin A is the primary component of bacitracin. It contains many uncommon amino acids and interferes with bacterial cell wall synthesis. http://purl.obolibrary.org/obo/ARO_3000630 bacitracin B http://purl.obolibrary.org/obo/ARO_0000041 bacitracin Bacitracin B is a component of bacitracin, an antibiotic mixture that interferes with bacterial cell wall synthesis. It differs from Bacitracin A with a valine instead of an isoleucine in its peptide. http://purl.obolibrary.org/obo/ARO_3000631 bacitracin F http://purl.obolibrary.org/obo/ARO_0000041 bacitracin Bacitracin F is a component of bacitracin, an antibiotic mixture that interferes with bacterial cell wall synthesis. It is formed when the thiazoline ring of bacitracin A is oxidatively deaminated. http://purl.obolibrary.org/obo/ARO_3000632 benzylpenicillin http://purl.obolibrary.org/obo/ARO_3009124 beta-lactamase sensitive penicillin Benzylpenicillin, commonly referred to as penicillin G, is effective against both Gram-positive and Gram-negative bacteria. It is unstable in acid. http://purl.obolibrary.org/obo/ARO_3000633 phenoxymethylpenicillin http://purl.obolibrary.org/obo/ARO_3009124 beta-lactamase sensitive penicillin Phenoxymethylpenicillin, or penicillin V, is a penicillin derivative that is acid stable but less active than benzylpenicillin (penicillin G). http://purl.obolibrary.org/obo/ARO_3000634 propicillin http://purl.obolibrary.org/obo/ARO_3009124 beta-lactamase sensitive penicillin Propicillin is an orally taken penicillin derivative that has high absorption but poor activity. http://purl.obolibrary.org/obo/ARO_3000635 dicloxacillin http://purl.obolibrary.org/obo/ARO_3009125 beta-lactamase resistant penicillin Dicloxacillin is a penicillin derivative that has an extra chlorine atom in comparison to cloxacillin. While more active than cloxacillin, its high affinity for serum protein reduces its activity in human serum in vitro. http://purl.obolibrary.org/obo/ARO_3000636 flucloxacillin http://purl.obolibrary.org/obo/ARO_3009125 beta-lactamase resistant penicillin Flucloxacillin is similar to cloxacillin, with an extra additional fluorine atom. http://purl.obolibrary.org/obo/ARO_3000637 ampicillin http://purl.obolibrary.org/obo/ARO_3009123 penicillin with extended spectrum Ampicillin is a penicillin derivative that is highly acid stable, with its activity similar to benzylpenicillin. http://purl.obolibrary.org/obo/ARO_3000638 azlocillin http://purl.obolibrary.org/obo/ARO_3009123 penicillin with extended spectrum Azlocillin is a semisynthetic derivative of penicillin that is notably active against Ps. aeruginosa and other Gram-negative bacteria. http://purl.obolibrary.org/obo/ARO_3000639 mezlocillin http://purl.obolibrary.org/obo/ARO_3009123 penicillin with extended spectrum Mezlocillin is a penicillin derivative taken parenterally. http://purl.obolibrary.org/obo/ARO_3000640 doripenem http://purl.obolibrary.org/obo/ARO_0000020 carbapenem Doripenem is a carbapenem with a broad range of activity against Gram-positive and Gram-negative bacteria, and along with meropenem, it is the most active beta-lactam antibiotic against Pseudomonas aeruginosa. It inhibits bacterial cell wall synthesis. http://purl.obolibrary.org/obo/ARO_3000641 cefalexin http://purl.obolibrary.org/obo/ARO_3009105 first-generation cephalosporin Cefalexin is a cephalosporin antibiotic that causes filamentation. It is resistant to staphylococcal beta-lactamase, but degraded by enterobacterial beta-lactamases. http://purl.obolibrary.org/obo/ARO_3000642 cefadroxil http://purl.obolibrary.org/obo/ARO_3009105 first-generation cephalosporin Cefadroxil, or p-hydroxycephalexin, is an cephalosporin antibiotic similar to cefalexin. http://purl.obolibrary.org/obo/ARO_3000643 cefotiam http://purl.obolibrary.org/obo/ARO_3009106 second-generation cephalosporin Cefotiam is a cephalosporin antibiotic with similar activity to cefuroxime but more active against enterobacteria. It is consumed orally as the prodrug cefotiam hexetil. http://purl.obolibrary.org/obo/ARO_3000644 cefaclor http://purl.obolibrary.org/obo/ARO_3009106 second-generation cephalosporin Cefaclor is a semisynthetic cephalosporin derived from cephalexin. It has broad-spectrum antibiotic activity. http://purl.obolibrary.org/obo/ARO_3000645 cefotaxime http://purl.obolibrary.org/obo/ARO_3009107 third-generation cephalosporin Cefotaxime is a semisynthetic cephalosporin taken parenterally. It is resistant to most beta-lactamases and active against Gram-negative rods and cocci due to its aminothiazoyl and methoximino functional groups. http://purl.obolibrary.org/obo/ARO_3000646 cefixime http://purl.obolibrary.org/obo/ARO_3009107 third-generation cephalosporin Cefixime is a cephalosporin resistant to most beta-lactamases. It is active against many enterobacteria, but activity against staphylococci is poor. http://purl.obolibrary.org/obo/ARO_3000647 cefpodoxime http://purl.obolibrary.org/obo/ARO_3009107 third-generation cephalosporin Cefpodoxime is a semisynthetic cephalosporin that acts similarly to cefotaxime with broad-spectrum activity. It is stable to many plasmid-mediated beta-lactamses. Cefpodoxime is consumed as the prodrug cefpodoxime proxetil. http://purl.obolibrary.org/obo/ARO_3000648 ceftibuten http://purl.obolibrary.org/obo/ARO_3009107 third-generation cephalosporin Ceftibuten is a semisynthetic cephalosporin active against Gram-negative bacilli. It is resistant against many plasmid-mediated beta-lactamases. http://purl.obolibrary.org/obo/ARO_3000649 cefditoren http://purl.obolibrary.org/obo/ARO_3009107 third-generation cephalosporin Cefditoren is a semisynthetic cephalosporin active against staphylococci, streptococci, and and most enterobacteria. It is resistant to staphylococcal and most enterobacterial beta-lactamases, and is usually taken as the prodrug cefditoren pivoxil. http://purl.obolibrary.org/obo/ARO_3000650 cefdinir http://purl.obolibrary.org/obo/ARO_3009107 third-generation cephalosporin Cefdinir is similar to cefixime with a modified side-chain at its 7-amino position. It also shares similar activity with cefixime but is more active against staphylococci. It has also be shown to enhance phagocytosis. http://purl.obolibrary.org/obo/ARO_3000651 ceftaroline http://purl.obolibrary.org/obo/ARO_3009109 other cephalosporins and penems Ceftaroline is a novel cephalosporin active against methicillin resistant Staphylococcus aureus. Like other cephalosporins it binds penicillin-binding proteins to inhibit cell wall synthesis. It strongly binds with PBP2a, associated with methicillin resistance. It is taken orally as the prodrug ceftaroline fosamil. http://purl.obolibrary.org/obo/ARO_3000652 isepamicin http://purl.obolibrary.org/obo/ARO_0000016 aminoglycoside antibiotic A semi-synthetic derivative of gentamicin B (hydroxyamino propionyl genamicin B). It is modified to combat microbial inactivation and has a slightly larger spectrum of activity compared to other aminoglycosides, including Ser marcescens, Enterobacteria, and K pneumoniae. http://purl.obolibrary.org/obo/ARO_3000653 G418 http://purl.obolibrary.org/obo/ARO_0000016 aminoglycoside antibiotic A gentamicin class aminoglycoside antibiotic often used in mammalian cell culture work as a selectable marker for the neo cassette (APH3'). http://purl.obolibrary.org/obo/ARO_3000654 arbekacin http://purl.obolibrary.org/obo/ARO_0000016 aminoglycoside antibiotic A synthetic derivative (1-N-(4-amino-2-hydroxybutyryl) of dibekacin used in Japan. It is active against methicillin-resistant Staph. aureus and shows synergy with ampicillin when treating gentamicin and vancomycin resistant enterocci. http://purl.obolibrary.org/obo/ARO_3000655 gentamicin B http://purl.obolibrary.org/obo/ARO_3007382 gentamicin Gentamicin B is a semisynthetic aminoglycoside antibacterial. http://purl.obolibrary.org/obo/ARO_3000656 AcrS http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux AcrS is a repressor of the AcrAB efflux complex and is associated with the expression of AcrEF. AcrS is believed to regulate a switch between AcrAB and AcrEF efflux. http://purl.obolibrary.org/obo/ARO_3000657 paromomycin http://purl.obolibrary.org/obo/ARO_0000016 aminoglycoside antibiotic An aminoglycoside antibiotic used for the treatment of parasitic infections. It is similar to neomycin sharing a similar spectrum of activity, but its hydroxyl group at the 6'-position instead of an amino group makes it resistant to AAC(6') modifying enzymes. http://purl.obolibrary.org/obo/ARO_3000658 lividomycin http://purl.obolibrary.org/obo/ARO_0000016 aminoglycoside antibiotic Lividomycins are aminoglycosidic antibiotics produced by Streptomyces lividus. They contain 2-amino-2,3-dideoxy-D-glucose. http://purl.obolibrary.org/obo/ARO_3000659 gatifloxacin http://purl.obolibrary.org/obo/ARO_0000001 fluoroquinolone antibiotic Gatifloxacin is an 8-methoxy, 7-piperazinyl, 6-fluoroquinolone that can be taken orally or by intravenous administration. It is active against most Gram-positive and Gram-negative bacteria, but inactive against non-fermenting Gram-negative rods including Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3000660 lomefloxacin http://purl.obolibrary.org/obo/ARO_0000001 fluoroquinolone antibiotic Lomefloxacin is a difluoropiperazinyl quinolone, sharing similar activities with other fluoroquinolones. It is used to treat urinary tract infections. Relative to other fluoroquinolones, it has a longer half life and has higher serum concentrations. http://purl.obolibrary.org/obo/ARO_3000661 nalidixic acid http://purl.obolibrary.org/obo/ARO_0000001 fluoroquinolone antibiotic Nalidixic acid is a quinolone derivative of naphthyridine active against many enterobacteria, but ineffective against Ps aeruginosa, Gram-positive bacteria, and anaerobes. Acquired resistance is common in nalidixic acid treatments. http://purl.obolibrary.org/obo/ARO_3000662 norfloxacin http://purl.obolibrary.org/obo/ARO_0000001 fluoroquinolone antibiotic Norfloxacin is a 6-fluoro, 7-piperazinyl quinolone with a wide range of activity against Gram-negative bacteria. It is inactive against most anaerobes. http://purl.obolibrary.org/obo/ARO_3000663 ofloxacin http://purl.obolibrary.org/obo/ARO_0000001 fluoroquinolone antibiotic Ofloxacin is a 6-fluoro, 7-piperazinyl quinolone with a methyl-substituted oxazine ring. It has a broad spectrum of activity including many enterobacteria and mycoplasma but most anaerobes are resistant. http://purl.obolibrary.org/obo/ARO_3000664 trovafloxacin http://purl.obolibrary.org/obo/ARO_0000001 fluoroquinolone antibiotic Trovafloxacin is a trifluoroquinalone with a broad spectrum of activity that acts by inhibiting the uncoiling of supercoiled DNA. While potent against many Gram-positive and Gram-negative bacteria, it is less active against pseudomonads and Cl. difficile. It is usually taken as the prodrug trovafloxacin mesylate or alatrofloxacin mesylate for oral or intravenous administration, respectively. http://purl.obolibrary.org/obo/ARO_3000665 grepafloxacin http://purl.obolibrary.org/obo/ARO_0000001 fluoroquinolone antibiotic Grepafloxacin is a broad-spectrum antibacterial quinoline. It is no longer taken due to its high toxicity. http://purl.obolibrary.org/obo/ARO_3000666 sparfloxacin http://purl.obolibrary.org/obo/ARO_0000001 fluoroquinolone antibiotic Sparfloxacin is a dimethylpiperazinyl difluoroquinolone that acts by inhibiting DNA gyrase. It is active against aerobic Gram-positive and Gram-negative bacteria, as well as some mycobacteria. It has moderate activity against some anaerobes. http://purl.obolibrary.org/obo/ARO_3000667 demeclocycline http://purl.obolibrary.org/obo/ARO_3000050 tetracycline antibiotic Demeclocycline is a tetracycline analog with 7-chloro and 6-methyl groups. Due to its fast absorption and slow excretion, it maintains higher effective blood levels compared to other tetracyclines. http://purl.obolibrary.org/obo/ARO_3000668 oxytetracycline http://purl.obolibrary.org/obo/ARO_3000050 tetracycline antibiotic Oxytetracycline is a derivative of tetracycline with a 5-hydroxyl group. Its activity is similar to other tetracyclines. http://purl.obolibrary.org/obo/ARO_3000669 virginiamycin M1 http://purl.obolibrary.org/obo/ARO_0000034 streptogramin A antibiotic Virginiamycin M1 is a streptogramin A antibiotic. http://purl.obolibrary.org/obo/ARO_3000670 pleuromutilin antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule Pleuromutilins are natural fungal products that target bacterial protein translation by binding the the 23S rRNA, blocking the ribosome P site at the 50S subunit. They are mostly used for agriculture and veterinary purposes. http://purl.obolibrary.org/obo/ARO_3000671 tiamulin http://purl.obolibrary.org/obo/ARO_3000670 pleuromutilin antibiotic Tiamulin is a pleuromutilin derivative currently used in veterinary medicine. It binds to the 23 rRNA of the 50S ribosomal subunit to inhibit protein translation. http://purl.obolibrary.org/obo/ARO_3000672 madumycin II http://purl.obolibrary.org/obo/ARO_0000034 streptogramin A antibiotic Madumycin II is a streptogramin A antibiotic. http://purl.obolibrary.org/obo/ARO_3000673 griseoviridin http://purl.obolibrary.org/obo/ARO_0000034 streptogramin A antibiotic Griseoviridin is a streptogramin A antibiotic. http://purl.obolibrary.org/obo/ARO_3000674 dalfopristin http://purl.obolibrary.org/obo/ARO_0000034 streptogramin A antibiotic Dalfopristin is a water-soluble semi-synthetic derivative of pristinamycin IIA. It is produced by Streptomyces pristinaespiralis and is used in combination with quinupristin in a 7:3 ratio. Both work together to inhibit protein synthesis, and is active against Gram-positive bacteria. http://purl.obolibrary.org/obo/ARO_3000675 pristinamycin IB http://purl.obolibrary.org/obo/ARO_0000050 streptogramin B antibiotic Pristinamycin IB is a class B streptogramin similar to pristinamycin IA, the former containing a N-methyl-4-(methylamino)phenylalanine instead of a N-methyl-4-(dimethylamino)phenylalanine in its class A streptogramin counterpart (one less methyl group). http://purl.obolibrary.org/obo/ARO_3000676 H-NS http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux H-NS is a histone-like protein involved in global gene regulation in Gram-negative bacteria. It is a repressor of the membrane fusion protein genes acrE, mdtE, and emrK as well as nearby genes of many RND-type multidrug exporters. http://purl.obolibrary.org/obo/ARO_3000677 virginiamycin S2 http://purl.obolibrary.org/obo/ARO_0000050 streptogramin B antibiotic Virginiamycin S2 is a streptogramin B antibiotic. http://purl.obolibrary.org/obo/ARO_3000678 pristinamycin IC http://purl.obolibrary.org/obo/ARO_0000050 streptogramin B antibiotic Pristinamycin IC is a class B streptogramin derived from virginiamycin S1. http://purl.obolibrary.org/obo/ARO_3000679 vernamycin C http://purl.obolibrary.org/obo/ARO_0000050 streptogramin B antibiotic Vernamycin C is a streptogramin B antibiotic. http://purl.obolibrary.org/obo/ARO_3000680 patricin A http://purl.obolibrary.org/obo/ARO_0000050 streptogramin B antibiotic Patricin A is a streptogramin B antibiotic. http://purl.obolibrary.org/obo/ARO_3000681 patricin B http://purl.obolibrary.org/obo/ARO_0000050 streptogramin B antibiotic Patricin B is a streptogramin B antibiotic. http://purl.obolibrary.org/obo/ARO_3000682 ostreogrycin B3 http://purl.obolibrary.org/obo/ARO_0000050 streptogramin B antibiotic Ostreogrycin B3 is a derivative of pristinamycin IA, with an additional 3-hydroxy group on its 4-oxopipecolic acid. http://purl.obolibrary.org/obo/ARO_3000683 sulfacetamide http://purl.obolibrary.org/obo/ARO_3000282 sulfonamide antibiotic Sulfacetamide is a very soluable sulfonamide antibiotic previously used to treat urinary tract infections. Its relatively low activity and toxicity to those with Stevens-Johnson syndrome have reduced its use and availability. http://purl.obolibrary.org/obo/ARO_3000684 mafenide http://purl.obolibrary.org/obo/ARO_3000282 sulfonamide antibiotic Mafenide is a sulfonamide used topically for treating burns. http://purl.obolibrary.org/obo/ARO_3000685 arylomycin http://purl.obolibrary.org/obo/ARO_3000035 lipopeptide antibiotic Arylomycins are lipopeptide antibiotics, sharing a lipohexapeptide with a C-terminal tripeptide macrolide and varying by the length of its alkyl chains. http://purl.obolibrary.org/obo/ARO_3000686 thiostrepton http://purl.obolibrary.org/obo/ARO_3000053 peptide antibiotic Thiostrepton is a cyclic peptide active against Gram-positive bacteria. It is produced by streptomyces bacteria. http://purl.obolibrary.org/obo/ARO_3000687 moenomycin antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule Moemomycin antibiotics are phosphoglycolipids that contain a 3-phosphoglyceric acid, often used as a mixture. They inhibit petidoglycan glycosyltransferases to prevent bacterial cell wall biosynthesis. http://purl.obolibrary.org/obo/ARO_3000688 furazolidone http://purl.obolibrary.org/obo/ARO_3004116 nitrofuran antibiotic Furazolidone is a nitrofuran antibiotic that is a non-ionic synthetic compound. It is taken orally and is active against many enteric pathogens. Furazolidone also has antiprotozoal activity and acts by inhibiting monoamine oxidase. http://purl.obolibrary.org/obo/ARO_3000689 metronidazole http://purl.obolibrary.org/obo/ARO_3004115 nitroimidazole antibiotic Metronidazole is a nitroimidazole that is active against anaerobic bacteria and protozoa. It is not effective against aerobic bacteria. Nitroimidazoles act by oxidizing DNA causing strand breaks and cell death. http://purl.obolibrary.org/obo/ARO_3000690 bleomycinic acid http://purl.obolibrary.org/obo/ARO_3000081 glycopeptide antibiotic Bleomycinic acid is a glycopeptide antibiotic produced by Streptomyces verticillus taken as a mixture of bleomycins. It induces stand breaks in bacterial nucleic acids. http://purl.obolibrary.org/obo/ARO_3000691 bleomycin A2 http://purl.obolibrary.org/obo/ARO_3000081 glycopeptide antibiotic Bleomycin A2 is a glycopeptide antibiotic produced by Streptomyces verticillus taken as a mixture of bleomycins. It induces stand breaks in bacterial nucleic acids. http://purl.obolibrary.org/obo/ARO_3000692 bleomycin B2 http://purl.obolibrary.org/obo/ARO_3000081 glycopeptide antibiotic Bleomycin B2 is a glycopeptide antibiotic produced by Streptomyces verticillus taken as a mixture of bleomycins. It induces stand breaks in bacterial nucleic acids. http://purl.obolibrary.org/obo/ARO_3000693 defensin http://purl.obolibrary.org/obo/ARO_3000053 peptide antibiotic Defensins are natural cationic peptides that have antibiotic properties. It is part of the innate immune system of plants and animals. http://purl.obolibrary.org/obo/ARO_3000694 magainin http://purl.obolibrary.org/obo/ARO_3000053 peptide antibiotic Magainins are antimicrobial peptides produced by amphibians skil cells as part of their innate immune system. It is active against a broad range of gram-negative and gram-positive bacteria, fungi and protozoa. http://purl.obolibrary.org/obo/ARO_3000695 actinomycin http://purl.obolibrary.org/obo/ARO_3000053 peptide antibiotic Actinomycins are peptide antibiotics that interact with DNA. This prevents RNA synthesis, thus preventing the production of proteins vital to the cell. http://purl.obolibrary.org/obo/ARO_3000696 Dactinomycin http://purl.obolibrary.org/obo/ARO_3000695 actinomycin Dactinomycin, also known as Actinomycin D, is a cyclic peptide antibiotic that interacts with DNA to inhibit RNA synthesis. http://purl.obolibrary.org/obo/ARO_3000697 moenomycin A1 http://purl.obolibrary.org/obo/ARO_3000687 moenomycin antibiotic Moenomycin A1 is a major component of moenomycin mixtures. It is produced by Streptomyces ghanaensis, S. bambergiensis, S. ederensis, and S. geysiriensis. http://purl.obolibrary.org/obo/ARO_3000698 sulfasalazine http://purl.obolibrary.org/obo/ARO_3000282 sulfonamide antibiotic Sulfasalazine is a derivative of the early sulfonamide sulfapyridine (salicylazosulfapyridine). It was developed to increase water solubility and is taken orally for ulcerative colitis. http://purl.obolibrary.org/obo/ARO_3000699 sulfamethizole http://purl.obolibrary.org/obo/ARO_3000282 sulfonamide antibiotic Sulfamethizole is a short-acting sulfonamide that inhibits dihydropteroate synthetase. http://purl.obolibrary.org/obo/ARO_3000700 lividomycin A http://purl.obolibrary.org/obo/ARO_3000658 lividomycin Lividomycin A is a pentasaccharide antibiotic which interferes with bacterial protein synthesis. http://purl.obolibrary.org/obo/ARO_3000701 lividomycin B http://purl.obolibrary.org/obo/ARO_3000658 lividomycin Lividomycin B is a derivative of lividomycin A with a removed mannose group (demannosyllividomycin A). Livodomycins interfere with bacterial protein synthesis. http://purl.obolibrary.org/obo/ARO_3000702 acrR http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux AcrR is a repressor of the AcrAB-TolC multidrug efflux complex. AcrR mutations result in high level antibiotic resistance. http://purl.obolibrary.org/obo/ARO_3000704 cefalotin http://purl.obolibrary.org/obo/ARO_3009105 first-generation cephalosporin Cefalotin is a semisynthetic cephalosporin antibiotic activate against staphylococci. It is resistant to staphylococci beta-lactamases but hydrolyzed by enterobacterial beta-lactamases. http://purl.obolibrary.org/obo/ARO_3000707 antibiotic mixture http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule Mixtures of antibiotics are commonly used clinically. These mixtures link to antibiotic molecules that are also listed in their respective families under antibiotic molecules. i.e. 'Gramicidin A' is part of the mixture 'gramicidin D', while 'Gramicidin A' is also a 'gramicidin', which is a 'peptide antibiotic'. http://purl.obolibrary.org/obo/ARO_3000708 antibiotic target http://purl.obolibrary.org/obo/ARO_1000001 process or component of antibiotic biology or chemistry Antibiotic targets are components of the bacterial or fungal cell. Bacterial targets are usually significantly different from their eukaryotic counterparts to allow for selective antibacterial activity. Exceptions include antibiotics that are converted to an active form inside the bacterium. Resistance mechanisms may modify these targets to protect bacteria or fungi from the effects of antibiotics. http://purl.obolibrary.org/obo/ARO_3000709 cell wall synthesis enzyme targeted by antibiotic http://purl.obolibrary.org/obo/ARO_3000708 antibiotic target Cell wall biosynthesis provides bacteria with a layer of peptidoglycan that provides rigidity and protects the cell from lysis due to osmotic pressure. Cell wall structures vary significantly between Gram-positive and Gram-negative bacteria, while mycobacteria have a unique cell wall composition. http://purl.obolibrary.org/obo/ARO_3000710 cell membrane component targeted by antibiotic http://purl.obolibrary.org/obo/ARO_3000708 antibiotic target Interaction with the cell membrane phospholipids interferes with membrane permeability and integrity, leading to the leakage of cell contents. The outer membrane of Gram-negative bacteria is particularly sensitive. http://purl.obolibrary.org/obo/ARO_3000711 protein synthesis machinery targeted by antibiotic http://purl.obolibrary.org/obo/ARO_3000708 antibiotic target Protein synthesis in bacteria is accomplished by cytosolic ribosomes that are structurally different from eukaryotic ribosomes, and thus a target for many antibiotics. By inhibiting ribosomal activity, either by directly binding to the ribosome or interacting with co-factors, antibiotics prevent protein synthesis. http://purl.obolibrary.org/obo/ARO_3000712 nucleic acid synthesis machinery targeted by antibiotic http://purl.obolibrary.org/obo/ARO_3000708 antibiotic target Bacterial DNA and RNA synthesis includes many enzymes unique to bacteria that are targeted by antibiotics. http://purl.obolibrary.org/obo/ARO_3000713 nucleic acid targeted by antibiotic http://purl.obolibrary.org/obo/ARO_3000708 antibiotic target Nucleic acids can also be targeted by antibiotics. These drugs are usually converted to an active form by enzymes unique to bacteria to prevent toxicity to the host. http://purl.obolibrary.org/obo/ARO_3000714 folate synthesis enzyme targeted by antibiotic http://purl.obolibrary.org/obo/ARO_3000708 antibiotic target Enzymes in the folate synthesis pathway are targeted by two main classes of antibiotics: sulfonamides and diaminopyrimidines. Inhibition of these enzymes block the production of key precursors for nucleotides and amino acids. http://purl.obolibrary.org/obo/ARO_3000715 isoprenoid synthesis enzyme targeted by antibiotic http://purl.obolibrary.org/obo/ARO_3000708 antibiotic target Enzymes in this pathway generate important precursors for macromolecules. While eukaryotes and prokaryotes both synthesize isoprenoids, many bacteria and notably mycobacteria use an alternative pathway that is targeted by antibiotics. http://purl.obolibrary.org/obo/ARO_3000716 mycolic acid synthesis enzyme targeted by antibiotic http://purl.obolibrary.org/obo/ARO_3000708 antibiotic target Mycolic acids are produced by mycobacteria. These fatty acids are required for the construction of cell walls. Enzymes that are targeted by antibiotics include synthases, elongases, and dehydrogenases. http://purl.obolibrary.org/obo/ARO_3000717 antibiotic sensitive signal peptidase I http://purl.obolibrary.org/obo/ARO_3000708 antibiotic target Signal peptidase I is a bacterial signal peptidase that cleaves signal peptides from translated proteins. These signal peptides direct proteins to their destination, and then must be cleaved in order to function. http://purl.obolibrary.org/obo/ARO_3000718 marR http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux MarR is a repressor of the mar operon marRAB, thus regulating the expression of marA, the activator of multidrug efflux pump AcrAB. http://purl.obolibrary.org/obo/ARO_3000719 bacitracin sensitive isoprenyl pyrophosphate http://purl.obolibrary.org/obo/ARO_3000709 cell wall synthesis enzyme targeted by antibiotic Isoprepnyl pyrophosphate removes a phosphate group that is added from the peptidoglycan subunit to permit its transfer across the cell membrane. The phosphate group must be removed before its incorporation into peptidoglycan macromolecules. http://purl.obolibrary.org/obo/ARO_3000720 acyl-D-alanyl-D-alanine http://purl.obolibrary.org/obo/ARO_3000721 cell wall component targeted by antibiotic The acyl-D-alanyl-D-alanine group is found at the terminal end of the pentapeptide chains of peptidoglycan subunits. Antibiotics that bind to this group block the addition of subunits, inhibiting peptidoglycan synthesis. This group is most accessible in Gram-postive bacteria. http://purl.obolibrary.org/obo/ARO_3000721 cell wall component targeted by antibiotic http://purl.obolibrary.org/obo/ARO_3000708 antibiotic target The cell wall is unique to bacteria and provides rigidity and protects the cell from lysis due to osmotic pressure. Its characteristic component is peptidoglycan, though cell wall structures vary significantly between Gram-positive and Gram-negative bacteria, as well as mycobacteria. http://purl.obolibrary.org/obo/ARO_3000722 cycloserine sensitive alr http://purl.obolibrary.org/obo/ARO_3000709 cell wall synthesis enzyme targeted by antibiotic Alanine racemase (alr) converts the natural L-alanine to the D-alanine required in the pentapeptide chains in peptidoglycan. It is found in both Gram-positive and Gram-negative bacteria. http://purl.obolibrary.org/obo/ARO_3000723 cycloserine sensitive D-alanine synthetase http://purl.obolibrary.org/obo/ARO_3000709 cell wall synthesis enzyme targeted by antibiotic D-Alanine synthetase (or ligase), also known as ddla, joins two D-alanines before their addition to the pentapeptide chains of peptidoglycan. It is found in both Gram-positive and Gram-negative bacteria. http://purl.obolibrary.org/obo/ARO_3000724 fosfomycin sensitive pyruvyl transferase (murA) http://purl.obolibrary.org/obo/ARO_3000709 cell wall synthesis enzyme targeted by antibiotic Pyruvyl transferase is responsible for the conversion of N-acetylglucosamine (NAG) to N-acetylmuramic acid (NAMA). NAMA is a part of the macromolecular backbone of peptidoglycans. Pyruvyl transferase is found in both Gram-positive and Gram-negative bacteria. http://purl.obolibrary.org/obo/ARO_3000725 antibiotic sensitive aftA http://purl.obolibrary.org/obo/ARO_3000709 cell wall synthesis enzyme targeted by antibiotic Arabinofuranosyltransferases allow for the polymerization of arabinose to form arabinan. Arabanan is required for formation of mycobacterial cell walls. http://purl.obolibrary.org/obo/ARO_3000726 pentaglycyl bridge http://purl.obolibrary.org/obo/ARO_3000721 cell wall component targeted by antibiotic The pentaglycyl bridge is part of Gram-positive peptidoglycan, allowing the formation of a thick and rigid cell wall. http://purl.obolibrary.org/obo/ARO_3000727 50S ribosomal subunit http://purl.obolibrary.org/obo/ARO_3000711 protein synthesis machinery targeted by antibiotic The larger of two ribosomal subunits that make up the 70S bacterial ribosome. http://purl.obolibrary.org/obo/ARO_3000728 30S ribosomal subunit http://purl.obolibrary.org/obo/ARO_3000711 protein synthesis machinery targeted by antibiotic The smaller of two ribosomal subunits that make up the 70S bacterial ribosome. http://purl.obolibrary.org/obo/ARO_3000729 ribosomal complex http://purl.obolibrary.org/obo/ARO_3000711 protein synthesis machinery targeted by antibiotic The ribosomal complex can be targeted by antibiotics that stabilize the entire complex and prevent further translation. These antibiotics target both subunits in the process of protein translation. http://purl.obolibrary.org/obo/ARO_3000730 elongation factor G http://purl.obolibrary.org/obo/ARO_3000711 protein synthesis machinery targeted by antibiotic Elongation factor G (EF-G) provides energy for the translocation step in protein synthesis. Antibiotics that target EF-G allow one round of translocation but prevent EF-G from dissociating from the ribosome-RNA complex. http://purl.obolibrary.org/obo/ARO_3000731 elongation factor Tu http://purl.obolibrary.org/obo/ARO_3000711 protein synthesis machinery targeted by antibiotic Elongation factor Tu is required for peptide elongation in bacterial protein synthesis. http://purl.obolibrary.org/obo/ARO_3000732 antibiotic sensitive Isoleucyl-tRNA transferase http://purl.obolibrary.org/obo/ARO_3000711 protein synthesis machinery targeted by antibiotic Isoleucyl-tRNA transferase recognizes isoleucine codons and works with the ribosome to incorporate isoleucine amino acids into polypeptide chains. It can be targeted by antibiotics that have an analog of isoleucine through competitive inhibition. http://purl.obolibrary.org/obo/ARO_3000733 fluoroquinolone sensitive gyrA http://purl.obolibrary.org/obo/ARO_3003254 antibiotic sensitive DNA topoisomerase subunit gyrA DNA gyrase is responsible for DNA supercoiling and consists of two alpha and two beta subunits. Binding the alpha-subunit is sufficient to inhibit DNA supercoiling. http://purl.obolibrary.org/obo/ARO_3000734 antibiotic sensitive DNA topoisomerase subunit gyrB http://purl.obolibrary.org/obo/ARO_3000766 antibiotic sensitive topoisomerase subunit DNA gyrase is responsible for DNA supercoiling and consists of two alpha and two beta subunits. Binding the beta-subunit is sufficient to inhibit DNA supercoiling. http://purl.obolibrary.org/obo/ARO_3000735 Fluoroquinolone sensitive parC http://purl.obolibrary.org/obo/ARO_3003256 antibiotic sensitive DNA topoisomerase subunit parC parC is a subunit of the DNA topoisomerase IV and is sensitive to fluoroquinolone. http://purl.obolibrary.org/obo/ARO_3000736 rho transcription terminator factor http://purl.obolibrary.org/obo/ARO_3000712 nucleic acid synthesis machinery targeted by antibiotic The rho transcription terminator factor moves along RNA as it is transcribed, unwinding the RNA from the DNA. It is also responsible for recognizing transcription termination pause sites, slowing down RNA polymerase and allowing mRNA to be released. http://purl.obolibrary.org/obo/ARO_3000737 rifamycin sensitive beta-subunit of RNA polymerase (rpoB) http://purl.obolibrary.org/obo/ARO_3003277 antibiotic sensitive beta-subunit of RNA polymerase (rpoB) The beta-subunit of RNA polymerase is targeted as a complex. When blocked, RNA strand elongation cannot continue after the first few nucleotides. http://purl.obolibrary.org/obo/ARO_3000738 deoxyribonucleic acid http://purl.obolibrary.org/obo/ARO_3000713 nucleic acid targeted by antibiotic Antibiotics can target DNA to cause strand breaks or prevent transcription. The activity of these antibiotics can be context dependent: some antibiotics are converted to an active form only in certain species, while others target DNA as it is being transcribed. http://purl.obolibrary.org/obo/ARO_3000739 RNA guanosine binding site http://purl.obolibrary.org/obo/ARO_3000740 ribonucleic acid RNA intron self-splicing action can be inhibited by antibiotics that target a G-binding site to compete with the guanosine cofactor. http://purl.obolibrary.org/obo/ARO_3000740 ribonucleic acid http://purl.obolibrary.org/obo/ARO_3000713 nucleic acid targeted by antibiotic Many types of ribonucleic acids (RNAs) are targeted by antibiotics, including mRNA templates and ribosomal RNA. Some antibiotics target all RNAs and cause strand breaks. http://purl.obolibrary.org/obo/ARO_3000741 transcription complex DNA http://purl.obolibrary.org/obo/ARO_3000738 deoxyribonucleic acid DNA in the transcriptional complex is partially unwound, allowing antibiotics to target exposed bases and prevent DNA transcription. http://purl.obolibrary.org/obo/ARO_3000742 anaerobe DNA http://purl.obolibrary.org/obo/ARO_3000738 deoxyribonucleic acid DNA in anaerobes are targeted by antibiotics that are converted to an active form in the anaerobe environment. For nitroimidazoles, the antibiotic is reduced to a highly oxidative intermediate that causes DNA oxidation and double-stranded breaks. http://purl.obolibrary.org/obo/ARO_3000743 1-deoxy-D-xylulose 5-phosphate reductoisomerase http://purl.obolibrary.org/obo/ARO_3000715 isoprenoid synthesis enzyme targeted by antibiotic This reductoisomerase is found in an alternate isoprenoid synthase pathway that is mevalonate independent. Isoprenoids are important precursors to many other macromolecules. This non-mevalonate pathway is used by plants and most bacteria, including mycobacteria, but not eukaryotes, allowing for selectivea action. Staphylococcus aureus and some other Gram-positive bacteria use a mevalonate-dependent pathway, and are resistant against 1-deoxy-D-xylose 5-phosphate reductoisomerase inhibitors. http://purl.obolibrary.org/obo/ARO_3000744 antibiotic sensitive dihydropteroate synthase http://purl.obolibrary.org/obo/ARO_3000714 folate synthesis enzyme targeted by antibiotic Dihydropteroate synthase catalyzes the conversion of p-aminobenzoic acid to dihydropteroic acid as part of the tetrahydrofolic acid biosynthetic pathway. Tetrahydrofolic acid is essential for folate synthesis, and a precursor of many nucleotides and amino acids. Inhibiting dihydropteroate leads to slow cell death, as bacteria can survive on existing folate storages for a few generations. http://purl.obolibrary.org/obo/ARO_3000745 antibiotic sensitive dihydrofolate reductase http://purl.obolibrary.org/obo/ARO_3000714 folate synthesis enzyme targeted by antibiotic Dihydrofolate reductase synthesizes the co-enzyme tetrahydrofolic acid, which is also an essential precursor in the de novo synthesis of the DNA nucleotide thymidine. http://purl.obolibrary.org/obo/ARO_3000746 mepR http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux MepR is an upstream repressor of MepA in Staphylococcus aureus. It is part of the mepRAB operon. http://purl.obolibrary.org/obo/ARO_3000747 mef http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump Mef efflux pumps are MFS-type transporters that confer macrolide resistance in Streptococcus pneumoniae. http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance http://purl.obolibrary.org/obo/ARO_3000159 efflux pump complex or subunit conferring antibiotic resistance Subunits of efflux proteins that pump antibiotic out of a cell to confer resistance. http://purl.obolibrary.org/obo/ARO_3000749 beta-lactam sensitive penicillin-binding protein http://purl.obolibrary.org/obo/ARO_3000709 cell wall synthesis enzyme targeted by antibiotic Penicillin-binding proteins (PBPs) are responsible for transpeptidation, joining subunits to form peptidoglycan. They are numbered according to descending molecular weight, and may vary between species. These numbers represent the PBPs of E. coli. Inhibition of the larger PBPs responsible for transpeptidation (1-3) are lethal. Smaller PBPs (4-6) are involed in carboxypeptidation; inhibition of these is non-lethal. http://purl.obolibrary.org/obo/ARO_3000750 protein of two-component regulatory system modulating antibiotic efflux http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux A protein, either a histidine kinase or a response regulator, that is part of a two-component regulatory system that directly or indirectly change rates of antibiotic efflux. http://purl.obolibrary.org/obo/ARO_3000753 abeM http://purl.obolibrary.org/obo/ARO_3000112 multidrug and toxic compound extrusion (MATE) transporter AbeM is an multidrug efflux pump found in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3000754 antibiotic sensitive peptidyl transferase (23S rRNA) http://purl.obolibrary.org/obo/ARO_3000740 ribonucleic acid The bacterial 23S rRNA, at the P site of the 50S subunit, has peptidyl transferase activity and is responsible for peptide synthesis and elongation. http://purl.obolibrary.org/obo/ARO_3000755 antibiotic sensitive 16S rRNA http://purl.obolibrary.org/obo/ARO_3000740 ribonucleic acid The 16S rRNA of the 30S ribosomal subunit helps to stabilize the aminoacyl-tRNAs for pairing with the mRNA codons. Some antibiotics (aminoglycosides) that target the 16S rRNA lead to mRNA misreading as well as premature termination. Other antibiotics (tetracyclines) that target the 16S rRNA prevent incoming charged-tRNAs from binding to the ribosome's A-site, stopping elongation. http://purl.obolibrary.org/obo/ARO_3000756 30S ribosomal subunit P-site http://purl.obolibrary.org/obo/ARO_3000728 30S ribosomal subunit The P-site of the ribosome binds the peptidyl-tRNA with the growing polypeptide chain. Antibiotics that target the P-site block fMet-tRNA from entering, thus inhibiting peptide elongation. http://purl.obolibrary.org/obo/ARO_3000757 50S ribosomal subunit P-site http://purl.obolibrary.org/obo/ARO_3000727 50S ribosomal subunit The P-site of the ribosome binds the peptidyl-tRNA with the growing polypeptide chain, and is a common target for many antibiotics that inhibit the 50S ribosomal subunit. Some antibiotics (oxazolidinones) block the 50S subunit from interacting with the 30S subunit to prevent the formation of the ribosomal complex. Other antibiotics (thiostrepton) block the 50S subunit from interacting with elongation factors G and Tu (EF-G, Ef-Tu), preventing GTP-dependent reactions of peptidyl transferase, and translocation, respectively. Other antibiotics (macrolides) prevent protein translocation. http://purl.obolibrary.org/obo/ARO_3000758 fosmidomycin http://purl.obolibrary.org/obo/ARO_3007149 phosphonic acid antibiotic Fosmidomycin is an inhibitor of 1-deoxy-D-xylulose 5-phosphate reductoisomerase, an enzyme in the non-mevalonate pathway for isoprenoid synthesis. It is active against enterobacteria, but not against Gram-positive bacteria or anaerobes. http://purl.obolibrary.org/obo/ARO_3000759 fusidic acid http://purl.obolibrary.org/obo/ARO_3007153 fusidane antibiotic Fusidic acid is the only commercially available fusidane, a group of steroid-like antibiotics. It is most active against Gram-positive bacteria, and acts by inhibiting elongation factor G to block protein synthesis. http://purl.obolibrary.org/obo/ARO_3000760 cycloserine http://purl.obolibrary.org/obo/ARO_3007154 cycloserine-like antibiotic Cycloserine is an anti-mycobacterial agent, and is active against enterobacteria, streptococci, M. tuberculosis, Staphylococcus aureus, and many Gram-negative and Gram-positive bacteria. It inhibits cell wall biosynthesis. http://purl.obolibrary.org/obo/ARO_3000761 mecillinam http://purl.obolibrary.org/obo/ARO_3009123 penicillin with extended spectrum Mecillinam is a broad-spectrum beta-lactam antibiotic that was semi-synthetically derived to have a different drug centre, being a 6-alpha-amidinopenicillanate instead of a 6-alpha-acylaminopenicillanate. Contrasting most beta-lactam drugs, mecillinam is most active against Gram-negative bacteria. It binds specifically to penicillin binding protein 2 (PBP2). http://purl.obolibrary.org/obo/ARO_3000762 pefloxacin http://purl.obolibrary.org/obo/ARO_0000001 fluoroquinolone antibiotic Pefloxacin is structurally and functionally similar to norfloxacin. It is poorly active against mycobacteria, while anaerobes are resistant. http://purl.obolibrary.org/obo/ARO_3000763 antibiotic sensitive embC http://purl.obolibrary.org/obo/ARO_3000725 antibiotic sensitive aftA EmbC is an arabinosyltransferase involved in lipoarabinomannan synthesis. http://purl.obolibrary.org/obo/ARO_3000764 antibiotic sensitive embA http://purl.obolibrary.org/obo/ARO_3000725 antibiotic sensitive aftA EmbA is an arabinosyltransferase that works as a heterodimer with EmbB. It is involved in the synthesis of arabinogalactan, a component of the mycobacterial cell wall. http://purl.obolibrary.org/obo/ARO_3000765 antibiotic sensitive embB http://purl.obolibrary.org/obo/ARO_3000725 antibiotic sensitive aftA EmbB is an arabinosyltransferase that works as a heterodimer with EmbA. It is involved in the synthesis of arabinogalactan, a component of the mycobacterial cell wall. http://purl.obolibrary.org/obo/ARO_3000766 antibiotic sensitive topoisomerase subunit http://purl.obolibrary.org/obo/ARO_3000712 nucleic acid synthesis machinery targeted by antibiotic Topoisomerases are responsible for winding and relaxing supercoiled DNA. The subunits of gyrase (gyrA, gyrB) and topoisomerase IV (parC, parE, parY) are targeted by antibiotics. http://purl.obolibrary.org/obo/ARO_3000767 avoparcin http://purl.obolibrary.org/obo/ARO_3000081 glycopeptide antibiotic Avoparcin is a glycopeptide antibiotic that is an analog of vancomycin. It was formally used to treat animals, but has since been banned because of its selection for vancomycin-resistant enterococci. http://purl.obolibrary.org/obo/ARO_3000768 abeS http://purl.obolibrary.org/obo/ARO_0010003 small multidrug resistance (SMR) antibiotic efflux pump AbeS in an efflux pump of the SMR family of transporters found in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3000769 PatA-PatB http://purl.obolibrary.org/obo/ARO_0010001 ATP-binding cassette (ABC) antibiotic efflux pump PatA-PatB is an efflux protein complex that is associated with fluoroquinolone resistance in Streptococcus pneumoniae. Experiments indicate that PatA and PatB form a heterodimeric transporter. http://purl.obolibrary.org/obo/ARO_3000770 AdeABC http://purl.obolibrary.org/obo/ARO_0010004 resistance-nodulation-cell division (RND) antibiotic efflux pump AdeABC is an RND multidrug efflux system in Acinetobacter species, notably A. baunmannii. AdeA is a membrane fusion protein, AdeB is the inner membrane transporter, and AdeC is the outer membrane factor. It confers resistance to tigecycline. http://purl.obolibrary.org/obo/ARO_3000771 AdeFGH http://purl.obolibrary.org/obo/ARO_0010004 resistance-nodulation-cell division (RND) antibiotic efflux pump AdeFGH is a RND multidrug efflux pump expressed in Acinetobacter baumannii. It confers resistance to fluoroquinolone, tetracycline, tigecycline, chloramphenicol, clindamycin, trimethoprim, and sulfamethoxazole. http://purl.obolibrary.org/obo/ARO_3000772 AdeIJK http://purl.obolibrary.org/obo/ARO_0010004 resistance-nodulation-cell division (RND) antibiotic efflux pump AdeIJK is a RND multidrug efflux pump expressed in Acinetobacter baumannii. It contributes to resistance for beta-lactams, chloramphenicol, tetracycline, erythromycin, lincosamides, fluoroquinolone, fusidic acid, novobiocin, rifampicin, trimethoprim, acridine, pyronine, and safranin. http://purl.obolibrary.org/obo/ARO_3000773 CmeABC http://purl.obolibrary.org/obo/ARO_0010004 resistance-nodulation-cell division (RND) antibiotic efflux pump CmeABC is a multidrug efflux pump in Campylobacter jejuni. Its overexpression led to enhanced resistance to ciprofloxacin, norfloxacin, cefotaxime, fusidic acid, and erythromycin. CmeA acts as the periplasmic fusion protein, CmeB is the inner membrane transporter, and CmeC is an outer membrane protein. http://purl.obolibrary.org/obo/ARO_3000774 adeA http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance AdeA is the membrane fusion protein of the multidrug efflux complex AdeABC. http://purl.obolibrary.org/obo/ARO_3000775 adeB http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance AdeB is the multidrug transporter of the adeABC efflux system. http://purl.obolibrary.org/obo/ARO_3000777 adeF http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance AdeF is the membrane fusion protein of the multidrug efflux complex AdeFGH. http://purl.obolibrary.org/obo/ARO_3000778 adeG http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance AdeG is the inner membrane transporter of the AdeFGH multidrug efflux complex. http://purl.obolibrary.org/obo/ARO_3000779 adeH http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance AdeH is the outer membrane channel protein of the AdeFGH multidrug efflux complex. http://purl.obolibrary.org/obo/ARO_3000780 adeI http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance AdeI is the membrane fusion protein of the AdeIJK multidrug efflux complex. http://purl.obolibrary.org/obo/ARO_3000781 adeJ http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance AdeJ is a RND efflux protein that acts as the inner membrane transporter of the AdeIJK efflux complex. It has 57% identity with E. coli AcrB. http://purl.obolibrary.org/obo/ARO_3000782 adeK http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance AdeK is the outer membrane factor protein in the adeIJK multidrug efflux complex. http://purl.obolibrary.org/obo/ARO_3000783 cmeA http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance CmeA is the membrane fusion protein of the CmeABC multidrug efflux complex. http://purl.obolibrary.org/obo/ARO_3000784 cmeB http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance CmeB is the inner membrane transporter the CmeABC multidrug efflux complex. http://purl.obolibrary.org/obo/ARO_3000785 cmeC http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance CmeC is the outer membrane channel protein of the CmeABC multidrug efflux complex. http://purl.obolibrary.org/obo/ARO_3000786 MdsABC http://purl.obolibrary.org/obo/ARO_0010004 resistance-nodulation-cell division (RND) antibiotic efflux pump MdsABC, or GesABC, is a RND-type efflux complex found in Salmonella. In addition to its metal-efflux system, GesABC is also capable of exporting beta-lactams, chloramphenicol, and thiamphenicol. GesB is the inner membrane transporter and is similar to MexF; GesA is the membrane-fusion protein, and GesC is the outer membrane factor. http://purl.obolibrary.org/obo/ARO_3000787 MdtABC-TolC http://purl.obolibrary.org/obo/ARO_0010004 resistance-nodulation-cell division (RND) antibiotic efflux pump MdtABC-TolC is a multidrug efflux system in Gram-negative bacteria, including E. coli and Salmonella. MdtA is a membrane fusion protein; TolC is the outer membrane channel; MdtBC form a drug transporter. In the absence of MdtB, the MdtAC-TolC has narrower drug specificity, leading to the loss of novobiocin resistance, for example. http://purl.obolibrary.org/obo/ARO_3000788 MdtEF-TolC http://purl.obolibrary.org/obo/ARO_0010004 resistance-nodulation-cell division (RND) antibiotic efflux pump MdtEF-TolC is a multidrug efflux complex in Gram-negative bacteria, including E. coli. MdtE is the membrane fusion protein, MdtF is the inner membrane transporter, while TolC is the outer membrane channel. http://purl.obolibrary.org/obo/ARO_3000789 mdsA http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MdsA is the membrane fusion protein of the multidrug and metal efflux complex MdsABC. http://purl.obolibrary.org/obo/ARO_3000790 mdsB http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MdsB is the inner membrane transporter of the multidrug and metal efflux complex MdsABC. mdsB corresponds to 1 locus in Pseudomonas aeruginosa PAO1 (gene name: mexQ) and 2 loci in Pseudomonas aeruginosa LESB58. http://purl.obolibrary.org/obo/ARO_3000791 mdsC http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MdsC is the outer membrane channel of the multidrug and metal efflux complex MdsABC. http://purl.obolibrary.org/obo/ARO_3000792 mdtA http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MdtA is the membrane fusion protein of the multidrug efflux complex mdtABC. http://purl.obolibrary.org/obo/ARO_3000793 mdtB http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MdtB is a transporter that forms a heteromultimer complex with MdtC to form a multidrug transporter. MdtBC is part of the MdtABC-TolC efflux complex. http://purl.obolibrary.org/obo/ARO_3000794 mdtC http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MdtC is a transporter that forms a heteromultimer complex with MdtB to form a multidrug transporter. MdtBC is part of the MdtABC-TolC efflux complex. In the absence of MdtB, MdtC can form a homomultimer complex that results in a functioning efflux complex with a narrower drug specificity. mdtC corresponds to 3 loci in Pseudomonas aeruginosa PAO1 (gene name: muxC/muxB) and 3 loci in Pseudomonas aeruginosa LESB58. http://purl.obolibrary.org/obo/ARO_3000795 mdtE http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MdtE is the membrane fusion protein of the MdtEF multidrug efflux complex. It shares 70% sequence similarity with AcrA. http://purl.obolibrary.org/obo/ARO_3000796 mdtF http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MdtF is the multidrug inner membrane transporter for the MdtEF-TolC efflux complex. http://purl.obolibrary.org/obo/ARO_3000797 MexCD-OprJ http://purl.obolibrary.org/obo/ARO_0010004 resistance-nodulation-cell division (RND) antibiotic efflux pump MexCD-OprJ is a multidrug efflux protein expressed in the Gram-negative Pseudomonas aeruginosa. MexC is the membrane fusion protein; MexD is the inner membrane transporter; and OprJ is the outer membrane channel. MexAB-OprM is associated with resistance to fluoroquinolones, chloramphenicol, and macrolides. MexCD-OprJ is typically quiescent in wild-type cells, with expression following mutation of the nfxB gene that is divergently transcribed from the mexCD-oprJ operon and encodes a repressor of mexCD-oprJ expression. Expression of mexCD–oprJ is controlled by a single known regulator, the NfxB repressor encoded by the nfxB gene, which is transcribed divergently from the efflux genes. http://purl.obolibrary.org/obo/ARO_3000798 MexEF-OprN http://purl.obolibrary.org/obo/ARO_0010004 resistance-nodulation-cell division (RND) antibiotic efflux pump MexEF-OprN is a multidrug efflux protein expressed in the Gram-negative Pseudomonas aeruginosa. MexE is the membrane fusion protein; MexF is the inner membrane transporter; and OprN is the outer membrane channel. MexEF-OprN is associated with resistance to fluoroquinolones, chloramphenicol, and trimethoprim. Regulation of mexEF-oprN operon expression is multifaceted with the MexT activator being one of the most prominent regulatory proteins. MexEF-OprN is the only positively regulated RND pump of P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3000799 MexGHI-OpmD http://purl.obolibrary.org/obo/ARO_0010004 resistance-nodulation-cell division (RND) antibiotic efflux pump MexGHI-OpmD is an efflux complex expressed in Pseudomonas aeruginosa. MexG is a membrane protein required for drug export; MexH is the membrane fusion protein; MexI is the inner membrane transporter; and MexJ is the outer membrane channel protein. MexGHI-OpmD confers resistance to vanadium, norfloxacin, and acriflavin. http://purl.obolibrary.org/obo/ARO_3000800 MexC http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MexC is the membrane fusion protein of the MexCD-OprJ multidrug efflux complex. http://purl.obolibrary.org/obo/ARO_3000801 MexD http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MexD is the multidrug inner membrane transporter of the MexCD-OprJ complex. http://purl.obolibrary.org/obo/ARO_3000802 OprJ http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance OprJ is the outer membrane channel component of the MexCD-OprJ multidrug efflux complex. http://purl.obolibrary.org/obo/ARO_3000803 MexE http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MexE is the membrane fusion protein of the MexEF-OprN multidrug efflux complex. http://purl.obolibrary.org/obo/ARO_3000804 MexF http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MexF is the multidrug inner membrane transporter of the MexEF-OprN complex. mexF corresponds to 2 loci in Pseudomonas aeruginosa PAO1 (gene name: mexF/mexB) and 4 loci in Pseudomonas aeruginosa LESB58 (gene name: mexD/mexB). http://purl.obolibrary.org/obo/ARO_3000805 OprN http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance OprN is the outer membrane channel component of the MexEF-OprN multidrug efflux complex. http://purl.obolibrary.org/obo/ARO_3000806 MexG http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MexG is a membrane protein required for MexGHI-OpmD efflux activity. http://purl.obolibrary.org/obo/ARO_3000807 MexH http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MexH is the membrane fusion protein of the efflux complex MexGHI-OpmD. http://purl.obolibrary.org/obo/ARO_3000808 MexI http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MexI is the inner membrane transporter of the efflux complex MexGHI-OpmD. http://purl.obolibrary.org/obo/ARO_3000809 OpmD http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance OpmD is the outer membrane channel protein of the efflux complex MexGHI-OpmD. http://purl.obolibrary.org/obo/ARO_3000810 mtrC http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MtrC is the membrane fusion protein of the MtrCDE multidrug efflux complex. http://purl.obolibrary.org/obo/ARO_3000811 mtrD http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MtrD is the inner membrane multidrug transporter of the MtrCDE efflux complex. http://purl.obolibrary.org/obo/ARO_3000812 mtrE http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MtrE is an outer membrane exporter protein that is part of the MtrCDE multidrug efflux complex. http://purl.obolibrary.org/obo/ARO_3000813 MexS http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux MexS is a suppressor of MexT, which is an activator of the multidrug pump MexEF-OprN. Mutations in MexS lead to multidrug resistance. http://purl.obolibrary.org/obo/ARO_3000814 MexT http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux MexT is a LysR-type transcriptional activator that positively regulates the expression of MexEF-OprN, OprD, and MexS. http://purl.obolibrary.org/obo/ARO_3000815 mgrA http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux MgrA, also known as NorR, is a regulator for norA, norB, and tet38. It is a positive regulator for norA expression, but is a direct repressor for norB and an indirect repressor of tet38. http://purl.obolibrary.org/obo/ARO_3000816 mtrA http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux MtrA is a transcriptional activator of the MtrCDE multidrug efflux pump of Neisseria gonorrhoeae. http://purl.obolibrary.org/obo/ARO_3000817 mtrR http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux MtrR is a repressor of mtrCDE expression. Mutations in mtrR increase multidrug resistance. http://purl.obolibrary.org/obo/ARO_3000818 nalC http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux NalC is a repressor of PA3720-PA3719, which are positive regulators of MexAB-OprM. Thus, nalC mutants confer multidrug resistance. http://purl.obolibrary.org/obo/ARO_3000819 nalD http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux NalD is a repressor of MexAB-OprM. Mutations lead to multidrug resistance and MexAB-OprM overexpression. http://purl.obolibrary.org/obo/ARO_3000820 NfxB http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux NfxB is a repressor of the efflux pump mexCD-oprJ and itself (NfxB binds upstream of the nfxB gene and negatively regulates its own expression). Increased expression of MexCD–OprJ brought about by mutations in NfxB. http://purl.obolibrary.org/obo/ARO_3000821 phoPQ http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux PhoPQ is a two-component regulatory system. phoP is phosphorylated by phoQ at a low [mg2+], activating the repressor. Its part of a two component regulating system that activates the PmrA/B system which has downstream effects, leading to Antimicrobial resistance in many pathogens. In Salmonella, phoP bind to macAB ABC transporter and represses it. In Escherichia coli, phoPQ regulates arnA expression. In Pseudomonas aeruginosa, phoPQ regulates OprH expression. phoPQ have other roles in other species. http://purl.obolibrary.org/obo/ARO_3000822 pmrA http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump PmrA is a MFS-type efflux pump expressed in Streptococcus pneumoniae that confers low-level resistance to norfloxacin, ciprofloxacin, and acriflavine. http://purl.obolibrary.org/obo/ARO_3000823 ramA http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux RamA (resistance antibiotic multiple) is a positive regulator of AcrAB-TolC and leads to high level multidrug resistance in Klebsiella pneumoniae, Salmonella enterica, and Enterobacter aerugenes, increasing the expression of both the mar operon as well as AcrAB. RamA also decreases OmpF expression. http://purl.obolibrary.org/obo/ARO_3000824 ramR http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux RamR is a repressor that regulates RamA expression. Mutations lead to the upregulation of AcrAB, which is positively regulated by RamA. http://purl.obolibrary.org/obo/ARO_3000825 rob http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux The robA protein is a positive regulator for the acrAB efflux genes, and is structurally similar to SoxS and MarA. http://purl.obolibrary.org/obo/ARO_3000826 sdiA http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux SdiA is a cell division regulator that is also a positive regulator of AcrAB only when it's expressed from a plasmid. When the sdiA gene is on the chromosome, it has no effect on expression of acrAB. http://purl.obolibrary.org/obo/ARO_3000827 soxRS http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux SoxRS is a two-component regulator part of the superoxide stress response. It is a positive regulator for many multidrug efflux pumps. http://purl.obolibrary.org/obo/ARO_3000828 baeR http://purl.obolibrary.org/obo/ARO_3000750 protein of two-component regulatory system modulating antibiotic efflux BaeR is a response regulator that promotes the expression of MdtABC and AcrD efflux complexes. http://purl.obolibrary.org/obo/ARO_3000829 baeS http://purl.obolibrary.org/obo/ARO_3000750 protein of two-component regulatory system modulating antibiotic efflux BaeS is a sensor kinase in the BaeSR regulatory system. While it phosphorylates BaeR to increase its activity, BaeS is not necessary for overexpressed BaeR to confer resistance. http://purl.obolibrary.org/obo/ARO_3000830 cpxA http://purl.obolibrary.org/obo/ARO_3000750 protein of two-component regulatory system modulating antibiotic efflux CpxA is a membrane-localized sensor kinase that is activated by envelope stress. It starts a kinase cascade that activates CpxR, which promotes efflux complex expression. http://purl.obolibrary.org/obo/ARO_3000831 CpxR http://purl.obolibrary.org/obo/ARO_3000750 protein of two-component regulatory system modulating antibiotic efflux CpxR is a regulator that promotes acrD expression when phosphorylated by a cascade involving CpxA, a sensor kinase. CpxR is also directly involved in activation of expression of RND efflux pump MexAB-OprM in P. aeruginosa. CpxR is required to enhance mexAB-oprM expression and drug resistance, in the absence of repressor MexR. http://purl.obolibrary.org/obo/ARO_3000832 evgA http://purl.obolibrary.org/obo/ARO_3000750 protein of two-component regulatory system modulating antibiotic efflux EvgA, when phosphorylated, is a positive regulator for efflux protein complexes emrKY and mdtEF. While usually phosphorylated in a EvgS dependent manner, it can be phosphorylated in the absence of EvgS when overexpressed. http://purl.obolibrary.org/obo/ARO_3000833 evgS http://purl.obolibrary.org/obo/ARO_3000750 protein of two-component regulatory system modulating antibiotic efflux EvgS is a sensor protein that phosphorylates the regulatory protein EvgA. evgS corresponds to 1 locus in Pseudomonas aeruginosa PAO1 and 1 locus in Pseudomonas aeruginosa LESB58. http://purl.obolibrary.org/obo/ARO_3000834 phoP http://purl.obolibrary.org/obo/ARO_3000750 protein of two-component regulatory system modulating antibiotic efflux PhoP is a direct repressor of the macAB efflux genes. http://purl.obolibrary.org/obo/ARO_3000835 phoQ http://purl.obolibrary.org/obo/ARO_3000750 protein of two-component regulatory system modulating antibiotic efflux PhoQ is a sensor protein that is induced by low Mg2+ concentrations. When activated, PhoQ donates a phosphate to activate PhoP. http://purl.obolibrary.org/obo/ARO_3000836 soxR http://purl.obolibrary.org/obo/ARO_3000219 mutant efflux regulatory protein conferring antibiotic resistance SoxR is a sensory protein that upregulates soxS expression in the presence of redox-cycling drugs. This stress response leads to the expression many multidrug efflux pumps. In Pseudomonas aeruginosa, which lacks SoxS, SoxR is able to directly upregulate the expression of the MexGHI-OpmD efflux pump. http://purl.obolibrary.org/obo/ARO_3000837 soxS http://purl.obolibrary.org/obo/ARO_3000219 mutant efflux regulatory protein conferring antibiotic resistance SoxS is a global regulator that up-regulates the expression of AcrAB efflux genes. It also reduces OmpF expression to decrease cell membrane permeability. http://purl.obolibrary.org/obo/ARO_3000838 arlR http://purl.obolibrary.org/obo/ARO_3000750 protein of two-component regulatory system modulating antibiotic efflux ArlR is a response regulator that binds to the norA promoter to activate expression. ArlR must first be phosphorylated by ArlS. http://purl.obolibrary.org/obo/ARO_3000839 arlS http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance ArlS is a protein histidine kinase that phosphorylates ArlR, a promoter for norA expression. http://purl.obolibrary.org/obo/ARO_3000840 JOHN-1 http://purl.obolibrary.org/obo/ARO_3004202 JOHN beta-lactamase JOHN-1 is an Ambler class B carbapenem-hydrolysing beta-lactamase from Flavobacterium johnsoniae. http://purl.obolibrary.org/obo/ARO_3000841 CGB-1 http://purl.obolibrary.org/obo/ARO_3004203 CGB beta-lactamase CGB-1 is an Ambler class B beta-lactamase that mediates resistance for carbapenems in Chryseobacterium gleum. http://purl.obolibrary.org/obo/ARO_3000842 EBR-1 http://purl.obolibrary.org/obo/ARO_3004204 EBR beta-lactamase EBR-1 is an Ambler class B beta-lactamase found in Empedobacter brevis and is known to mediate the hydrolysis of penicillins, cephalosporins, and carbapenems efficiently but not aztreonam. http://purl.obolibrary.org/obo/ARO_3000843 MUS-1 http://purl.obolibrary.org/obo/ARO_3004067 MUS beta-lactamase MUS-1 is a chromosome-encoded beta-lactamase from Myroides odoratus and Myroides odoratimimus. http://purl.obolibrary.org/obo/ARO_3000844 TUS-1 http://purl.obolibrary.org/obo/ARO_3004205 TUS beta-lactamase TUS-1 is a chromosome-encoded beta-lactamase from Myroides odoratus and Myroides odoratimimus. http://purl.obolibrary.org/obo/ARO_3000845 GIM-1 http://purl.obolibrary.org/obo/ARO_3003195 GIM beta-lactamase GIM-1 is an integron-encoded B1 beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3000846 SIM-1 http://purl.obolibrary.org/obo/ARO_3004206 SIM beta-lactamase SIM-1 is an integron-encoded Ambler class B beta-lactamase isolated from Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3000847 KHM-1 http://purl.obolibrary.org/obo/ARO_3004207 KHM beta-lactamase KHM-1 is a plasmid-mediated metallo-beta-lactamase found in Citrobacter freundii that confers resistance to all broad-spectrum beta-lactams, execpt for monobactams. http://purl.obolibrary.org/obo/ARO_3000848 DIM-1 http://purl.obolibrary.org/obo/ARO_3004208 DIM beta-lactamase Dutch imipenemase or DIM-1 is an integron-encoded metallo-beta-lactamase from Pseudomonas stutzeri. http://purl.obolibrary.org/obo/ARO_3000849 SFH-1 http://purl.obolibrary.org/obo/ARO_3004210 SFH beta-lactamase SFH-1 confers resistance to carbapenems in Serratia fonticola. http://purl.obolibrary.org/obo/ARO_3000850 GOB-1 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-1 confers resistance to cephalosporins in Elizabethkingia (Chryseobacterium) meningoseptica. http://purl.obolibrary.org/obo/ARO_3000851 THIN-B http://purl.obolibrary.org/obo/ARO_3004214 THIN-B beta-lactamase THIN-B, isolated from Janthinobacterium lividum, hydrolyzes a broad spectrum of beta-lactams including penicillins, cephalosporins, and carbapenems. http://purl.obolibrary.org/obo/ARO_3000853 AIM-1 http://purl.obolibrary.org/obo/ARO_3004216 AIM beta-lactamase AIM-1 is an Ambler class B beta-lactamase that hydrolyzes most beta-lactams except aztreonam and ceftazidime. It was isolated from Pseudomonas aeruginosa and was the first subclass B3 mobile-elements encoded beta-lactamase discovered. http://purl.obolibrary.org/obo/ARO_3000854 SMB-1 http://purl.obolibrary.org/obo/ARO_3004217 SMB beta-lactamase SMB-1 can hydrolyze a variety of beta-lactams, including penicillins, cephalosporins, and carbapenems. It was identified in Serratia marcescens. http://purl.obolibrary.org/obo/ARO_3000855 CAU-1 http://purl.obolibrary.org/obo/ARO_3004218 CAU beta-lactamase CAU-1 is a B3 metallo-beta-lactamase that is encoded by the Caulobacter crescentus chromosome. http://purl.obolibrary.org/obo/ARO_3000856 BJP-1 http://purl.obolibrary.org/obo/ARO_3004219 BJP beta-lactamase BJP-1 is a subclass B3 ortholog found in Bradyrhizobium japonicum that hydrolyzes most beta-lactams except aztreonam, ticarcillin, and temocillin. http://purl.obolibrary.org/obo/ARO_3000857 16S ribosomal RNA methyltransferase http://purl.obolibrary.org/obo/ARO_3000164 rRNA methyltransferase conferring antibiotic resistance Methyltransferases that modify the 16S rRNA of the 30S subunit of bacterial ribosomes, conferring resistance to drugs that target 16S rRNA. http://purl.obolibrary.org/obo/ARO_3000858 armA http://purl.obolibrary.org/obo/ARO_3004271 16S rRNA methyltransferase (G1405) ArmA is a 16S rRNA methyltransferase that targets mature or nearly mature 30S subunits. It transfers a methyl group from S-adenosyl-L-methionine to N7-G1405 of the 16S rRNA, an aminoglycoside binding site. http://purl.obolibrary.org/obo/ARO_3000859 rmtA http://purl.obolibrary.org/obo/ARO_3004271 16S rRNA methyltransferase (G1405) RmtA is a 16S rRNA methyltransferase found in Pseudomonas aeruginosa which methylates G1405 of the 16S rRNA. It confers high level resistance to many aminoglycosides. http://purl.obolibrary.org/obo/ARO_3000860 rmtB http://purl.obolibrary.org/obo/ARO_3004271 16S rRNA methyltransferase (G1405) RmtB is a 16S rRNA methyltransferase that targets mature or nearly mature 30S subunits. It transfers a methyl group from S-adenosyl-L-methionine to N7-G1405 of the 16S rRNA, an aminoglycoside binding site. http://purl.obolibrary.org/obo/ARO_3000861 rmtC http://purl.obolibrary.org/obo/ARO_3004271 16S rRNA methyltransferase (G1405) RmtC is a rRNA methyltransferase found in Proteus mirabilis with high level resistance to similar to aminoglycosides, with the exception of non-4,6-disubstituted deoxystreptamines (streptomycin and neomycin). It has also been isolated in Salmonella enterica ser. Virchow. It is hypothesized to methylate G1405, like related methyltransferases RmtA, RmtB, and ArmA. http://purl.obolibrary.org/obo/ARO_3000862 sgm http://purl.obolibrary.org/obo/ARO_3004271 16S rRNA methyltransferase (G1405) Sgm, or sisomicin-gentamicin methyltransferase, methylates G1405 of 16S rRNA to confer resistance to various aminoglycosides. http://purl.obolibrary.org/obo/ARO_3000863 defensin resistant mprF http://purl.obolibrary.org/obo/ARO_3003421 antibiotic resistant mprF MprF is a integral membrane protein that modifies the negatively-charged phosphatidylglycerol on the membrane surface of both Gram-positive and Gram-negative bacteria. This confers resistance to cationic peptides that disrupt the cell membrane, including defensins. http://purl.obolibrary.org/obo/ARO_3000864 fluoroquinolone resistant gyrB http://purl.obolibrary.org/obo/ARO_3000452 fluoroquinolone resistant DNA topoisomerase Point mutations in DNA gyrase subunit B (gyrB) observed in Mycobacterium tuberculosis can result in resistance to fluoroquinolones. http://purl.obolibrary.org/obo/ARO_3000865 oleD http://purl.obolibrary.org/obo/ARO_3000465 ole glycosyltransferase OleD is a glycotransferase found in Streptomyces antibioticus, a natural producer of oleandomycin. OleD can glycosylate a wide range of macrolides. Unlike oleI, oleD is not found in the oleandomycin biosynthetic cluster. http://purl.obolibrary.org/obo/ARO_3000866 oleI http://purl.obolibrary.org/obo/ARO_3000465 ole glycosyltransferase OleI is a glycosyltransferase found in Streptomyces antibioticus, specifically the oleandomycin biosynthetic cluster. OleI glycosylates oleandomycin to confer self-resistance. http://purl.obolibrary.org/obo/ARO_3000867 oleandomycin http://purl.obolibrary.org/obo/ARO_0000000 macrolide antibiotic Oleandomycin is a 14-membered macrolide produced by Streptomyces antibioticus. It is ssimilar to erythromycin, and contains a desosamine amino sugar and an oleandrose sugar. It targets the 50S ribosomal subunit to prevent protein synthesis. http://purl.obolibrary.org/obo/ARO_3000869 streptothricin acetyltransferase (SAT) http://purl.obolibrary.org/obo/ARO_3000557 antibiotic inactivation enzyme AcetylCoA dependent acetyltransferase that acetylate streptothricins such as nourseothricin at position 16 (beta position of beta-lysine). http://purl.obolibrary.org/obo/ARO_3000870 triclosan http://purl.obolibrary.org/obo/ARO_3005386 disinfecting agents and antiseptics Triclosan is a common antibacterial agent added to many consumer products as a biocide. It is an inhibitor of fatty acid biosynthesis by blocking enoyl-carrier protein reductase (FabI). http://purl.obolibrary.org/obo/ARO_3000871 fatty acid synthesis enzyme targeted by antibiotic http://purl.obolibrary.org/obo/ARO_3000708 antibiotic target Antibiotics can target bacteria-specific fatty acid biosynthesis enzymes. http://purl.obolibrary.org/obo/ARO_3000872 antibiotic sensitive enoyl-acyl carrier reductase http://purl.obolibrary.org/obo/ARO_3000871 fatty acid synthesis enzyme targeted by antibiotic Enoyl-acyl carrier reductases catalyze the final enoyl reduction step in bacterial type II fatty acid elongation. Triclosan antibiotics block enoyl reduction and therefore fatty acid synthesis, functioning as a broad spectrum biocide and antibiotic. http://purl.obolibrary.org/obo/ARO_3000873 TEM-1 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-1 is a broad-spectrum beta-lactamase found in many Gram-negative bacteria. Confers resistance to penicillins and first generation cephalosphorins. http://purl.obolibrary.org/obo/ARO_3000874 TEM-2 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-2 is a broad-spectrum beta-lactamase. http://purl.obolibrary.org/obo/ARO_3000875 TEM-3 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-3 is an extended-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3000876 TEM-4 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-4 is an extended-spectrum beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3000877 TEM-5 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-5 is an extended-spectrum beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3000878 TEM-6 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-6 is an extended-spectrum beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3000879 TEM-7 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-7 is an extended-spectrum beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3000880 TEM-8 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-8 is an extended-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3000881 TEM-9 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-9 is an extended-spectrum beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3000882 TEM-10 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-10 is an extended-spectrum beta-lactamase round in Morganella morganii. http://purl.obolibrary.org/obo/ARO_3000883 TEM-11 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-11 is an extended-spectrum beta-lactamase found in Proteus mirabilis. http://purl.obolibrary.org/obo/ARO_3000884 TEM-12 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-12 is an extended-spectrum beta-lactamase found in Klebsiella oxytoca. http://purl.obolibrary.org/obo/ARO_3000885 TEM-13 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-13 is a broad-spectrum beta-lactamase that has been found in clinical isolates. Sequence data unavailable. http://purl.obolibrary.org/obo/ARO_3000886 TEM-15 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-15 is an extended-spectrum beta-lactamase that has been found in Haemophilus parainfluenzae. http://purl.obolibrary.org/obo/ARO_3000887 TEM-16 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-16 is an extended-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3000888 TEM-17 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-17 is an extended-spectrum beta-lactamase found in Capnocytophaga ochracea. http://purl.obolibrary.org/obo/ARO_3000889 TEM-18 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase The beta-lactamase name TEM-18 has been depreciated. http://purl.obolibrary.org/obo/ARO_3000890 TEM-19 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-19 is an extended-spectrum beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3000891 TEM-20 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-20 is an extended-spectrum beta-lactamase found in several species of Gram-negative bacteria. http://purl.obolibrary.org/obo/ARO_3000892 TEM-21 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-21 is an extended-spectrum beta-lactamase found in many species of Gram-negative bacteria. http://purl.obolibrary.org/obo/ARO_3000893 TEM-22 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-22 is an extended-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3000894 TEM-24 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-24 is an extended-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3000895 TEM-25 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-25 is an extended-spectrum beta-lactamase that has been found in clinical isolates. Sequence data unavailable. http://purl.obolibrary.org/obo/ARO_3000896 TEM-26 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-26 is an extended-spectrum beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3000897 TEM-27 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-27 is an extended-spectrum beta-lactamase that has been found in clinical isolates. Sequence data unavailable. http://purl.obolibrary.org/obo/ARO_3000898 TEM-28 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-28 is an extended-spectrum beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3000899 TEM-29 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-29 is an extended-spectrum beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3000900 TEM-30 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-30 is an inhibitor-resistant beta-lactamase found in E. coli. Confers resistance to amoxycilllin-clavulanic acid, ticarcillin-clavulanic acid, kanamycin, neomycin, and intermediate resistance to mezlocillin and piperacillin. http://purl.obolibrary.org/obo/ARO_3000901 TEM-31 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-31 is an inhibitor-resistant beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3000902 TEM-32 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-32 is an inhibitor-resistant beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3000903 TEM-33 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-33 is an inhibitor-resistant beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3000904 TEM-34 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-34 is an inhibitor-resistant beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3000905 TEM-35 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-35 is an inhibitor-resistant beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3000906 TEM-36 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-36 is an inhibitor-resistant beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3000907 TEM-37 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-37 is an inhibitor-resistant beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3000908 TEM-38 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-38 is an inhibitor-resistant beta-lactamase that has been found in clinical isolates. Sequence data unavailable. http://purl.obolibrary.org/obo/ARO_3000909 TEM-39 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-39 is an inhibitor-resistant beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3000910 TEM-40 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-40 is an inhibitor-resistant beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3000911 TEM-42 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-42 is an extended-spectrum beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3000912 TEM-43 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-43 is an extended-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3000913 TEM-44 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-44 is an inhibitor-resistant beta-lactamase that has been found in clinical isolates. Sequence data unavailable. http://purl.obolibrary.org/obo/ARO_3000914 TEM-45 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-45 is an inhibitor-resistant beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3000915 TEM-46 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-46 is an extended-spectrum beta-lactamase that has been found in clinical isolates. Sequence data unavailable. http://purl.obolibrary.org/obo/ARO_3000916 TEM-47 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-47 is an extended-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3000917 TEM-48 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-48 is an extended-spectrum beta-lactamase found Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3000918 TEM-49 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-49 extended-spectrum beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3000919 TEM-50 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-50 is an inhibitor-resistant, extended-spectrum beta-lactamase that has been found in clinical isolates. Sequence data unavailable. http://purl.obolibrary.org/obo/ARO_3000920 TEM-51 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-51 is an inhibitor-resistant beta-lactamase that has been found in clinical isolates. Sequence data unavailable. http://purl.obolibrary.org/obo/ARO_3000921 TEM-52 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-52 is an extended-spectrum beta-lactamase found in Klebsiella pneumoniae and Salmonella enterica. http://purl.obolibrary.org/obo/ARO_3000922 TEM-53 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-53 is an extended-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3000923 TEM-54 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-54 is an inhibitor-resistant beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3000924 TEM-55 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-55 is a broad-spectrum beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3000925 TEM-56 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-56 is an extended-spectrum beta-lactamase that has been found in clinical isolates. Sequence data unavailable. http://purl.obolibrary.org/obo/ARO_3000926 TEM-57 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-57 is a broad-spectrum beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3000927 TEM-58 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-58 is an inhibitor-resistant beta-lactamase that has been found in clinical isolates. Sequence data unavailable. http://purl.obolibrary.org/obo/ARO_3000928 TEM-59 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-59 is an inhibitor-resistant beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3000929 TEM-60 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-60 is an extended-spectrum beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3000930 TEM-61 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-61 is an extended-spectrum beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3000931 TEM-63 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-63 is an extended-spectrum beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3000932 TEM-65 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-65 is an inhibitor-resistant beta-lactamase that has been found in clinical isolates. Sequence data unavailable. http://purl.obolibrary.org/obo/ARO_3000933 TEM-66 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-66 is an extended-spectrum beta-lactamase that has been found in clinical isolates. Sequence data unavailable. http://purl.obolibrary.org/obo/ARO_3000934 TEM-67 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-67 is an inhibitor-resistant beta-lactamase found in Proteus mirabilis. http://purl.obolibrary.org/obo/ARO_3000935 TEM-68 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-68 is an inhibitor resistant, extended-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3000936 TEM-70 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-70 is a beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3000937 TEM-71 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-71 is an extended-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3000938 TEM-72 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-72 is an extended-spectrum beta-lactamase found in Proteus mirabilis and Morganella morganii. http://purl.obolibrary.org/obo/ARO_3000939 TEM-73 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-73 is an inhibitor-resistant beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3000940 TEM-74 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-74 is an inhibitor-resistant beta-lactamase that has been found in clinical isolates. Sequence data unavailable. http://purl.obolibrary.org/obo/ARO_3000941 TEM-75 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-75 is an extended-spectrum beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3000942 TEM-76 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-76 is an inhibitor-resistant beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3000944 TEM-78 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-78 is an inhibitor-resistant beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3000946 TEM-79 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-79 is an inhibitor-resistant beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3000947 TEM-80 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-80 is an inhibitor-resistant beta-lactamase found in Enterobacter cloacae. http://purl.obolibrary.org/obo/ARO_3000948 TEM-81 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-81 is an inhibitor-resistant beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3000949 TEM-82 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-82 is an inhibitor-resistant beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3000950 TEM-83 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-83 is an inhibitor-resistant beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3000951 TEM-84 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-84 is an inhibitor-resistant beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3000952 TEM-85 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-85 is an extended-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3000953 TEM-86 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-86 is an extended-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3000954 TEM-87 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-87 is an extended-spectrum beta-lactamase found in Proteus mirabilis. http://purl.obolibrary.org/obo/ARO_3000955 TEM-88 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-88 is an extended-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3000956 TEM-89 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-89 is an inhibitor-resistant, extended-spectrum beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3000957 TEM-90 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-90 is a broad-spectrum beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3000958 TEM-91 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-91 is an extended-spectrum beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3000959 TEM-92 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-92 is an extended-spectrum beta-lactamase found in Proteus mirabilis. http://purl.obolibrary.org/obo/ARO_3000960 TEM-93 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-93 is an extended-spectrum beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3000961 TEM-94 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-94 is an extended-spectrum beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3000962 TEM-95 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-95 is a broad-spectrum beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3000963 TEM-96 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-96 is a beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3000964 TEM-101 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-101 is an extended-spectrum beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3000965 TEM-102 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-102 is an extended-spectrum beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3000966 TEM-103 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-103 is an inhibitor-resistant beta-lactamase that has been found in E. coli. http://purl.obolibrary.org/obo/ARO_3000967 TEM-104 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-104 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3000968 TEM-105 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-105 is a beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3000969 TEM-106 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-106 is an extended-spectrum beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3000970 TEM-107 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-107 is an extended-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3000971 TEM-108 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-108 is a beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3000972 TEM-109 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-109 is an inhibitor-resistant, extended-spectrum beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3000973 TEM-110 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-110 is a broad-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3000974 TEM-111 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-111 is a beta-lactamase found in E. coli and P. mirabilis. http://purl.obolibrary.org/obo/ARO_3000975 TEM-112 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-112 is an extended-spectrum beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3000976 TEM-113 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-113 is an extended-spectrum beta-lactamase found in Proteus mirabilis. http://purl.obolibrary.org/obo/ARO_3000977 TEM-114 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-114 is an extended-spectrum beta-lactamase found in Klebsiella aerogenes. http://purl.obolibrary.org/obo/ARO_3000978 TEM-115 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-115 is an extended-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3000979 TEM-116 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-116 is a broad-spectrum beta-lactamase found in many species of bacteria. http://purl.obolibrary.org/obo/ARO_3000980 TEM-117 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-117 is a beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3000981 TEM-118 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-118 is an extended-spectrum beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3000982 TEM-120 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-120 is an extended-spectrum beta-lactamase found in Klebsiella oxytoca. http://purl.obolibrary.org/obo/ARO_3000983 TEM-121 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-121 is an inhibitor-resistant, extended-spectrum beta-lactamase found in E. coli and Klebsiella aerogenes. http://purl.obolibrary.org/obo/ARO_3000984 TEM-122 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-122 is an inhibitor-resistant beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3000985 TEM-123 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-123 is an extended-spectrum beta-lactamase found in Proteus mirabilis. http://purl.obolibrary.org/obo/ARO_3000986 TEM-124 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-124 is an extended-spectrum beta-lactamase found in Morganella morganii. http://purl.obolibrary.org/obo/ARO_3000987 TEM-125 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-125 is a CMT-type, inhibitor-resistant, extended-spectrum beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3000988 TEM-126 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-126 is an extended-spectrum beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3000989 TEM-127 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-127 is a broad-spectrum beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3000990 TEM-128 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-128 is a broad-spectrum beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3000993 TEM-129 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-129 is an extended-spectrum beta-lactamase found in Klebsiella oxytoca. http://purl.obolibrary.org/obo/ARO_3000994 TEM-130 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-130 is an extended-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3000995 TEM-131 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-131 is an extended-spectrum beta-lactamase found in Salmonella enterica. http://purl.obolibrary.org/obo/ARO_3000996 TEM-132 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-132 is an extended-spectrum beta-lactamase found in E. coli and Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3000997 TEM-133 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-133 is an extended-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3000998 TEM-134 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-134 is an extended-spectrum beta-lactamase found in Citrobacter koseri. http://purl.obolibrary.org/obo/ARO_3000999 TEM-135 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-135 is a broad-spectrum beta-lactamase found in Salmonella enterica. http://purl.obolibrary.org/obo/ARO_3001000 TEM-136 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-136 is an extended-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001001 TEM-137 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-137 is an extended-spectrum beta-lactamase found in Shigella sonnei. http://purl.obolibrary.org/obo/ARO_3001002 TEM-138 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-138 is an extended-spectrum beta-lactamase found in Salmonella enterica. http://purl.obolibrary.org/obo/ARO_3001003 TEM-139 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-139 is an extended-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001004 TEM-141 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-141 is a broad-spectrum beta-lactamase found in Enterobacter cloacae. http://purl.obolibrary.org/obo/ARO_3001005 TEM-142 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-142 is an beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3001006 TEM-143 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-143 is an extended-spectrum beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3001007 TEM-144 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-144 is an extended-spectrum beta-lactamase found in Salmonella enterica. http://purl.obolibrary.org/obo/ARO_3001012 TEM-145 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-145 is an inhibitor-resistant beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3001013 TEM-146 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-146 is a beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3001014 TEM-147 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-147 is an extended-spectrum beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3001015 TEM-148 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-148 is a TEM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001016 TEM-149 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-149 is an extended-spectrum beta-lactamase found in Klebsiella aerogenes. http://purl.obolibrary.org/obo/ARO_3001017 TEM-150 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-150 is a beta-lactamase found in Enterobacter spp., E. coli, and Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001018 TEM-151 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-151 is a CMT-type, inhibitor-resistant, extended-spectrum beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3001019 TEM-152 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-152 is a CMT-type, inhibitor-resistant, extended-spectrum beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3001020 TEM-154 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-154 is a CMT-type, inhibitor-resistant, extended-spectrum beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001021 TEM-155 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-155 is an extended-spectrum beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001022 TEM-156 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-156 is a TEM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001023 TEM-157 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-157 is an extended-spectrum beta-lactamase found in Enterobacter cloacae. http://purl.obolibrary.org/obo/ARO_3001024 TEM-158 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-158 is an inhibitor-resistant, extended-spectrum beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3001025 TEM-159 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-159 is an inhibitor-resistant beta-lactamase found in Proteus mirabilis. http://purl.obolibrary.org/obo/ARO_3001026 TEM-160 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-160 is an inhibitor-resistant beta-lactamase found in Proteus mirabilis. http://purl.obolibrary.org/obo/ARO_3001027 TEM-161 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase The beta-lactamase name TEM-161 has been depreciated. http://purl.obolibrary.org/obo/ARO_3001028 TEM-162 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-162 is a beta-lactamase found in Acinetobacter haemolyticus. http://purl.obolibrary.org/obo/ARO_3001029 TEM-163 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-163 is an inhibitor resistant beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3001030 TEM-164 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-164 is an extended-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001031 TEM-165 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-165 is a beta-lactamase that has been found in clinical isolates. Sequence data unavailable. http://purl.obolibrary.org/obo/ARO_3001032 TEM-166 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-166 is a beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3001033 TEM-167 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-167 is an extended-spectrum beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3001034 TEM-168 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-168 is an extended-spectrum beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001035 TEM-169 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-169 is an extended spectrum beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001036 TEM-170 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-170 is a beta-lactamase. Sequence data unavailable. http://purl.obolibrary.org/obo/ARO_3001037 TEM-171 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-171 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001038 TEM-172 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-172 is a beta-lactamase. Sequence data unavailable. http://purl.obolibrary.org/obo/ARO_3001039 TEM-173 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-173 is a beta-lactamase. Sequence data unavailable. http://purl.obolibrary.org/obo/ARO_3001040 TEM-174 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-174 is a beta-lactamase. Sequence data unavailable. http://purl.obolibrary.org/obo/ARO_3001041 TEM-176 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-176 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001042 TEM-177 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-177 is an extended-spectrum beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001043 TEM-178 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-178 is an inhibitor-resistant, extended-spectrum beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001044 TEM-181 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-181 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001045 TEM-183 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-183 is a broad-spectrum beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001046 TEM-186 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-186 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001047 TEM-187 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-187 is an extended-spectrum beta-lactamase found in P. mirabilis. http://purl.obolibrary.org/obo/ARO_3001048 TEM-188 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-188 is an extended-spectrum beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001049 TEM-189 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-189 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001050 TEM-190 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-190 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001051 TEM-191 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-191 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001052 TEM-192 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-192 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001053 TEM-193 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-193 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001054 TEM-194 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-194 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001055 TEM-195 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-195 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001056 TEM-197 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-197 is an extended-spectrum beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001057 TEM-198 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-198 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001058 TEM-199 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-199 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001059 SHV-1 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-1 is a broad-spectrum beta-lactamase found in Klebsiella spp., as well as Acinetobacter spp., E. coli., Raoultella terrigena, and Yersinia pestis. http://purl.obolibrary.org/obo/ARO_3001060 SHV-2 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-2 is an extended-spectrum beta-lactamase found in E. coli., Klebsiella pneumoniae, and Shigella flexneri. http://purl.obolibrary.org/obo/ARO_3001061 SHV-2A http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-2A is an extended-spectrum beta-lactamase found in Enterobacter cloacae, Klebsiella pneumoniae, Pseudomonas aeruginosa, and Salmonella enterica. http://purl.obolibrary.org/obo/ARO_3001062 SHV-3 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-3 is an extended-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001063 SHV-4 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-4 is an extended-spectrum beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3001064 SHV-5 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-5 is an extended-spectrum beta-lactamase found in Acinetobacter baumannii, Enterobacter cloacae, E. coli, Klebsiella pneumoniae, Pseudomonas aeruginosa, and Salmonella enterica. http://purl.obolibrary.org/obo/ARO_3001065 SHV-6 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-6 is an extended-spectrum beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3001066 SHV-7 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-7 is an extended-spectrum beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3001067 SHV-8 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-8 is an extended-spectrum beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3001068 SHV-9 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-9 is an extended-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001069 SHV-10 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-10 is an inhibitor-resistant beta-lactamase that has been found in clinical isolates. Sequence data unavailable. http://purl.obolibrary.org/obo/ARO_3001070 SHV-11 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-11 is a broad-spectrum beta-lactamase found in E. coli, Klebsiella pneumoniae, Proteus mirabilis, and Shigella dysenteriae. http://purl.obolibrary.org/obo/ARO_3001071 SHV-12 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-12 is an extended-spectrum beta-lactamase found in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3001072 SHV-13 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-13 is an extended-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001073 SHV-14 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-14 is an broad-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001074 SHV-15 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-15 is an extended-spectrum beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3001075 SHV-16 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-16 is an extended-spectrum beta-lactamase that has been found in clinical isolates. It differs from SHV-1 by a 163DRWET167 insertion. http://purl.obolibrary.org/obo/ARO_3001076 SHV-18 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-18 is an extended-spectrum beta-lactamase found in Acinetobacter baumannii and Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001077 SHV-19 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-19 is a broad-spectrum beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3001078 SHV-20 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-20 is a broad-spectrum beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3001079 SHV-21 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-21 is a broad-spectrum beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3001080 SHV-22 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-22 is a broad-spectrum beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3001081 SHV-23 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-23 is an extended-spectrum beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3001082 SHV-24 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-24 is an extended-spectrum beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3001083 SHV-25 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-25 is a broad-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001084 SHV-26 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-26 is an inhibitor-resistant beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001085 SHV-27 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-27 is an extended-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001086 SHV-28 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-28 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001087 SHV-29 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-29 is an extended-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001088 SHV-30 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-30 is an extended-spectrum beta-lactamase found in Enterobacter cloacae. http://purl.obolibrary.org/obo/ARO_3001089 SHV-31 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-31 is an extended-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001090 SHV-32 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-32 is a broad-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001091 SHV-33 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-33 is an broad-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001092 SHV-34 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-34 is an extended-spectrum beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3001093 SHV-35 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-35 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001094 SHV-36 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-36 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001095 SHV-37 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-37 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001096 SHV-38 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-38 is an extended-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001097 SHV-39 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-39 is an extended-spectrum beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3001098 SHV-40 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-40 is an extended-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001099 SHV-41 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-41 is an extended-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001100 SHV-42 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-42 is an extended-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001101 SHV-43 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-43 is a broad-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001102 SHV-44 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-44 is a broad-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001103 SHV-45 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-45 is an extended-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001104 SHV-46 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-46 is an extended-spectrum beta-lactamase found in Klebsiella oxytoca. http://purl.obolibrary.org/obo/ARO_3001105 SHV-48 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-48 is a broad-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001106 SHV-49 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-49 is an inhibitor-resistant beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001107 SHV-50 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-50 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001108 SHV-51 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-51 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001109 SHV-52 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-52 is a beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3001110 SHV-53 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-53 is a beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3001111 SHV-55 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-55 is an extended-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001112 SHV-56 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-56 is an inhibitor-resistant beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001113 SHV-57 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-57 is an extended-spectrum beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3001114 SHV-59 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-59 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001115 SHV-60 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-60 is a broad-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001116 SHV-61 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-61 is a broad-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001117 SHV-62 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-62 is a broad-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001118 SHV-63 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-63 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001119 SHV-64 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-64 is an extended-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001120 SHV-65 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-65 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001121 SHV-66 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-66 is an extended-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001122 SHV-67 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-67 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001123 SHV-69 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-69 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001124 SHV-70 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-70 is an extended-spectrum beta-lactamase found in Enterobacter cloacae. http://purl.obolibrary.org/obo/ARO_3001125 SHV-71 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-71 is a broad-spectrum beta-lactamase found in Klebsiella pneumoniae and Shigella. http://purl.obolibrary.org/obo/ARO_3001126 SHV-72 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-72 is an inhibitor-resistant beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001127 SHV-73 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-73 is a broad-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001128 SHV-74 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-74 is a broad-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001129 SHV-75 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-75 is a broad-spectrum beta-lactamase that is found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3001130 SHV-76 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-76 is a broad-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001131 SHV-77 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-77 is a broad-spectrum beta-lactamase found in Klebsiella pneumoniae and E. coli. http://purl.obolibrary.org/obo/ARO_3001132 SHV-78 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-78 is a broad-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001133 SHV-79 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-79 is a broad-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001134 SHV-80 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-80 is a broad-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001135 SHV-81 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-81 is a broad-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001136 SHV-82 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-82 is a broad-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001137 SHV-83 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-83 is a broad-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001138 SHV-84 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-84 is an inhibitor-resistant beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3001139 SHV-85 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-85 is a broad-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001140 SHV-86 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-86 is an extended-spectrum beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3001141 SHV-89 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-89 is a broad-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001142 SHV-90 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-90 is an extended-spectrum beta-lactamase that has been found in clinical isolates. Sequence data unavailable. http://purl.obolibrary.org/obo/ARO_3001143 SHV-91 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-91 is an extended-spectrum beta-lactamase that has been found in clinical isolates. Sequence data unavailable. http://purl.obolibrary.org/obo/ARO_3001144 SHV-92 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-92 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001145 SHV-93 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-93 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001146 SHV-94 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-94 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001147 SHV-95 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-95 is a beta-lactamase found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3001148 SHV-96 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-96 is a beta-lactamase found in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3001149 SHV-97 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-97 is a beta-lactamase found in Enterococcus faecalis. http://purl.obolibrary.org/obo/ARO_3001150 SHV-101 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-101 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001151 SHV-102 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-102 is an extended spectrum beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3001152 SHV-103 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-103 is a beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3001153 SHV-104 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-104 is an extended-spectrum beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3001154 SHV-105 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-105 is an extended-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001155 SHV-106 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-106 is an extended-spectrum beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3001156 SHV-107 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-107 is an inhibitor-resistant beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001157 SHV-108 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-108 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001158 SHV-109 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-109 is a broad-spectrum beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001159 SHV-110 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-110 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001160 SHV-111 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-111 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001161 SHV-112 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-112 is a beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3001162 SHV-113 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase The beta-lactamase name SHV-113 has been depreciated. http://purl.obolibrary.org/obo/ARO_3001163 SHV-114 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase The beta-lactamase name SHV-114 has been depreciated. http://purl.obolibrary.org/obo/ARO_3001164 SHV-115 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-115 is an extended-spectrum beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3001165 SHV-116 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-116 is a beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3001166 SHV-117 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase The beta-lactamase name SHV-117 has been depreciated. http://purl.obolibrary.org/obo/ARO_3001167 SHV-120 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-120 is a beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3001168 SHV-121 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-121 is a beta-lactamase that has been found in clinical isolates. Identical to SHV-136. http://purl.obolibrary.org/obo/ARO_3001169 SHV-122 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-122 is a beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3001170 SHV-123 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-123 is a beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3001171 SHV-124 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-124 is a beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3001172 SHV-125 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-125 is a beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3001173 SHV-126 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-126 is a beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3001174 SHV-127 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-127 is a beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3001175 SHV-128 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-128 is an extended-spectrum beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3001176 SHV-129 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-129 is an extended-spectrum beta-lactamase that has been found in clinical isolates. http://purl.obolibrary.org/obo/ARO_3001177 SHV-133 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-133 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001178 SHV-134 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-134 is an extended-spectrum beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001179 SHV-135 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-135 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001181 SHV-137 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-137 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001182 SHV-140 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-140 is a broad-spectrum beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001183 SHV-141 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-141 is a broad-spectrum beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001184 SHV-142 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-142 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001185 SHV-145 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-145 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001186 SHV-147 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-147 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001187 SHV-148 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-148 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001188 SHV-149 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-149 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001189 SHV-150 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-150 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001190 SHV-151 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-151 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001191 SHV-152 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-152 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001192 SHV-153 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-153 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001193 SHV-154 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-154 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001194 SHV-155 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-155 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001195 SHV-156 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-156 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001196 SHV-157 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-157 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001197 SHV-158 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-158 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001198 SHV-159 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-159 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001199 SHV-160 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-160 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001200 SHV-161 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-161 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001201 SHV-162 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-162 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001202 SHV-163 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-163 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001203 SHV-165 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-165 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001204 SHV-167 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-167 is a beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001205 BRP(MBL) http://purl.obolibrary.org/obo/ARO_3004256 Bleomycin resistant protein A novel bleomycin resistance protein encoded by a metallo-beta-lactamase-associated ble gene. Expression of BRP(MBL) confers resistance to bleomycin and bleomycin-like antibiotics in Enterobacteriaceae and Acinetobacter, where it is co-expressed with an MBL and controlled by the same promoter region. http://purl.obolibrary.org/obo/ARO_3001206 antibiotic inactivation by sequestration http://purl.obolibrary.org/obo/ARO_0001004 antibiotic inactivation Inactivation of an antibiotic by formation of a complex, preventing interaction of the antibiotic with its target. http://purl.obolibrary.org/obo/ARO_3001207 gene involved in antibiotic sequestration http://purl.obolibrary.org/obo/ARO_3000000 determinant of antibiotic resistance A gene whose product inactivates an antibiotic by formation of a complex, preventing interaction of the antibiotic with its target. http://purl.obolibrary.org/obo/ARO_3001208 methicillin resistant PBP2 http://purl.obolibrary.org/obo/ARO_3003040 beta-lactam resistant penicillin-binding proteins In methicillin sensitive S. aureus (MSSA), beta-lactams bind to native penicillin-binding proteins (PBPs) and disrupt synthesis of the cell membrane's peptidoglycan layer. In methicillin resistant S. aureus (MRSA), foreign PBP2a acquired by lateral gene transfer is able to perform peptidoglycan synthesis in the presence of beta-lactams. http://purl.obolibrary.org/obo/ARO_3001209 mecC http://purl.obolibrary.org/obo/ARO_3001208 methicillin resistant PBP2 A foreign PBP2a acquired by lateral gene transfer that able to perform peptidoglycan synthesis in the presence of beta-lactams. http://purl.obolibrary.org/obo/ARO_3001214 mdtM http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump Multidrug resistance protein MdtM. http://purl.obolibrary.org/obo/ARO_3001216 mdtH http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump Multidrug resistance protein MdtH. http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr http://purl.obolibrary.org/obo/ARO_3003425 antibiotic resistant dihydrofolate reductase Alternative dihydropteroate synthase dfr present on plasmids produces alternate proteins that are less sensitive to trimethoprim from inhibiting its role in folate synthesis, thus conferring trimethoprim resistance. http://purl.obolibrary.org/obo/ARO_3001219 elfamycin antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule Elfamycins are molecules that inhibit bacterial elongation factor Tu (EF-Tu), a key protein which brings aminoacyl-tRNA (aa-tRNA) to the ribosome during protein synthesis. Elfamycins defined by their target (EF-Tu), rather than a conserved chemical backbone. Elfamycins follow two mechanisms to disrupt protein synthesis: 1. kirromycins and enacyloxin fix EF-Tu in the GTP bound conformation and lock EF-Tu onto the ribosome, and 2. pulvomycin and GE2270 cover the binding site of aa-tRNA disallowing EF-Tu from being charged with aa-tRNA. All elfamycins cause increased the affinity of EF-Tu for GTP. http://purl.obolibrary.org/obo/ARO_3001220 factumycin http://purl.obolibrary.org/obo/ARO_3001310 kirromycin-like antibiotics Factumycin is a kirromycin-like antibiotic produced by Kitasatospora setae and Streptomyces strains. Its biosynthetic cluster has been characterized which has interesting acetyl transferase domains in trans, or outside of the polyketide synthase domains. Factumycin has specific, rather than broad spectrum, antibacterial properties, especially targeting various Acinetobacter baumanii strains. http://purl.obolibrary.org/obo/ARO_3001221 josamycin http://purl.obolibrary.org/obo/ARO_0000000 macrolide antibiotic A macrolide antibiotic from Streptomyces narbonensis subsp. josamyceticus. The drug has antimicrobial activity against a wide spectrum of pathogens. http://purl.obolibrary.org/obo/ARO_3001222 chalcomycin http://purl.obolibrary.org/obo/ARO_0000000 macrolide antibiotic Produced by Streptomyces bikiniensis. http://purl.obolibrary.org/obo/ARO_3001223 midecamycin http://purl.obolibrary.org/obo/ARO_0000000 macrolide antibiotic Produced by Streptomyces mycarofaciens. http://purl.obolibrary.org/obo/ARO_3001224 mycinamicin http://purl.obolibrary.org/obo/ARO_0000000 macrolide antibiotic Produced by Micromonospora griseorubida. http://purl.obolibrary.org/obo/ARO_3001225 megalomycin http://purl.obolibrary.org/obo/ARO_0000000 macrolide antibiotic Produced by Micromonospora megalomicia. http://purl.obolibrary.org/obo/ARO_3001226 narbomycin http://purl.obolibrary.org/obo/ARO_0000000 macrolide antibiotic Produced by Streptomyces narbonensis. http://purl.obolibrary.org/obo/ARO_3001227 kitasamycin http://purl.obolibrary.org/obo/ARO_0000000 macrolide antibiotic Kitasamycin is a macrolide antibiotic and is produced by Streptoverticillium kitasatoense. The drug has antimicrobial activity against a wide spectrum of pathogens. http://purl.obolibrary.org/obo/ARO_3001228 carbomycin http://purl.obolibrary.org/obo/ARO_0000000 macrolide antibiotic Produced by Streptomyces halstedii and Streptomyces thermotolerans. http://purl.obolibrary.org/obo/ARO_3001229 rosaramicin http://purl.obolibrary.org/obo/ARO_0000000 macrolide antibiotic Produced by Micromonospora rosaria. http://purl.obolibrary.org/obo/ARO_3001230 niddamycin http://purl.obolibrary.org/obo/ARO_0000000 macrolide antibiotic Produced by Streptomyces caelestis. http://purl.obolibrary.org/obo/ARO_3001231 celesticetin http://purl.obolibrary.org/obo/ARO_0000017 lincosamide antibiotic Produced by Streptomyces caelestis, which also produces the macrolide niddamycin. http://purl.obolibrary.org/obo/ARO_3001232 methymycin http://purl.obolibrary.org/obo/ARO_0000000 macrolide antibiotic Produced by Streptomyces venezuelae ATCC 15439. http://purl.obolibrary.org/obo/ARO_3001233 pikromycin http://purl.obolibrary.org/obo/ARO_0000000 macrolide antibiotic Produced by Streptomyces venezuelae ATCC 15439. http://purl.obolibrary.org/obo/ARO_3001234 kirromycin http://purl.obolibrary.org/obo/ARO_3001310 kirromycin-like antibiotics Kirromycin, also known as mocimycin, is the representative molecule of its own class of elfamycins which is composed of more than 10 analogs. Kirromycin binds to the domain 1,2 interface of elongation factor Tu. This interaction maintains the EF-Tu*GTP conformation even after GTP is hydrolyzed to GDP. EF-Tu*GDP normally releases aa-tRNA and then exits the ribosome; however, kirromycin*EF-Tu*GDP*aa-tRNA forms a strong complex and remains bound to the ribosome, prohibits translocation of the peptide chain and translation is halted. http://purl.obolibrary.org/obo/ARO_3001235 aurodox http://purl.obolibrary.org/obo/ARO_3001310 kirromycin-like antibiotics Aurodox is an elongation factor Tu inhibiting antibiotic. It was first referred to as X-5108. It is produced by Streptomyces goldiniensis var. goldiniensis and is active primarily against gram-positive bacteria. http://purl.obolibrary.org/obo/ARO_3001236 efrotomycin http://purl.obolibrary.org/obo/ARO_3001310 kirromycin-like antibiotics Efrotomycin is produced by Streptomyces lactamodurans NRRL 3802. This kirromycin-like antibiotic is used in animal agriculture, especially in the production of swine. Generally gram negative bacteria are susceptible to efrotomycin, while gram positive bacteria are resistant. http://purl.obolibrary.org/obo/ARO_3001237 GE2270A http://purl.obolibrary.org/obo/ARO_3001309 cyclic thiazolyl peptide elfamycin GE2270A is the model molecule of cyclic thiazolyl peptide elfamycins. GE2270A is produced by Planobispora rosea. Biosynthesis of the molecule has been shown to originate as a ribosomally synthesized peptide that undergoes significant post-translational modification. Clinical use of cyclic thiazolyl peptides is hindered by their low water solubility and bioavailability. http://purl.obolibrary.org/obo/ARO_3001242 enacyloxin IIa http://purl.obolibrary.org/obo/ARO_3001219 elfamycin antibiotic Enacyloxin IIa is structurally distinct but acts in a similar mechanism to kirromycin-like elfamycins. It prohibits the transfer of the amino acid at the A site to the elongating peptide chain. It is most likely that the mechanism of action is that EF-Tu*GDP is locked in the EF-Tu*GTP form, and EF-Tu*GDP*aa-tRNA is immobilized on the ribosome. It is an open question whether enacyloxin IIa actually belongs to the kirromycin-like group of elfamycins due to their high similarity. http://purl.obolibrary.org/obo/ARO_3001246 kirrothricin http://purl.obolibrary.org/obo/ARO_3001310 kirromycin-like antibiotics Kirrothricin is produced by Streptomyces cinnamoneus and is structurally related to kirromycin, aurodox, heneicomycin and shares a similar spectrum of antibacterial activity. http://purl.obolibrary.org/obo/ARO_3001247 azimycin http://purl.obolibrary.org/obo/ARO_3001310 kirromycin-like antibiotics Azimycin is produced by Streptomyces diastatochromogenes ATCC 31013. http://purl.obolibrary.org/obo/ARO_3001248 dihydromocimycin http://purl.obolibrary.org/obo/ARO_3001310 kirromycin-like antibiotics Dihydromocimycin is produced by Streptomyces ramocissimus CBS190.69. http://purl.obolibrary.org/obo/ARO_3001249 phenelfamycin A http://purl.obolibrary.org/obo/ARO_3001310 kirromycin-like antibiotics Phenelfamycin A was isolated from two environmental isolates called AB999F-80 and AB1047T-33. They were both identified as Streptomyces violaceoniger strains. Both these strains were found to produce phenelfamycins A-F and unphenelfamycin. Phenelfamycin A has a monosaccaride moeity and is isomeric with phenelfamycin B. All phenelfamycins were selected due to their activity against anaerobic bacteria, especially Clostridioides difficile. http://purl.obolibrary.org/obo/ARO_3001250 phenelfamycin B http://purl.obolibrary.org/obo/ARO_3001310 kirromycin-like antibiotics Phenelfamycin B was isolated from two environmental isolates called AB999F-80 and AB1047T-33. They were both identified as Streptomyces violaceoniger strains. Both these strains were found to produce phenelfamycins A-F and unphenelfamycin. Phenelfamycin B has a monosaccaride moeity and is isomeric with phenelfamycin A. All phenelfamycins were selected due to their activity against anaerobic bacteria, especially Clostridioides difficile. http://purl.obolibrary.org/obo/ARO_3001251 phenelfamycin C http://purl.obolibrary.org/obo/ARO_3001310 kirromycin-like antibiotics Phenelfamycin C was isolated from two environmental isolates called AB999F-80 and AB1047T-33. They were both identified as Streptomyces violaceoniger strains. Both these strains were found to produce phenelfamycins A-F and unphenelfamycin. Phenelfamycin C has a disaccaride moeity and is isomeric with phenelfamycin D. All phenelfamycins were selected due to their activity against anaerobic bacteria, especially Clostridioides difficile. http://purl.obolibrary.org/obo/ARO_3001252 phenelfamycin D http://purl.obolibrary.org/obo/ARO_3001310 kirromycin-like antibiotics Phenelfamycin D was isolated from two environmental isolates called AB999F-80 and AB1047T-33. They were both identified as Streptomyces violaceoniger strains. Both these strains were found to produce phenelfamycins A-F and unphenelfamycin. Phenelfamycin D has a disaccaride moeity and is isomeric with phenelfamycin C. All phenelfamycins were selected due to their activity against anaerobic bacteria, especially Clostridioides difficile. http://purl.obolibrary.org/obo/ARO_3001253 phenelfamycin E http://purl.obolibrary.org/obo/ARO_3001310 kirromycin-like antibiotics Phenelfamycin E was isolated from two environmental isolates called AB999F-80 and AB1047T-33. They were both identified as Streptomyces violaceoniger strains. Both these strains were found to produce phenelfamycins A-F and unphenelfamycin. Phenelfamycin E has a trisaccaride moeity and is isomeric with phenelfamycin F. All phenelfamycins were selected due to their activity against anaerobic bacteria, especially Clostridioides difficile. Phenelfamycin E and F are the most potent of the phenelfamycins. http://purl.obolibrary.org/obo/ARO_3001256 phenelfamycin F http://purl.obolibrary.org/obo/ARO_3001310 kirromycin-like antibiotics Phenelfamycin F was isolated from two environmental isolates called AB999F-80 and AB1047T-33. They were both identified as Streptomyces violaceoniger strains. Both these strains were found to produce phenelfamycins A-F and unphenelfamycin. Phenelfamycin F has a trisaccaride moeity and is isomeric with phenelfamycin E. All phenelfamycins were selected due to their activity against anaerobic bacteria, especially Clostridioides difficile. Phenelfamycin E and F are the most potent of the phenelfamycins. http://purl.obolibrary.org/obo/ARO_3001257 unphenelfamycin http://purl.obolibrary.org/obo/ARO_3001310 kirromycin-like antibiotics Unphenelfamycin was isolated from two environmental isolates called AB999F-80 and AB1047T-33. They were both identified as Streptomyces violaceoniger strains. Both these strains were found to produce phenelfamycins A-F and unphenelfamycin. Unphenelfamycin has a monosaccaride moeity and lacks the phenacetyl moeity present in the other phenelfamycins. All phenelfamycins were selected due to their activity against anaerobic bacteria, especially Clostridioides difficile. http://purl.obolibrary.org/obo/ARO_3001258 L-681,217 http://purl.obolibrary.org/obo/ARO_3001310 kirromycin-like antibiotics L-681217 is a kirromycin-like antibiotic produced by Streptomyces cattleya. Its biosynthetic gene cluster is characterized. http://purl.obolibrary.org/obo/ARO_3001259 GE37468 http://purl.obolibrary.org/obo/ARO_3001309 cyclic thiazolyl peptide elfamycin GE37468 is a thiazolyl peptide produced by Streptomyces ATCC 55365. GE37468 is produced by post-transcription modification of a ribosomally synthesized preprotein, of which the biosynthetic gene cluster has been elucidated. http://purl.obolibrary.org/obo/ARO_3001260 amythiamicin A http://purl.obolibrary.org/obo/ARO_3001309 cyclic thiazolyl peptide elfamycin Amythiamicin A is a cyclic thiazolyl peptide antibiotic with a structure similar to GE2270A. Amythiamicin B, C, and D also exist, but are not discussed further here. Amythiamicin A was shown to have the highest activity in cell free protein synthesis assays. http://purl.obolibrary.org/obo/ARO_3001264 heneicomycin http://purl.obolibrary.org/obo/ARO_3001310 kirromycin-like antibiotics Heneicomycin is a kirromycin-like antibiotic, isolated from Streptomyces filipinensis. It is structurally related to kirromycin, aurodox and efrotomycin. http://purl.obolibrary.org/obo/ARO_3001265 Erm(30) http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase Erm(30) confers a MLSb resistant phenotype. Along with erm(31), these genes are responsible for self-resistance in the pikromycin/narbomycin/methymycin/neomethymycin producer, Streptomyces venezuelae. http://purl.obolibrary.org/obo/ARO_3001294 verdamicin http://purl.obolibrary.org/obo/ARO_0000016 aminoglycoside antibiotic A gentamicin-group aminoglycoside isolated from Micromonospora. http://purl.obolibrary.org/obo/ARO_3001295 vertilimicin http://purl.obolibrary.org/obo/ARO_0000016 aminoglycoside antibiotic A semisynthetic genamicin-group aminoglycoside, derived from verdamicin. http://purl.obolibrary.org/obo/ARO_3001296 kasugamycin http://purl.obolibrary.org/obo/ARO_0000016 aminoglycoside antibiotic An unusual aminoglycoside because the cyclitol ring is not amino substituted; it was discovered as a fermentation product of Streptomyces kasugaensis. http://purl.obolibrary.org/obo/ARO_3001298 non-erm 23S ribosomal RNA methyltransferase (G748) http://purl.obolibrary.org/obo/ARO_3004274 23S ribosomal RNA methyltransferase Non-erm 23S ribosomal RNA methyltransferases modify guanosine 748 (E. coli numbering) to confer resistance to some macrolides and lincosamides. http://purl.obolibrary.org/obo/ARO_3001299 tlrB conferring tylosin resistance http://purl.obolibrary.org/obo/ARO_3001298 non-erm 23S ribosomal RNA methyltransferase (G748) TlrB is a methyltransferase found in Streptomyces fradiae and confers resistance to mycinamicin, tylosin and lincosamides. Specifically, this enzyme adds a methyl group to guanosine 748 (E. coli numbering). TlrB is found in the tylosin biosynthetic cluster and is one mechanism by which S. fradiae protects itself from self-destruction when producing this macrolide. http://purl.obolibrary.org/obo/ARO_3001300 myrA http://purl.obolibrary.org/obo/ARO_3001298 non-erm 23S ribosomal RNA methyltransferase (G748) myrA is a methyltransferase found in Micromonospora griseorubida and confers resistance to mycinamicin and tylosin. Specifically, this enzyme adds a methyl group to guanosine 748 (E. coli numbering) of 23S ribosomal RNA. MyrA is found in the mycinamicin biosynthetic cluster and is one mechanism by which M. griseorubida protects itself from self-destruction when producing this macrolide. http://purl.obolibrary.org/obo/ARO_3001301 RlmA(II) http://purl.obolibrary.org/obo/ARO_3001298 non-erm 23S ribosomal RNA methyltransferase (G748) RlmA(II) is a methyltransferase found in Streptococcus pneumoniae and confers resistance to tylosin and mycinamicin. Specifically, this enzyme adds a methyl group to guanosine 748 (E. coli numbering) of 23S ribosomal RNA. http://purl.obolibrary.org/obo/ARO_3001302 chrB http://purl.obolibrary.org/obo/ARO_3001298 non-erm 23S ribosomal RNA methyltransferase (G748) ChrB is a methyltransferase found in Streptomyces bikiniensis and confers resistance to chalcomycin, mycinamicin, and tylosin. Specifically, this enzyme adds a methyl group to guanosine 748 (E. coli numbering). chrB is found in the chalcomycin biosynthetic cluster and is responsible for self-resistance in S. bikiniensis. http://purl.obolibrary.org/obo/ARO_3001303 ErmO-srmA http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase ErmO (gene srmA) is a methyltransferase found in the spiramycin producer Streptomyces ambofaciens. Like other Erm enzymes, it catalyzes the methylation of A2058 of the 23S ribosomal RNA. Specifically, this enzyme transfers only one methyl group. The gene is responsible for self-resistance to spiramycin. http://purl.obolibrary.org/obo/ARO_3001304 ErmS http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase ErmS is a methyltransferase found in the tylosin producer Streptomyces fradiae. Like other Erm enzymes, it catalyzes the methylation of A2058 of the 23S ribosomal RNA. Specifically, this enzyme transfers two methyl groups. The gene is found within the tylosin biosynthetic cluster and is responsible for self-resistance. http://purl.obolibrary.org/obo/ARO_3001305 ErmU http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase ErmU is a methyltransferase found in the lincomycin producer Streptomyces lincolnensis. Like other Erm enzymes, it catalyzes the methylation of A2058 of the 23S ribosomal RNA. Specifically, this enzyme transfers only one methyl group. The gene is found in the lincomycin biosynthetic cluster and is responsible for self-resistance. http://purl.obolibrary.org/obo/ARO_3001306 ErmW http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase ErmW is a methyltransferase found in the mycinamicin producer Micromonospora griseorubida. Like other Erm enzymes, it catalyzes the methylation of A2058 of the 23S ribosomal RNA. The gene is found within the mycinamicin biosynthetic cluster and is responsible for self-resistance. http://purl.obolibrary.org/obo/ARO_3001307 vgbA http://purl.obolibrary.org/obo/ARO_3000376 streptogramin vgb lyase vgbA inactivates streptogramin B-type antibiotics by linearizing the lactone ring on the ester bond using an elimination mechanism, thus conferring resistance to these compounds. http://purl.obolibrary.org/obo/ARO_3001308 vgbB http://purl.obolibrary.org/obo/ARO_3000376 streptogramin vgb lyase VgbB inactivates streptogramin B-type antibiotics by linearizing the lactone ring on the ester bond through an elimination mechanism, thus conferring resistance. http://purl.obolibrary.org/obo/ARO_3001309 cyclic thiazolyl peptide elfamycin http://purl.obolibrary.org/obo/ARO_3001219 elfamycin antibiotic Cyclic thiazolyl peptide elfamycins inhibit protein synthesis by preventing the formation of the EF-Tu*GTP-aa-tRNA ternary complex, a mechanism similar to that of pulvomycin. There are non-elfamycin cyclic thiazolyl peptide antibiotics which inhibit protein synthesis by by targeting the 50S ribosomal subunit and are not discussed here further. http://purl.obolibrary.org/obo/ARO_3001310 kirromycin-like antibiotics http://purl.obolibrary.org/obo/ARO_3001219 elfamycin antibiotic Kirromycin-like antibiotics bind to the domain 1,2 interface of elongation factor Tu. This interaction maintains the EF-Tu*GTP conformation even after GTP is hydrolyzed to GDP. EF-Tu*GDP normally releases aa-tRNA and then exits the ribosome; however, kirromycin*EF-Tu*GDP*aa-tRNA forms a strong complex and remains bound to the ribosome, prohibits translocation of the peptide chain and translation is halted. http://purl.obolibrary.org/obo/ARO_3001312 elfamycin resistant EF-Tu http://purl.obolibrary.org/obo/ARO_3003356 Antibiotic resistant EF-Tu Sequence variants of elongation factor Tu that confer resistance to elfamycin antibiotics. http://purl.obolibrary.org/obo/ARO_3001313 facT http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump Efflux protein facT confers resistance to factumycin. The gene has been heterologously expressed in S. coelicolor and its function confirmed. It is possible that this gene can export other kirromycin-like elfamycins, but this has not been tested. http://purl.obolibrary.org/obo/ARO_3001314 retapamulin http://purl.obolibrary.org/obo/ARO_3000670 pleuromutilin antibiotic Retapamulin is a semi-synthetic pleuromutilin antibiotic approved for the treatment of skin infections. http://purl.obolibrary.org/obo/ARO_3001315 valnemulin http://purl.obolibrary.org/obo/ARO_3000670 pleuromutilin antibiotic Two semi-synthetic pleuromutilin derivatives, tiamulin and valnemulin, have been developed as antibiotics for veterinary use. http://purl.obolibrary.org/obo/ARO_3001316 azamulin http://purl.obolibrary.org/obo/ARO_3000670 pleuromutilin antibiotic Azamulin is a semi-synthetic pleuromutilin derivative that failed Stage 1 clinical trials due to poor bioavailability. http://purl.obolibrary.org/obo/ARO_3001317 pleuromutilin http://purl.obolibrary.org/obo/ARO_3000670 pleuromutilin antibiotic Pleuromutilin is a natural product antibiotic produced by Clitopilus passeckerianus. Related antibiotics of clinical significance, such as tiamulin and retapamulin, are semi-synthetic derivatives of this compound. http://purl.obolibrary.org/obo/ARO_3001318 macrocyclic antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule Narrow spectrum macrocyclic antibiotics, in the general sense, is a cyclic molecule containing more than 12 atoms in the macrocyclic lactone ring. http://purl.obolibrary.org/obo/ARO_3001319 fidaxomicin http://purl.obolibrary.org/obo/ARO_3001318 macrocyclic antibiotic A narrow spectrum antibiotic effective against Clostridioides difficile infection (CDI). It is active against gram positive and gram negative bacteria by inhibiting RNA polymerase's switch region leading to cell death. http://purl.obolibrary.org/obo/ARO_3001320 SB22484 http://purl.obolibrary.org/obo/ARO_3001310 kirromycin-like antibiotics SB22484 antibiotics are of the same chemical group as kirromycins. SB22484 antibiotics are produced by Streptomyces sp. NRRL 15496. There are two SB22484 isomers with the same UV absorption spectra, but differing molecular masses. These antibiotics are strongly active against Neisseria species, but also show activity against Streptococci, and Haemophilus influenzae. http://purl.obolibrary.org/obo/ARO_3001321 UK-69,753 http://purl.obolibrary.org/obo/ARO_3001310 kirromycin-like antibiotics UK-69,753 is a glycosylated form of factumycin. The disaccharide moiety of UK-69,753 is virtually identical to that of efrotomycin, another member of this class of antibiotics. UK-69,753 has been shown to have strong in vitro and in vivo activity toward a swine pathogen, Treponema hyodysenteriae. http://purl.obolibrary.org/obo/ARO_3001322 phenelfamycin G http://purl.obolibrary.org/obo/ARO_3001310 kirromycin-like antibiotics Phenelfamycin G is produced by Streptomyces albospinus strain Acta 3619. Phenelfamycin G and H are isomeric and similar to phenelfamycin E and F only with the addition of a hydroxyl group at position C-30. Phenelfamycin G and H have a narrow antibacterial spectrum with potent activity against Cutibacterium acnes. http://purl.obolibrary.org/obo/ARO_3001323 phenelfamycin H http://purl.obolibrary.org/obo/ARO_3001310 kirromycin-like antibiotics Phenelfamycin H is produced by Streptomyces albospinus strain Acta 3619. Phenelfamycin G and H are isomeric and similar to phenelfamycin E and F only with the addition of a hydroxyl group at position C-30. Phenelfamycin G and H have a narrow antibacterial spectrum with potent activity against Cutibacterium acnes. http://purl.obolibrary.org/obo/ARO_3001326 ganefromycin http://purl.obolibrary.org/obo/ARO_3001310 kirromycin-like antibiotics One of a small group of kirromycin-like elfamycins which lack the pyridone moiety. Ganefromycin is produced by Streptomyces lydicus spp. tanzanius, and was considered for use as a growth promoting antibiotic in agriculture. http://purl.obolibrary.org/obo/ARO_3001327 MdtK http://purl.obolibrary.org/obo/ARO_3000112 multidrug and toxic compound extrusion (MATE) transporter A multidrug and toxic compound extrusions (MATE) transporter conferring resistance to norfloxacin, doxorubicin and acriflavine. http://purl.obolibrary.org/obo/ARO_3001328 Escherichia coli mdfA http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump Multidrug efflux pump in E. coli. This multidrug efflux system was originally identified as the Cmr/CmlA chloramphenicol exporter. http://purl.obolibrary.org/obo/ARO_3001329 mdtG http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump The MdtG protein, also named YceE, appears to be a member of the major facilitator superfamily of transporters, and it has been reported, when overexpressed, to increase fosfomycin and deoxycholate resistances. mdtG is a member of the marA-soxS-rob regulon. http://purl.obolibrary.org/obo/ARO_3001331 SHV-54 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-54 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001332 SHV-58 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-58 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001333 SHV-68 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-68 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001334 SHV-87 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-87 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001335 SHV-88 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-88 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001336 SHV-98 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-98 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001337 SHV-99 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-99 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001338 SHV-100 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-100 is a beta-lactamase found in Klebsiella pneumoniae. It differs from SHV-1 by a 35SESQLSGRVGMIE36 insertion. http://purl.obolibrary.org/obo/ARO_3001339 SHV-118 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-118 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001340 SHV-119 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-119 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001341 SHV-132 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-132 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001342 SHV-138 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-138 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001343 SHV-139 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-139 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001344 SHV-143 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-143 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001345 SHV-144 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-144 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001346 SHV-146 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-146 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001347 SHV-164 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-164 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001348 SHV-166 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-166 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001349 SHV-174 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase The beta-lactamase name SHV-174 has been depreciated. http://purl.obolibrary.org/obo/ARO_3001350 SHV-180 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-180 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001351 SHV-183 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-183 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001352 SHV-168 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-168 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001353 SHV-169 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-169 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001354 SHV-170 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-170 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001355 SHV-171 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-171 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001356 SHV-172 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-172 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001357 SHV-173 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-173 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001358 SHV-175 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-175 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001359 SHV-176 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-176 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001360 SHV-177 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-177 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001361 SHV-178 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-178 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001362 SHV-179 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-179 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001363 SHV-181 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-181 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001364 SHV-182 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-182 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001365 SHV-184 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-184 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001366 TEM-100 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-100 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001367 TEM-119 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-119 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001368 TEM-140 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-140 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001369 TEM-153 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-153 is a beta-lactamase found in Enterobacteriaceae. http://purl.obolibrary.org/obo/ARO_3001370 TEM-175 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-175 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001371 TEM-179 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-179 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001372 TEM-180 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-180 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001373 TEM-182 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-182 is a beta-lactamase found in clinical isolates of H. parainfluenzae. http://purl.obolibrary.org/obo/ARO_3001374 TEM-185 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-185 is a beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3001375 TEM-184 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-184 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001376 TEM-196 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-196 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001377 TEM-200 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-200 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001378 TEM-201 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-201 is a beta-lactamase found in Enterobacteriaceae. http://purl.obolibrary.org/obo/ARO_3001379 TEM-202 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-202 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001380 TEM-203 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-203 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001381 TEM-204 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-204 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001382 TEM-205 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-205 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001383 TEM-206 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-206 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001384 TEM-207 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-207 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001385 TEM-208 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-208 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001386 TEM-209 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-209 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001387 TEM-210 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-210. http://purl.obolibrary.org/obo/ARO_3001388 TEM-211 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-211 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001389 TEM-212 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-212 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001390 TEM-213 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-213 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001391 TEM-214 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-214 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001392 TEM-215 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-215 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001393 TEM-216 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-216 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001394 TEM-217 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-217 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001395 TEM-218 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-218 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001396 OXA-1 http://purl.obolibrary.org/obo/ARO_3007696 OXA-1-like beta-lactamase OXA-1 is a beta-lactamase found in E. coli. http://purl.obolibrary.org/obo/ARO_3001397 OXA-2 http://purl.obolibrary.org/obo/ARO_3007704 OXA-2-like beta-lactamase OXA-2 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3001398 OXA-3 http://purl.obolibrary.org/obo/ARO_3007704 OXA-2-like beta-lactamase OXA-3 is a beta-lactamase found in P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3001399 OXA-4 http://purl.obolibrary.org/obo/ARO_3007696 OXA-1-like beta-lactamase OXA-4 is a beta-lactamase found in Enterobacteriaceae and P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3001400 OXA-5 http://purl.obolibrary.org/obo/ARO_3007723 OXA-5-like beta-lactamase OXA-5 is a beta-lactamase found in P. aeruginosa and Enterobacteriaceae. http://purl.obolibrary.org/obo/ARO_3001401 OXA-6 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase The beta-lactamase name OXA-6 has been depreciated. http://purl.obolibrary.org/obo/ARO_3001402 OXA-7 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-7 is a beta-lactamase found in P. aeruginosa and Enterobacteriaceae. http://purl.obolibrary.org/obo/ARO_3001403 OXA-8 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase The beta-lactamase name OXA-8 has been depreciated. http://purl.obolibrary.org/obo/ARO_3001404 OXA-9 http://purl.obolibrary.org/obo/ARO_3007735 OXA-9-like beta-lactamase OXA-9 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001405 OXA-10 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-10 is a beta-lactamase found in Acinetobacter baumannii and P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3001406 OXA-11 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-11 is a beta-lactamase found in P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3001407 OXA-12 http://purl.obolibrary.org/obo/ARO_3007699 OXA-12-like beta-lactamase OXA-12 is a beta-lactamase found in Aeromonas jandaei. http://purl.obolibrary.org/obo/ARO_3001408 OXA-13 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-13 is a beta-lactamase found in P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3001409 OXA-14 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-14 is a beta-lactamase found in P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3001410 OXA-15 http://purl.obolibrary.org/obo/ARO_3007704 OXA-2-like beta-lactamase OXA-15 is a beta-lactamase found in P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3001411 OXA-16 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-16 is a beta-lactamase found in P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3001412 OXA-17 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-17 is a beta-lactamase found in P. aeruginosa and Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001413 OXA-18 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-18 is a beta-lactamase found in P. aeruginosa and Rickettsia. http://purl.obolibrary.org/obo/ARO_3001414 OXA-19 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-19 is a beta-lactamase found in P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3001415 OXA-20 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-20 is a beta-lactamase found in P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3001416 OXA-21 http://purl.obolibrary.org/obo/ARO_3007704 OXA-2-like beta-lactamase OXA-21 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001417 OXA-22 http://purl.obolibrary.org/obo/ARO_3007708 OXA-22-like beta-lactamase OXA-22 is a beta-lactamase found in Ralstonia pickettii. http://purl.obolibrary.org/obo/ARO_3001418 OXA-23 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-23 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001419 OXA-24 http://purl.obolibrary.org/obo/ARO_3007711 OXA-24-like beta-lactamase OXA-24 is a beta-lactamase found in A. baumannii and P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3001420 OXA-25 http://purl.obolibrary.org/obo/ARO_3007711 OXA-24-like beta-lactamase OXA-25 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001421 OXA-26 http://purl.obolibrary.org/obo/ARO_3007711 OXA-24-like beta-lactamase OXA-26 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001422 OXA-27 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-27 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001423 OXA-28 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-28 is a beta-lactamase found in P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3001424 OXA-29 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-29 is a beta-lactamase found in Legionella gormanii. http://purl.obolibrary.org/obo/ARO_3001425 OXA-31 http://purl.obolibrary.org/obo/ARO_3007696 OXA-1-like beta-lactamase OXA-31 is a beta-lactamase found in P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3001426 OXA-32 http://purl.obolibrary.org/obo/ARO_3007704 OXA-2-like beta-lactamase OXA-32 is a beta-lactamase found in P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3001427 OXA-33 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-33 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001428 OXA-34 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-34 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001429 OXA-35 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-35 is a beta-lactamase found in P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3001430 OXA-36 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-36 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001431 OXA-37 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-37 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001432 OXA-38 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-38 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001433 OXA-39 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-39 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001434 OXA-41 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-41 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001435 OXA-44 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-44 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001436 OXA-52 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-52 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001437 OXA-67 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-67 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001438 OXA-100 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-100 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001439 OXA-101 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-101 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001440 OXA-115 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-115 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001441 OXA-116 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-116 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001442 OXA-117 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-117 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001443 OXA-121 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-121 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001444 OXA-122 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-122 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001445 OXA-123 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-123 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001446 OXA-124 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-124 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001447 OXA-125 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-125 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001448 OXA-126 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-126 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001449 OXA-127 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-127 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001451 OXA-139 http://purl.obolibrary.org/obo/ARO_3007711 OXA-24-like beta-lactamase OXA-139 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001452 OXA-140 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-140 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001453 OXA-148 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-148 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001454 OXA-149 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-149 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001455 OXA-150 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-150 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001456 OXA-151 http://purl.obolibrary.org/obo/ARO_3007731 OXA-62-like beta-lactamase OXA-151 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001457 OXA-152 http://purl.obolibrary.org/obo/ARO_3007731 OXA-62-like beta-lactamase OXA-152 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001458 OXA-153 http://purl.obolibrary.org/obo/ARO_3007731 OXA-62-like beta-lactamase OXA-153 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001459 OXA-154 http://purl.obolibrary.org/obo/ARO_3007731 OXA-62-like beta-lactamase OXA-154 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001460 OXA-155 http://purl.obolibrary.org/obo/ARO_3007731 OXA-62-like beta-lactamase OXA-155 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001461 OXA-156 http://purl.obolibrary.org/obo/ARO_3007731 OXA-62-like beta-lactamase OXA-156 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001462 OXA-157 http://purl.obolibrary.org/obo/ARO_3007731 OXA-62-like beta-lactamase OXA-157 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001463 OXA-158 http://purl.obolibrary.org/obo/ARO_3007731 OXA-62-like beta-lactamase OXA-158 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001464 OXA-159 http://purl.obolibrary.org/obo/ARO_3007731 OXA-62-like beta-lactamase OXA-159 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001465 OXA-165 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-165 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001466 OXA-166 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-166 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001467 OXA-167 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-167 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001468 OXA-168 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-168 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001469 OXA-169 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-169 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001470 OXA-170 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-170 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001471 OXA-171 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-171 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001472 OXA-178 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-178 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001473 OXA-179 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-179 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001474 OXA-180 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-180 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001475 OXA-183 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-183 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001476 OXA-184 http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase OXA-184 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001477 OXA-185 http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase OXA-185 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001478 OXA-193 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-193 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001479 OXA-194 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-194 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001480 OXA-195 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-195 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001481 OXA-196 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-196 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001482 OXA-197 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-197 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001483 OXA-205 http://purl.obolibrary.org/obo/ARO_3007720 OXA-46-like beta-lactamase OXA-205 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001484 OXA-206 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-206 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001485 OXA-207 http://purl.obolibrary.org/obo/ARO_3007711 OXA-24-like beta-lactamase OXA-207 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001486 OXA-208 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-208 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001487 OXA-210 http://purl.obolibrary.org/obo/ARO_3007704 OXA-2-like beta-lactamase OXA-210 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001488 OXA-216 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-216 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001489 OXA-217 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-217 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001490 OXA-220 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-220 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001491 OXA-221 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-221 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001492 OXA-222 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-222 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001493 OXA-225 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-225 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001494 OXA-227 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-227 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001495 OXA-233 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-233 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001496 OXA-234 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-234 is a beta-lactamase found in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3001497 OXA-238 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-238 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001498 OXA-239 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-239 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001499 OXA-240 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-240 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001500 OXA-251 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-251 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001501 OXA-252 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-252 is a beta-lactamase found in Shewanella spp. http://purl.obolibrary.org/obo/ARO_3001502 OXA-256 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-256 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001503 OXA-258 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-258 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001504 OXA-309 http://purl.obolibrary.org/obo/ARO_3007705 OXA-211-like beta-lactamase OXA-309 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001505 OXA-310 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-310 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001506 OXA-311 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-311 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001507 OXA-318 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-318 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001508 OXA-319 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-319 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001509 OXA-321 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-321 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001510 OXA-322 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-322 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001511 OXA-323 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-323 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001512 OXA-324 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-324 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001513 OXA-325 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-325 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001514 OXA-326 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-326 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001515 OXA-327 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-327 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001516 OXA-328 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-328 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001517 OXA-329 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-329 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001518 OXA-330 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-330 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001519 OXA-331 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-331 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001520 OXA-332 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-332 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001521 OXA-333 http://purl.obolibrary.org/obo/ARO_3007705 OXA-211-like beta-lactamase OXA-333 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001522 OXA-334 http://purl.obolibrary.org/obo/ARO_3007705 OXA-211-like beta-lactamase OXA-334 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001523 OXA-335 http://purl.obolibrary.org/obo/ARO_3007700 OXA-134-like beta-lactamase OXA-335 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001524 OXA-336 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-336 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001525 OXA-337 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-337 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001526 OXA-338 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-338 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001527 OXA-339 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-339 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001528 OXA-340 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-340 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001529 OXA-341 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-341 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001530 OXA-342 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-342 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001531 OXA-343 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-343 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001532 OXA-344 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-344 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001533 OXA-345 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-345 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001534 OXA-346 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-346 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001535 OXA-348 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-348 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001536 OXA-349 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-349 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001537 OXA-350 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-350 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001538 OXA-351 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-351 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001539 OXA-352 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-352 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001540 OXA-353 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-353 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001541 OXA-354 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-354 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001542 OXA-355 http://purl.obolibrary.org/obo/ARO_3007709 OXA-229-like beta-lactamase OXA-355 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001543 OXA-356 http://purl.obolibrary.org/obo/ARO_3007709 OXA-229-like beta-lactamase OXA-356 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001544 OXA-357 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-357 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001545 OXA-358 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-358 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001546 OXA-359 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-359 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001547 OXA-360 http://purl.obolibrary.org/obo/ARO_3007700 OXA-134-like beta-lactamase OXA-360 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001548 OXA-361 http://purl.obolibrary.org/obo/ARO_3007700 OXA-134-like beta-lactamase OXA-361 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001549 OXA-362 http://purl.obolibrary.org/obo/ARO_3007700 OXA-134-like beta-lactamase OXA-362 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001550 OXA-363 http://purl.obolibrary.org/obo/ARO_3007700 OXA-134-like beta-lactamase OXA-363 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001551 OXA-364 http://purl.obolibrary.org/obo/ARO_3007716 OXA-364-like beta-lactamase OXA-364 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001552 OXA-365 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-365 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001553 OXA-366 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-366 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001554 OXA-367 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-367 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001555 OXA-368 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-368 is a beta-lactamase found in Aeromonas sobria. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001557 OXA-371 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-371 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001558 OXA-372 http://purl.obolibrary.org/obo/ARO_3007717 OXA-372-like beta-lactamase OXA-372 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001559 OXA-373 http://purl.obolibrary.org/obo/ARO_3007705 OXA-211-like beta-lactamase OXA-373 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001560 OXA-374 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-374 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001561 OXA-375 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-375 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001562 OXA-376 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-376 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001563 OXA-377 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-377 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001564 OXA-378 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-378 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001565 OXA-379 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-379 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001566 OXA-380 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-380 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001567 OXA-381 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-381 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001568 OXA-382 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-382 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001569 OXA-383 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-383 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001570 OXA-384 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-384 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001571 OXA-385 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-385 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001572 OXA-386 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-386 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001573 OXA-387 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-387 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001574 OXA-388 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-388 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001575 OXA-389 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-389 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001576 OXA-390 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-390 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001577 OXA-391 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-391 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001578 OXA-392 http://purl.obolibrary.org/obo/ARO_3007696 OXA-1-like beta-lactamase OXA-392 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001579 OXA-393 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-393 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001580 OXA-394 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-394 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001581 OXA-395 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-395 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001582 OXA-396 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-396 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001583 OXA-397 http://purl.obolibrary.org/obo/ARO_3007728 OXA-58-like beta-lactamase OXA-397 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001584 OXA-398 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-398 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001585 OXA-399 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-399 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001586 OXA-400 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-400 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001587 OXA-401 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-401 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001588 OXA-402 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-402 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001589 OXA-403 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-403 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001595 OXA-404 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-404 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001596 OXA-405 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-405 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001597 OXA-406 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-406 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001598 OXA-407 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-407 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001599 OXA-408 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-408 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001600 OXA-409 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-409 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001601 OXA-410 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-410 is an OXA-51-like beta-lactamase. http://purl.obolibrary.org/obo/ARO_3001602 OXA-411 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-411 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001603 OXA-412 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-412 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001604 OXA-413 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-413 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001605 OXA-414 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-414 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001606 OXA-415 http://purl.obolibrary.org/obo/ARO_3007704 OXA-2-like beta-lactamase OXA-415 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001607 OXA-416 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-416 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001608 OXA-417 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-417 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001609 OXA-114a http://purl.obolibrary.org/obo/ARO_3007698 OXA-114-like beta-lactamase OXA-114a is a beta-lactamase found in Achromobacter xylosoxidans. http://purl.obolibrary.org/obo/ARO_3001610 OXA-243 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-243 is a beta-lactamase found in Achromobacter xylosoxidans. http://purl.obolibrary.org/obo/ARO_3001611 OXA-58 http://purl.obolibrary.org/obo/ARO_3007728 OXA-58-like beta-lactamase OXA-58 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001612 OXA-51 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-51 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001613 OXA-64 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-64 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001614 OXA-65 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-65 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001615 OXA-66 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-66 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001616 OXA-68 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-68 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001617 OXA-69 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-69 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001618 OXA-70 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-70 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001619 OXA-71 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-71 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001620 OXA-75 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-75 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001621 OXA-76 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-76 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001622 OXA-77 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-77 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001623 OXA-83 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-83 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001624 OXA-84 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-84 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001625 OXA-89 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-89 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001626 OXA-88 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-88 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001627 OXA-91 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-91 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001628 OXA-93 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-93 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001629 OXA-94 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-94 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001630 OXA-95 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-95 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001631 OXA-96 http://purl.obolibrary.org/obo/ARO_3007728 OXA-58-like beta-lactamase OXA-96 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001632 OXA-92 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-92 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001633 OXA-79 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-79 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001634 OXA-80 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-80 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001635 OXA-82 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-82 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001636 OXA-104 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-104 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001637 OXA-106 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-106 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001638 OXA-107 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-107 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001639 OXA-108 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-108 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001640 OXA-109 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-109 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001641 OXA-110 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-110 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001642 OXA-111 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-111 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001643 OXA-112 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-112 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001644 OXA-113 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-113 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001645 OXA-78 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-78 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001646 OXA-98 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-98 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001647 OXA-97 http://purl.obolibrary.org/obo/ARO_3007728 OXA-58-like beta-lactamase OXA-97 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001648 OXA-128 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-128 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001649 OXA-99 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-99 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001650 OXA-90 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-90 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001651 OXA-130 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-130 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001652 OXA-131 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-131 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001653 OXA-132 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-132 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001654 OXA-143 http://purl.obolibrary.org/obo/ARO_3007701 OXA-143-like beta-lactamase OXA-143 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001655 OXA-138 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-138 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001656 OXA-172 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-172 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001657 OXA-173 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-173 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001658 OXA-174 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-174 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001659 OXA-175 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-175 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001660 OXA-176 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-176 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001661 OXA-177 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-177 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001662 OXA-164 http://purl.obolibrary.org/obo/ARO_3007728 OXA-58-like beta-lactamase OXA-164 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001663 OXA-160 http://purl.obolibrary.org/obo/ARO_3007711 OXA-24-like beta-lactamase OXA-160 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001664 OXA-203 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-203 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001665 OXA-200 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-200 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001666 OXA-201 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-201 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001667 OXA-202 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-202 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001668 OXA-219 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-219 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001669 OXA-223 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-223 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001670 OXA-231 http://purl.obolibrary.org/obo/ARO_3007701 OXA-143-like beta-lactamase OXA-231 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001671 OXA-49 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-49 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001672 OXA-120 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-120 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001673 OXA-248 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-248 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001674 OXA-249 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-249 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001675 OXA-250 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-250 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001676 OXA-235 http://purl.obolibrary.org/obo/ARO_3007700 OXA-134-like beta-lactamase OXA-235 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001677 OXA-236 http://purl.obolibrary.org/obo/ARO_3007700 OXA-134-like beta-lactamase OXA-236 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001678 OXA-237 http://purl.obolibrary.org/obo/ARO_3007700 OXA-134-like beta-lactamase OXA-237 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001679 OXA-241 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-241 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001680 OXA-242 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-242 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001681 OXA-278 http://purl.obolibrary.org/obo/ARO_3007700 OXA-134-like beta-lactamase OXA-278 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001682 OXA-254 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-254 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001683 OXA-312 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-312 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001684 OXA-313 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-313 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001685 OXA-314 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-314 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001686 OXA-315 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-315 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001687 OXA-316 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-316 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001688 OXA-317 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-317 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001689 OXA-253 http://purl.obolibrary.org/obo/ARO_3007701 OXA-143-like beta-lactamase OXA-253 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001690 OXA-255 http://purl.obolibrary.org/obo/ARO_3007701 OXA-143-like beta-lactamase OXA-255 is a beta-lactamase found in A. baumannii. http://purl.obolibrary.org/obo/ARO_3001691 OXA-228 http://purl.obolibrary.org/obo/ARO_3007709 OXA-229-like beta-lactamase OXA-228 is a beta-lactamase found in A. bereziniae. http://purl.obolibrary.org/obo/ARO_3001692 OXA-229 http://purl.obolibrary.org/obo/ARO_3007709 OXA-229-like beta-lactamase OXA-229 is a beta-lactamase found in A. bereziniae. http://purl.obolibrary.org/obo/ARO_3001693 OXA-230 http://purl.obolibrary.org/obo/ARO_3007709 OXA-229-like beta-lactamase OXA-230 is a beta-lactamase found in A. bereziniae. http://purl.obolibrary.org/obo/ARO_3001694 OXA-257 http://purl.obolibrary.org/obo/ARO_3007709 OXA-229-like beta-lactamase OXA-257 is a beta-lactamase found in A. bereziniae. http://purl.obolibrary.org/obo/ARO_3001695 OXA-134 http://purl.obolibrary.org/obo/ARO_3007700 OXA-134-like beta-lactamase OXA-134 is a beta-lactamase found in A. lwoffii. http://purl.obolibrary.org/obo/ARO_3001696 OXA-186 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase The beta-lactamase name OXA-186 has been depreciated. http://purl.obolibrary.org/obo/ARO_3001697 OXA-187 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase The beta-lactamase name OXA-187 has been depreciated. http://purl.obolibrary.org/obo/ARO_3001698 OXA-188 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase The beta-lactamase name OXA-188 has been depreciated. http://purl.obolibrary.org/obo/ARO_3001699 OXA-189 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase The beta-lactamase name OXA-189 has been depreciated. http://purl.obolibrary.org/obo/ARO_3001700 OXA-190 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase The beta-lactamase name OXA-190 has been depreciated. http://purl.obolibrary.org/obo/ARO_3001701 OXA-191 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase The beta-lactamase name OXA-191 has been depreciated. http://purl.obolibrary.org/obo/ARO_3001702 OXA-133 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-133 is a beta-lactamase found in A. radioresistens. http://purl.obolibrary.org/obo/ARO_3001703 OXA-86 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-86 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001704 OXA-87 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-87 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001705 OXA-72 http://purl.obolibrary.org/obo/ARO_3007711 OXA-24-like beta-lactamase OXA-72 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001706 OXA-102 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase The beta-lactamase name OXA-102 has been depreciated. http://purl.obolibrary.org/obo/ARO_3001707 OXA-103 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-103 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001708 OXA-105 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-105 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001709 OXA-182 http://purl.obolibrary.org/obo/ARO_3007701 OXA-143-like beta-lactamase OXA-182 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001710 OXA-211 http://purl.obolibrary.org/obo/ARO_3007705 OXA-211-like beta-lactamase OXA-211 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001711 OXA-212 http://purl.obolibrary.org/obo/ARO_3007705 OXA-211-like beta-lactamase OXA-212 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001712 OXA-213 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-213 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001713 OXA-214 http://purl.obolibrary.org/obo/ARO_3007707 OXA-214-like beta-lactamase OXA-214 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001714 OXA-215 http://purl.obolibrary.org/obo/ARO_3007707 OXA-214-like beta-lactamase OXA-215 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001715 OXA-259 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-259 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001716 OXA-260 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-260 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001717 OXA-261 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-261 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001718 OXA-262 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-262 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001719 OXA-263 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-263 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001720 OXA-264 http://purl.obolibrary.org/obo/ARO_3007707 OXA-214-like beta-lactamase OXA-264 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001721 OXA-265 http://purl.obolibrary.org/obo/ARO_3007707 OXA-214-like beta-lactamase OXA-265 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001722 OXA-266 http://purl.obolibrary.org/obo/ARO_3007712 OXA-266-like beta-lactamase OXA-266 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001723 OXA-267 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-267 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001724 OXA-268 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-268 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001725 OXA-269 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-269 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001726 OXA-270 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-270 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001727 OXA-271 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-271 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001728 OXA-272 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-272 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001729 OXA-273 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-273 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001730 OXA-274 http://purl.obolibrary.org/obo/ARO_3007713 OXA-274-like beta-lactamase OXA-274 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001731 OXA-275 http://purl.obolibrary.org/obo/ARO_3007713 OXA-274-like beta-lactamase OXA-275 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001732 OXA-276 http://purl.obolibrary.org/obo/ARO_3007700 OXA-134-like beta-lactamase OXA-276 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001733 OXA-277 http://purl.obolibrary.org/obo/ARO_3007700 OXA-134-like beta-lactamase OXA-277 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001734 OXA-279 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-279 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001735 OXA-280 http://purl.obolibrary.org/obo/ARO_3007705 OXA-211-like beta-lactamase OXA-280 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001736 OXA-281 http://purl.obolibrary.org/obo/ARO_3007705 OXA-211-like beta-lactamase OXA-281 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001737 OXA-282 http://purl.obolibrary.org/obo/ARO_3007700 OXA-134-like beta-lactamase OXA-282 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001738 OXA-283 http://purl.obolibrary.org/obo/ARO_3007700 OXA-134-like beta-lactamase OXA-283 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001739 OXA-284 http://purl.obolibrary.org/obo/ARO_3007700 OXA-134-like beta-lactamase OXA-284 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001740 OXA-285 http://purl.obolibrary.org/obo/ARO_3007700 OXA-134-like beta-lactamase OXA-285 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001741 OXA-286 http://purl.obolibrary.org/obo/ARO_3007714 OXA-286-like beta-lactamase OXA-286 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001742 OXA-287 http://purl.obolibrary.org/obo/ARO_3007714 OXA-286-like beta-lactamase OXA-287 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001743 OXA-288 http://purl.obolibrary.org/obo/ARO_3007714 OXA-286-like beta-lactamase OXA-288 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001744 OXA-289 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-289 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001745 OXA-290 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-290 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001746 OXA-291 http://purl.obolibrary.org/obo/ARO_3007714 OXA-286-like beta-lactamase OXA-291 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001747 OXA-292 http://purl.obolibrary.org/obo/ARO_3007714 OXA-286-like beta-lactamase OXA-292 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001748 OXA-293 http://purl.obolibrary.org/obo/ARO_3007714 OXA-286-like beta-lactamase OXA-293 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001749 OXA-294 http://purl.obolibrary.org/obo/ARO_3007715 OXA-294-like beta-lactamase OXA-294 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001750 OXA-295 http://purl.obolibrary.org/obo/ARO_3007715 OXA-294-like beta-lactamase OXA-295 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001751 OXA-296 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-296 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001752 OXA-297 http://purl.obolibrary.org/obo/ARO_3007715 OXA-294-like beta-lactamase OXA-297 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001753 OXA-298 http://purl.obolibrary.org/obo/ARO_3007715 OXA-294-like beta-lactamase OXA-298 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001754 OXA-299 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-299 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001755 OXA-300 http://purl.obolibrary.org/obo/ARO_3007709 OXA-229-like beta-lactamase OXA-300 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001756 OXA-301 http://purl.obolibrary.org/obo/ARO_3007709 OXA-229-like beta-lactamase OXA-301 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001757 OXA-302 http://purl.obolibrary.org/obo/ARO_3007714 OXA-286-like beta-lactamase OXA-302 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001758 OXA-303 http://purl.obolibrary.org/obo/ARO_3007714 OXA-286-like beta-lactamase OXA-303 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001759 OXA-304 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-304 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001760 OXA-305 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-305 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001761 OXA-306 http://purl.obolibrary.org/obo/ARO_3007714 OXA-286-like beta-lactamase OXA-306 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001762 OXA-307 http://purl.obolibrary.org/obo/ARO_3007714 OXA-286-like beta-lactamase OXA-307 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001763 OXA-308 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-308 is a beta-lactamase found in Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001764 OXA-63 http://purl.obolibrary.org/obo/ARO_3007732 OXA-63-like beta-lactamase OXA-63 is a beta-lactamase found in Brachyspira spp. http://purl.obolibrary.org/obo/ARO_3001765 OXA-136 http://purl.obolibrary.org/obo/ARO_3007732 OXA-63-like beta-lactamase OXA-136 is a beta-lactamase found in Brachyspira spp. http://purl.obolibrary.org/obo/ARO_3001766 OXA-192 http://purl.obolibrary.org/obo/ARO_3007732 OXA-63-like beta-lactamase OXA-192 is a beta-lactamase found in Brachyspira spp. http://purl.obolibrary.org/obo/ARO_3001767 OXA-137 http://purl.obolibrary.org/obo/ARO_3007732 OXA-63-like beta-lactamase OXA-137 is a beta-lactamase found in Brachyspira spp. http://purl.obolibrary.org/obo/ARO_3001768 OXA-118 http://purl.obolibrary.org/obo/ARO_3007720 OXA-46-like beta-lactamase OXA-118 is a beta-lactamase found in Burkholderia cepacia. http://purl.obolibrary.org/obo/ARO_3001769 OXA-42 http://purl.obolibrary.org/obo/ARO_3007718 OXA-42-like beta-lactamase OXA-42 is a beta-lactamase found in Burkholderia pseudomallei. http://purl.obolibrary.org/obo/ARO_3001770 OXA-43 http://purl.obolibrary.org/obo/ARO_3007718 OXA-42-like beta-lactamase OXA-43 is a beta-lactamase found in Burkholderia pseudomallei. http://purl.obolibrary.org/obo/ARO_3001771 OXA-57 http://purl.obolibrary.org/obo/ARO_3007718 OXA-42-like beta-lactamase OXA-57 is a beta-lactamase found in Burkholderia pseudomallei. http://purl.obolibrary.org/obo/ARO_3001772 OXA-59 http://purl.obolibrary.org/obo/ARO_3007718 OXA-42-like beta-lactamase OXA-59 is a beta-lactamase found in Burkholderia pseudomallei. http://purl.obolibrary.org/obo/ARO_3001773 OXA-61 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-61 is a beta-lactamase found in Campylobacter jejuni. http://purl.obolibrary.org/obo/ARO_3001774 OXA-370 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-370 is a beta-lactamase found in Enterobacter hormaechei. http://purl.obolibrary.org/obo/ARO_3001775 OXA-119 http://purl.obolibrary.org/obo/ARO_3007720 OXA-46-like beta-lactamase OXA-119 is a beta-lactamase found in Enterobacteriaceae. http://purl.obolibrary.org/obo/ARO_3001776 OXA-162 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-162 is a beta-lactamase found in Enterobacteriaceae. http://purl.obolibrary.org/obo/ARO_3001777 OXA-347 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-347 is a beta-lactamase found in Enterobacteriaceae. http://purl.obolibrary.org/obo/ARO_3001778 OXA-232 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-232 is a beta-lactamase found in Enterobacteriaceae. http://purl.obolibrary.org/obo/ARO_3001779 OXA-146 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-146 is a beta-lactamase found in Enterobacteriaceae. http://purl.obolibrary.org/obo/ARO_3001780 OXA-85 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-85 is a beta-lactamase found in Fusobacterium nucleatum. http://purl.obolibrary.org/obo/ARO_3001781 OXA-47 http://purl.obolibrary.org/obo/ARO_3007696 OXA-1-like beta-lactamase OXA-47 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001782 OXA-48 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-48 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001783 OXA-163 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-163 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001784 OXA-181 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-181 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001785 OXA-73 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-73 is a beta-lactamase found in Klebsiella pneumonia. http://purl.obolibrary.org/obo/ARO_3001786 OXA-244 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-244 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001787 OXA-245 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-245 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001788 OXA-204 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-204 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001791 OXA-247 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-247 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001792 OXA-62 http://purl.obolibrary.org/obo/ARO_3007731 OXA-62-like beta-lactamase OXA-62 is a beta-lactamase found in Pandoraea pnomenusa. http://purl.obolibrary.org/obo/ARO_3001793 OXA-320 http://purl.obolibrary.org/obo/ARO_3007696 OXA-1-like beta-lactamase OXA-320 is a beta-lactamase found in Proteus mirabilis. http://purl.obolibrary.org/obo/ARO_3001794 OXA-45 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-45 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3001795 OXA-56 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-56 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3001796 OXA-50 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-50 is a beta-lactamase found in Pseudomonas aeruginosa. It confers decreased susceptibility to ampicillin and ticarcillin and, interestingly, to moxalactam and meropenem in P. aeruginosa but not in E. coli. Also confers resistance to piperacillin-tazobactam and cephalotin. http://purl.obolibrary.org/obo/ARO_3001797 OXA-46 http://purl.obolibrary.org/obo/ARO_3007720 OXA-46-like beta-lactamase OXA-46 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3001798 OXA-74 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-74 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3001799 OXA-161 http://purl.obolibrary.org/obo/ARO_3007704 OXA-2-like beta-lactamase OXA-161 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3001800 OXA-226 http://purl.obolibrary.org/obo/ARO_3007704 OXA-2-like beta-lactamase OXA-226 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3001801 OXA-147 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-147 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3001802 OXA-141 http://purl.obolibrary.org/obo/ARO_3007704 OXA-2-like beta-lactamase OXA-141 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3001803 OXA-142 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-142 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3001804 OXA-145 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-145 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3001805 OXA-198 http://purl.obolibrary.org/obo/ARO_3007703 OXA-198-like beta-lactamase OXA-198 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3001806 OXA-224 http://purl.obolibrary.org/obo/ARO_3007696 OXA-1-like beta-lactamase OXA-224 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3001807 OXA-246 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-246 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3001808 OXA-60 http://purl.obolibrary.org/obo/ARO_3007729 OXA-60-like beta-lactamase OXA-60 is a beta-lactamase found in Ralstonia pickettii. http://purl.obolibrary.org/obo/ARO_3001809 OXA-209 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-209 is a beta-lactamase found in Riemerella anatipestifer. http://purl.obolibrary.org/obo/ARO_3001810 OXA-53 http://purl.obolibrary.org/obo/ARO_3007704 OXA-2-like beta-lactamase OXA-53 is a beta-lactamase found in Salmonella enterica. http://purl.obolibrary.org/obo/ARO_3001811 OXA-129 http://purl.obolibrary.org/obo/ARO_3007723 OXA-5-like beta-lactamase OXA-129 is a beta-lactamase found in Salmonella enterica. http://purl.obolibrary.org/obo/ARO_3001812 OXA-54 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-54 is a beta-lactamase found in Shewanella spp. http://purl.obolibrary.org/obo/ARO_3001813 OXA-55 http://purl.obolibrary.org/obo/ARO_3007727 OXA-55-like beta-lactamase OXA-55 is a beta-lactamase found in Shewanella spp. http://purl.obolibrary.org/obo/ARO_3001814 OXA-199 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-199 is a beta-lactamase found in Shewanella spp. http://purl.obolibrary.org/obo/ARO_3001815 ACC-1 http://purl.obolibrary.org/obo/ARO_3000073 ACC beta-lactamase ACC-1 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001816 ACC-2 http://purl.obolibrary.org/obo/ARO_3000073 ACC beta-lactamase ACC-2 is a beta-lactamase found in Hafnia alvei. http://purl.obolibrary.org/obo/ARO_3001817 ACC-3 http://purl.obolibrary.org/obo/ARO_3000073 ACC beta-lactamase ACC-3 is a beta-lactamase found in Hafnia alvei. http://purl.obolibrary.org/obo/ARO_3001818 ACC-4 http://purl.obolibrary.org/obo/ARO_3000073 ACC beta-lactamase ACC-4 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001819 ACC-5 http://purl.obolibrary.org/obo/ARO_3000073 ACC beta-lactamase ACC-5 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001821 ACT-1 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-1 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001822 ACT-2 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-2 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001823 ACT-3 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-3 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001824 ACT-5 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-5 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001825 ACT-6 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-6 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001826 ACT-9 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-9 is a beta-lactamase found in Pantoea agglomerans. This sequence and nomenclature has been superseded by ACT-143. http://purl.obolibrary.org/obo/ARO_3001827 ACT-16 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-16 is a beta-lactamase found in Enterobacteriaceae. http://purl.obolibrary.org/obo/ARO_3001828 ACT-23 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-23 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001829 ACT-4 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-4 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001830 ACT-7 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-7 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001831 ACT-8 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-8 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001832 ACT-10 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-10 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001833 ACT-11 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-11 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001834 ACT-12 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-12 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001835 ACT-13 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-13 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001836 ACT-14 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-14 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001837 ACT-15 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-15 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001838 ACT-17 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-17 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001839 ACT-18 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-18 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001840 ACT-19 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-19 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001841 ACT-20 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-20 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001842 ACT-21 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-21 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001843 ACT-22 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-22 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001844 ACT-24 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-24 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001845 ACT-25 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-25 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001847 ACT-27 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-27 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001848 ACT-28 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-28 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001849 ACT-29 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-29 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001850 ACT-30 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-30 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001851 ACT-31 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-31 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001852 ACT-32 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-32 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001853 ACT-33 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-33 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001854 ACT-34 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-34 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001855 ACT-35 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-35 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001856 CFE-1 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CFE-1 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001857 LAT-1 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase LAT-1 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001858 IMI-1 http://purl.obolibrary.org/obo/ARO_3000018 IMI beta-lactamase IMI-1 is a beta-lactamase found in Enterobacter cloacae. http://purl.obolibrary.org/obo/ARO_3001859 IMI-2 http://purl.obolibrary.org/obo/ARO_3000018 IMI beta-lactamase IMI-2 is a beta-lactamase found in Enterobacteriaceae. http://purl.obolibrary.org/obo/ARO_3001860 IMI-3 http://purl.obolibrary.org/obo/ARO_3000018 IMI beta-lactamase IMI-3 is a beta-lactamase found in Enterobacteriaceae. http://purl.obolibrary.org/obo/ARO_3001861 IMI-4 http://purl.obolibrary.org/obo/ARO_3000018 IMI beta-lactamase IMI-4 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001862 IMI-5 http://purl.obolibrary.org/obo/ARO_3000018 IMI beta-lactamase IMI-5 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001863 IMI-6 http://purl.obolibrary.org/obo/ARO_3000018 IMI beta-lactamase IMI-6 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001864 CTX-M-1 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-1 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3001865 CTX-M-2 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-2 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3001866 CTX-M-3 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-3 is a beta-lactamase found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3001867 CTX-M-4 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-4 is a beta-lactamase found in Salmonella typhimurium. http://purl.obolibrary.org/obo/ARO_3001868 CTX-M-5 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-5 is a beta-lactamase found in Salmonella typhimurium. http://purl.obolibrary.org/obo/ARO_3001869 CTX-M-6 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-6 is a beta-lactamase found in Salmonella typhimurium. http://purl.obolibrary.org/obo/ARO_3001870 CTX-M-7 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-7 is a beta-lactamase found in Salmonella typhimurium. http://purl.obolibrary.org/obo/ARO_3001871 CTX-M-8 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-8 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3001872 CTX-M-9 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-9 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3001873 CTX-M-10 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-10 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001874 CTX-M-11 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-11 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001875 CTX-M-12 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-12 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001876 CTX-M-13 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-13 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3001877 CTX-M-14 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-14 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3001878 CTX-M-15 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-15 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3001879 CTX-M-16 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-16 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001880 CTX-M-17 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-17 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001881 CTX-M-19 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-19 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001882 CTX-M-20 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-20 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3001883 CTX-M-21 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-21 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3001884 CTX-M-22 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-22 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3001885 CTX-M-23 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-23 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3001886 CTX-M-24 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-24 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3001887 CTX-M-25 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-25 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001888 CTX-M-26 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-26 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001889 CTX-M-27 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-27 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001890 CTX-M-28 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-28 is a beta-lactamase found in Salmonella enterica. http://purl.obolibrary.org/obo/ARO_3001891 CTX-M-29 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-29 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3001892 CTX-M-30 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-30 is a beta-lactamase found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3001893 CTX-M-31 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-31 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3001894 CTX-M-32 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-32 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001895 CTX-M-33 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-33 is a beta-lactamase found in Salmonella enterica. http://purl.obolibrary.org/obo/ARO_3001896 CTX-M-34 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-34 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3001897 CTX-M-35 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-35 is a beta-lactamase found in Citrobacter koseri. http://purl.obolibrary.org/obo/ARO_3001898 CTX-M-36 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-36 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001899 CTX-M-37 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-37 is a beta-lactamase found in Salmonella enterica. http://purl.obolibrary.org/obo/ARO_3001900 CTX-M-38 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-38 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001901 CTX-M-39 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-39 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001902 CTX-M-40 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-40 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001903 CTX-M-41 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-41 is a beta-lactamase found in Proteus mirabilis. http://purl.obolibrary.org/obo/ARO_3001904 CTX-M-42 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-42 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001905 CTX-M-43 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-43 is a beta-lactamase found in Pseudomonas aeruginosa and Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3001906 CTX-M-44 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-44 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3001907 CTX-M-45 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-45 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001908 CTX-M-46 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-46 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3001909 CTX-M-47 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-47 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3001910 CTX-M-48 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-48 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3001911 CTX-M-49 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-49 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3001912 CTX-M-50 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-50 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3001913 CTX-M-51 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-51 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001914 CTX-M-52 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-52 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001915 CTX-M-53 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-53 is a beta-lactamase found in Salmonella enterica. http://purl.obolibrary.org/obo/ARO_3001916 CTX-M-54 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-54 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001917 CTX-M-55 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-55 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3001918 CTX-M-56 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-56 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001919 CTX-M-58 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-58 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001920 CTX-M-59 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-59 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001921 CTX-M-60 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-60 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001922 CTX-M-61 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-61 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3001923 CTX-M-62 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-62 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001924 CTX-M-63 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-63 is a beta-lactamase found in Salmonella enterica. http://purl.obolibrary.org/obo/ARO_3001925 CTX-M-64 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-64 is a beta-lactamase found in Shigella sonnei. http://purl.obolibrary.org/obo/ARO_3001926 CTX-M-65 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-65 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001927 CTX-M-66 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-66 is a beta-lactamase found in Proteus mirabilis. http://purl.obolibrary.org/obo/ARO_3001928 CTX-M-67 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-67 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001929 CTX-M-68 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-68 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3001930 CTX-M-69 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-69 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001931 CTX-M-70 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-70 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001932 CTX-M-71 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-71 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001933 CTX-M-72 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-72 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001934 CTX-M-73 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-73 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001935 CTX-M-74 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-74 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3001936 CTX-M-75 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-75 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3001937 CTX-M-76 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-76 is a beta-lactamase found in Kluyvera spp. http://purl.obolibrary.org/obo/ARO_3001938 CTX-M-77 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-77 is a beta-lactamase found in Kluyvera spp. http://purl.obolibrary.org/obo/ARO_3001939 CTX-M-78 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-78 is a beta-lactamase found in Kluyvera georgiana. http://purl.obolibrary.org/obo/ARO_3001940 CTX-M-79 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-79 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001941 CTX-M-80 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-80 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001942 CTX-M-81 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-81 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001943 CTX-M-82 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-82 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3001944 CTX-M-83 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-83 is a beta-lactamase found in Salmonella enterica. http://purl.obolibrary.org/obo/ARO_3001945 CTX-M-84 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-84 is a beta-lactamase found in Salmonella enterica. http://purl.obolibrary.org/obo/ARO_3001946 CTX-M-86 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-86 is a beta-lactamase found in Salmonella enterica. http://purl.obolibrary.org/obo/ARO_3001947 CTX-M-87 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-87 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001948 CTX-M-88 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-88 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001949 CTX-M-89 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-89 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3001950 CTX-M-90 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-90 is a beta-lactamase found in Proteus mirabilis. http://purl.obolibrary.org/obo/ARO_3001951 CTX-M-91 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-91 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001952 CTX-M-92 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-92 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001953 CTX-M-93 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-93 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001954 CTX-M-94 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-94 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001955 CTX-M-95 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-95 is a beta-lactamase found in Kluyvera spp. http://purl.obolibrary.org/obo/ARO_3001956 CTX-M-96 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-96 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001957 CTX-M-98 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-98 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001958 CTX-M-99 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-99 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3001959 CTX-M-100 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-100 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001960 CTX-M-101 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-101 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001961 CTX-M-102 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-102 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001962 CTX-M-103 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-103 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001963 CTX-M-104 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-104 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001965 CTX-M-105 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-105 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001966 CTX-M-106 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-106 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001967 CTX-M-107 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-107 is a beta-lactamase found in Shigella spp. http://purl.obolibrary.org/obo/ARO_3001968 CTX-M-108 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-108 is a beta-lactamase found in Shigella spp. http://purl.obolibrary.org/obo/ARO_3001969 CTX-M-109 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-109 is a beta-lactamase found in Shigella spp. http://purl.obolibrary.org/obo/ARO_3001970 CTX-M-110 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-110 is a beta-lactamase found in Shigella spp. http://purl.obolibrary.org/obo/ARO_3001971 CTX-M-111 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-111 is a beta-lactamase found in Shigella spp. http://purl.obolibrary.org/obo/ARO_3001972 CTX-M-112 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-112 is a beta-lactamase found in Shigella spp. http://purl.obolibrary.org/obo/ARO_3001973 CTX-M-113 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-113 is a beta-lactamase found in Shigella spp. http://purl.obolibrary.org/obo/ARO_3001974 CTX-M-114 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-114 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001975 CTX-M-115 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-115 is a beta-lactamase found in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3001976 CTX-M-116 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-116 is a beta-lactamase found in Proteus mirabilis. http://purl.obolibrary.org/obo/ARO_3001977 CTX-M-117 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-117 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001978 CTX-M-119 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-119 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001979 CTX-M-120 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-120 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001980 CTX-M-121 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-121 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001981 CTX-M-122 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-122 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001982 CTX-M-123 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-123 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001983 CTX-M-124 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-124 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001984 CTX-M-125 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-125 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001985 CTX-M-126 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-126 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001986 CTX-M-127 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-127 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001987 CTX-M-128 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-128 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001988 CTX-M-129 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-129 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001989 CTX-M-130 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-130 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001990 CTX-M-131 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-131 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001991 CTX-M-132 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-132 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001992 CTX-M-134 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-134 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001993 CTX-M-135 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase The beta-lactamase name CTX-M-135 has been depreciated. http://purl.obolibrary.org/obo/ARO_3001994 CTX-M-137 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-137 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3001995 CTX-M-136 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-136 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001996 CTX-M-138 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-138 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001997 CTX-M-139 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-139 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001998 CTX-M-140 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-140 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3001999 CTX-M-141 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-141 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002000 CTX-M-142 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-142 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002001 CTX-M-143 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-143 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002002 CTX-M-144 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-144 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002003 CTX-M-145 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-145 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002004 CTX-M-146 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-146 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002005 CTX-M-147 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-147 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002006 CTX-M-148 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-148 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002007 CTX-M-150 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-150 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002008 CTX-M-151 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-151 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002009 CTX-M-152 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-152 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002010 CTX-M-153 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-153 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002011 CTX-M-154 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-154 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002012 CMY-1 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-1 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3002013 CMY-2 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-2 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002014 CMY-3 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-3 is a beta-lactamase found in Proteus mirabilis. Sequence data unavailable. http://purl.obolibrary.org/obo/ARO_3002015 CMY-4 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-4 is a beta-lactamase found in Proteus mirabilis. http://purl.obolibrary.org/obo/ARO_3002016 CMY-5 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-5 is a beta-lactamase found in Klebsiella oxytoca. http://purl.obolibrary.org/obo/ARO_3002017 CMY-6 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-6 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002018 CMY-7 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-7 is a beta-lactamase found in Salmonella typhimurium. http://purl.obolibrary.org/obo/ARO_3002019 CMY-8 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-8 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002020 CMY-9 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-9 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002021 CMY-10 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-10 is a beta-lactamase found in Klebsiella aerogenes. http://purl.obolibrary.org/obo/ARO_3002022 CMY-11 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-11 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002023 CMY-12 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-12 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3002024 CMY-13 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-13 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002025 CMY-14 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-14 is a beta-lactamase found in Proteus mirabilis. http://purl.obolibrary.org/obo/ARO_3002026 CMY-15 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-15 is a beta-lactamase found in Proteus mirabilis. http://purl.obolibrary.org/obo/ARO_3002027 CMY-16 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-16 is a beta-lactamase found in Proteus mirabilis. http://purl.obolibrary.org/obo/ARO_3002028 CMY-17 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-17 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002029 CMY-18 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-18 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3002030 CMY-19 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-19 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002031 CMY-20 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-20 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002032 CMY-21 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-21 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002033 CMY-22 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-22 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002034 CMY-23 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-23 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3002035 CMY-24 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-24 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3002036 CMY-25 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-25 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3002037 CMY-26 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-26 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3002038 CMY-27 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-27 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3002039 CMY-28 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-28 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002040 CMY-29 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-29 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3002041 CMY-30 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-30 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002042 CMY-31 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-31 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3002043 CMY-32 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-32 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002044 CMY-33 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-33 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002045 CMY-34 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-34 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002046 CMY-35 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-35 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002047 CMY-36 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-36 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002048 CMY-37 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-37 is a beta-lactamase found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3002049 CMY-38 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-38 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3002050 CMY-39 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-39 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002051 CMY-40 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-40 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3002052 CMY-41 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-41 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3002053 CMY-42 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-42 is a plasmid-borne AmpC cephalosporinase gene found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002054 CMY-43 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-43 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002055 CMY-44 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-44 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002056 CMY-45 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-45 is a beta-lactamase found in Proteus mirabilis. http://purl.obolibrary.org/obo/ARO_3002057 CMY-46 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-46 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002058 CMY-47 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-47 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002059 CMY-48 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-48 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002060 CMY-49 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-49 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002061 CMY-50 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-50 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002062 CMY-51 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-51 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002063 CMY-52 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-52 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002064 CMY-53 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-53 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002065 CMY-54 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-54 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3002066 CMY-55 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-55 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3002067 CMY-56 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-56 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3002068 CMY-57 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-57 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3002069 CMY-59 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-59 is a beta-lactamase found in Shigella spp. http://purl.obolibrary.org/obo/ARO_3002070 CMY-99 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-99 is a beta-lactamase found in Proteus mirabilis. http://purl.obolibrary.org/obo/ARO_3002071 CMY-110 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-110 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002072 CMY-58 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-58 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002073 CMY-60 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-60 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002074 CMY-61 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-61 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002075 CMY-62 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-62 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002076 CMY-63 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-63 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002077 CMY-64 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-64 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002078 CMY-65 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-65 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002079 CMY-66 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-66 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002080 CMY-67 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-67 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002081 CMY-68 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-68 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002082 CMY-69 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-69 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002083 CMY-70 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-70 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002084 CMY-71 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-71 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002085 CMY-72 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-72 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002086 CMY-73 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-73 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002087 CMY-74 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-74 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002088 CMY-75 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-75 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002089 CMY-76 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-76 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002090 CMY-77 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-77 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002091 CMY-78 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-78 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002092 CMY-79 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-79 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002093 CMY-80 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-80 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002094 CMY-81 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-81 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002095 CMY-82 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-82 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002096 CMY-83 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-83 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002097 CMY-84 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-84 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002098 CMY-85 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-85 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002099 CMY-86 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-86 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002100 CMY-87 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-87 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002101 CMY-88 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-88 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002102 CMY-89 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-89 is a beta-lactamase found in Citrobacter freundii. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3002103 CMY-90 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-90 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002104 CMY-91 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-91 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002105 CMY-92 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-92 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002106 CMY-93 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-93 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002107 CMY-94 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-94 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002108 CMY-95 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-95 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002109 CMY-96 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-96 is a beta-lactamase found in Escherichia coli. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3002110 CMY-97 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-97 is a beta-lactamase found in Escherichia coli. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3002111 CMY-98 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-98 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002112 CMY-100 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-100 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002113 CMY-101 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-101 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002114 CMY-102 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-102 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002115 CMY-103 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-103 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002116 CMY-104 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-104 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002117 CMY-105 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-105 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002118 CMY-106 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-106 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002119 CMY-107 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-107 is a beta-lactamase found in Escherichia coli. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3002120 CMY-108 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-108 is a beta-lactamase present in plasmids of clinical Escherichia coli from humans and companion animals in the upper Midwestern USA . Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002121 CMY-109 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-109 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002122 CMY-111 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-111 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002123 CMY-112 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-112 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002124 CMY-113 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-113 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002125 CMY-114 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-114 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002126 CMY-115 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-115 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002127 CMY-116 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-116 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002128 CMY-117 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-117 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002129 CMY-118 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-118 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002130 CMY-119 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-119 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002131 CMY-120 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-120 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002132 DHA-1 http://purl.obolibrary.org/obo/ARO_3000068 DHA beta-lactamase DHA-1 is a class C beta-lactamase found in Morganella morganii and Salmonella enterica. http://purl.obolibrary.org/obo/ARO_3002133 DHA-2 http://purl.obolibrary.org/obo/ARO_3000068 DHA beta-lactamase DHA-2 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002134 DHA-3 http://purl.obolibrary.org/obo/ARO_3000068 DHA beta-lactamase DHA-3 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002135 DHA-6 http://purl.obolibrary.org/obo/ARO_3000068 DHA beta-lactamase DHA-6 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3002136 DHA-7 http://purl.obolibrary.org/obo/ARO_3000068 DHA beta-lactamase DHA-7 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3002137 DHA-4 http://purl.obolibrary.org/obo/ARO_3000068 DHA beta-lactamase DHA-4 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002138 DHA-5 http://purl.obolibrary.org/obo/ARO_3000068 DHA beta-lactamase DHA-5 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002139 DHA-8 http://purl.obolibrary.org/obo/ARO_3000068 DHA beta-lactamase DHA-8 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002140 DHA-9 http://purl.obolibrary.org/obo/ARO_3000068 DHA beta-lactamase DHA-9 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002141 DHA-10 http://purl.obolibrary.org/obo/ARO_3000068 DHA beta-lactamase DHA-10 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002142 DHA-11 http://purl.obolibrary.org/obo/ARO_3000068 DHA beta-lactamase DHA-11 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002143 DHA-12 http://purl.obolibrary.org/obo/ARO_3000068 DHA beta-lactamase DHA-12 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002144 DHA-13 http://purl.obolibrary.org/obo/ARO_3000068 DHA beta-lactamase DHA-13 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002145 DHA-14 http://purl.obolibrary.org/obo/ARO_3000068 DHA beta-lactamase DHA-14 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002146 DHA-15 http://purl.obolibrary.org/obo/ARO_3000068 DHA beta-lactamase DHA-15 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002147 DHA-16 http://purl.obolibrary.org/obo/ARO_3000068 DHA beta-lactamase DHA-16 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002148 DHA-17 http://purl.obolibrary.org/obo/ARO_3000068 DHA beta-lactamase DHA-17 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002149 DHA-18 http://purl.obolibrary.org/obo/ARO_3000068 DHA beta-lactamase DHA-18 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002150 DHA-19 http://purl.obolibrary.org/obo/ARO_3000068 DHA beta-lactamase DHA-19 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002151 DHA-20 http://purl.obolibrary.org/obo/ARO_3000068 DHA beta-lactamase DHA-20 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002152 DHA-21 http://purl.obolibrary.org/obo/ARO_3000068 DHA beta-lactamase DHA-21 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002153 DHA-22 http://purl.obolibrary.org/obo/ARO_3000068 DHA beta-lactamase DHA-22 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002154 DHA-23 http://purl.obolibrary.org/obo/ARO_3000068 DHA beta-lactamase DHA-23 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002155 FOX-1 http://purl.obolibrary.org/obo/ARO_3000067 FOX beta-lactamase FOX-1 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002156 FOX-2 http://purl.obolibrary.org/obo/ARO_3000067 FOX beta-lactamase FOX-2 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002157 FOX-3 http://purl.obolibrary.org/obo/ARO_3000067 FOX beta-lactamase FOX-3 is a beta-lactamase found in Klebsiella oxytoca. http://purl.obolibrary.org/obo/ARO_3002158 FOX-4 http://purl.obolibrary.org/obo/ARO_3000067 FOX beta-lactamase FOX-4 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002159 FOX-5 http://purl.obolibrary.org/obo/ARO_3000067 FOX beta-lactamase FOX-5 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002160 FOX-7 http://purl.obolibrary.org/obo/ARO_3000067 FOX beta-lactamase FOX-7 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002161 FOX-8 http://purl.obolibrary.org/obo/ARO_3000067 FOX beta-lactamase FOX-8 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3002162 FOX-10 http://purl.obolibrary.org/obo/ARO_3000067 FOX beta-lactamase FOX-10 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002163 FOX-9 http://purl.obolibrary.org/obo/ARO_3000067 FOX beta-lactamase FOX-9 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002164 FOX-11 http://purl.obolibrary.org/obo/ARO_3000067 FOX beta-lactamase FOX-11 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002165 FOX-12 http://purl.obolibrary.org/obo/ARO_3000067 FOX beta-lactamase FOX-12 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002166 MIR-1 http://purl.obolibrary.org/obo/ARO_3000058 MIR beta-lactamase MIR-1 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002167 MIR-4 http://purl.obolibrary.org/obo/ARO_3000058 MIR beta-lactamase MIR-4 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002168 MIR-2 http://purl.obolibrary.org/obo/ARO_3000058 MIR beta-lactamase MIR-2 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002169 MIR-3 http://purl.obolibrary.org/obo/ARO_3000058 MIR beta-lactamase MIR-3 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002170 MIR-5 http://purl.obolibrary.org/obo/ARO_3000058 MIR beta-lactamase MIR-5 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002171 MIR-6 http://purl.obolibrary.org/obo/ARO_3000058 MIR beta-lactamase MIR-6 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002172 MIR-7 http://purl.obolibrary.org/obo/ARO_3000058 MIR beta-lactamase MIR-7 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002174 MIR-9 http://purl.obolibrary.org/obo/ARO_3000058 MIR beta-lactamase MIR-9 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002175 MIR-10 http://purl.obolibrary.org/obo/ARO_3000058 MIR beta-lactamase MIR-10 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002176 MIR-11 http://purl.obolibrary.org/obo/ARO_3000058 MIR beta-lactamase MIR-11 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002177 MIR-12 http://purl.obolibrary.org/obo/ARO_3000058 MIR beta-lactamase MIR-12 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002178 MIR-13 http://purl.obolibrary.org/obo/ARO_3000058 MIR beta-lactamase MIR-13 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002179 MIR-14 http://purl.obolibrary.org/obo/ARO_3000058 MIR beta-lactamase MIR-14 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002180 MIR-15 http://purl.obolibrary.org/obo/ARO_3000058 MIR beta-lactamase MIR-15 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002181 MIR-16 http://purl.obolibrary.org/obo/ARO_3000058 MIR beta-lactamase MIR-16 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002182 MOX-1 http://purl.obolibrary.org/obo/ARO_3000083 MOX beta-lactamase MOX-1 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002183 MOX-2 http://purl.obolibrary.org/obo/ARO_3000083 MOX beta-lactamase MOX-2 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002184 MOX-4 http://purl.obolibrary.org/obo/ARO_3000083 MOX beta-lactamase MOX-4 is a beta-lactamase found in Aeromonas caviae. http://purl.obolibrary.org/obo/ARO_3002185 MOX-6 http://purl.obolibrary.org/obo/ARO_3000083 MOX beta-lactamase MOX-6 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002186 MOX-3 http://purl.obolibrary.org/obo/ARO_3000083 MOX beta-lactamase MOX-3 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002188 MOX-5 http://purl.obolibrary.org/obo/ARO_3000083 MOX beta-lactamase MOX-5 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002189 MOX-7 http://purl.obolibrary.org/obo/ARO_3000083 MOX beta-lactamase MOX-7 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002190 MOX-8 http://purl.obolibrary.org/obo/ARO_3000083 MOX beta-lactamase MOX-8 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002191 MOX-9 http://purl.obolibrary.org/obo/ARO_3000083 MOX beta-lactamase MOX-9 is a beta-lactamase found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3002192 IMP-1 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-1 is a beta-lactamase found in Serratia marcescens. http://purl.obolibrary.org/obo/ARO_3002193 IMP-2 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-2 is a beta-lactamase found in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3002194 IMP-3 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-3 is a beta-lactamase found in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3002195 IMP-4 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-4 is a beta-lactamase found in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3002196 IMP-5 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-5 is a beta-lactamase found in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3002197 IMP-6 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-6 is a beta-lactamase found in Serratia marcescens. http://purl.obolibrary.org/obo/ARO_3002198 IMP-7 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-7 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002199 IMP-8 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-8 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002200 IMP-9 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-9 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002201 IMP-10 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-10 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002202 IMP-11 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-11 is a beta-lactamase found in Pseudomonas and Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3002203 IMP-12 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-12 is a beta-lactamase found in Pseudomonas putida. http://purl.obolibrary.org/obo/ARO_3002204 IMP-13 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-13 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002205 IMP-14 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-14 is a beta-lactamase found in Pseudomonas and Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3002206 IMP-15 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-15 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002207 IMP-16 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-16 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002208 IMP-17 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-17 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002209 IMP-18 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-18 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002210 IMP-19 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-19 is a beta-lactamase found in Aeromonas caviae. http://purl.obolibrary.org/obo/ARO_3002211 IMP-20 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-20 is a beta-lactamase found in Pseudomonas and Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3002212 IMP-21 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-21 is a beta-lactamase found in Pseudomonas and Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3002213 IMP-22 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-22 is a beta-lactamase found in Pseudomonas spp. http://purl.obolibrary.org/obo/ARO_3002214 IMP-23 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-23 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002215 IMP-24 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-24 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002216 IMP-25 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-25 is a beta-lactamase found in Serratia marcescens. http://purl.obolibrary.org/obo/ARO_3002217 IMP-26 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-26 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002218 IMP-27 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-27 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002219 IMP-28 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-28 is a beta-lactamase found in Klebsiella oxytoca. http://purl.obolibrary.org/obo/ARO_3002220 IMP-29 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-29 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002221 IMP-30 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-30 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002222 IMP-31 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-31 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002223 IMP-32 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-32 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002224 IMP-33 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-33 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002225 IMP-34 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-34 is a beta-lactamase found in Klebsiella spp. http://purl.obolibrary.org/obo/ARO_3002226 IMP-35 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-35 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002227 IMP-36 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-36 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002228 IMP-37 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-37 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002229 IMP-38 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-38 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002230 IMP-39 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-39 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002231 IMP-40 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-40 is a beta-lactamase found in Pseudomonas and Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3002232 IMP-41 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-41 is a beta-lactamase found in Pseudomonas and Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3002233 IMP-42 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-42 is a beta-lactamase found in Pseudomonas and Acinetobacter spp. http://purl.obolibrary.org/obo/ARO_3002234 IMP-43 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-43 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002235 IMP-44 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-44 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002236 IMP-45 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-45 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002237 IMP-46 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-46 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002239 IMP-48 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-48 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002240 CARB-1 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-1 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002241 CARB-2 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-2 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002242 CARB-3 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-3 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002243 CARB-4 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-4 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002244 CARB-5 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-5 is a beta-lactamase found in Acinetobacter calcoaceticus. http://purl.obolibrary.org/obo/ARO_3002245 CARB-6 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-6 is a beta-lactamase found in Vibrio cholerae. http://purl.obolibrary.org/obo/ARO_3002246 CARB-7 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-7 is a beta-lactamase found in Vibrio cholerae. http://purl.obolibrary.org/obo/ARO_3002247 CARB-8 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-8 is a beta-lactamase found in Oligella urethralis. http://purl.obolibrary.org/obo/ARO_3002248 CARB-9 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-9 is a beta-lactamase found in Vibrio cholerae. http://purl.obolibrary.org/obo/ARO_3002249 CARB-10 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-10 is a beta-lactamase found in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3002250 CARB-12 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-12 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002251 CARB-13 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-13 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002252 CARB-14 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-14 is a beta-lactamase found in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3002253 CARB-15 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-15 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002254 CARB-17 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-17 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002255 CARB-16 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-16 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002256 IND-1 http://purl.obolibrary.org/obo/ARO_3000060 IND beta-lactamase IND-1 is a beta-lactamase found in Chryseobacterium indologenes. http://purl.obolibrary.org/obo/ARO_3002257 IND-2 http://purl.obolibrary.org/obo/ARO_3000060 IND beta-lactamase IND-2 is a beta-lactamase found in Chryseobacterium indologenes. http://purl.obolibrary.org/obo/ARO_3002258 IND-2a http://purl.obolibrary.org/obo/ARO_3000060 IND beta-lactamase IND-2a is a beta-lactamase found in Chryseobacterium indologenes. http://purl.obolibrary.org/obo/ARO_3002259 IND-3 http://purl.obolibrary.org/obo/ARO_3000060 IND beta-lactamase IND-3 is a beta-lactamase found in Chryseobacterium indologenes. http://purl.obolibrary.org/obo/ARO_3002260 IND-4 http://purl.obolibrary.org/obo/ARO_3000060 IND beta-lactamase IND-4 is a beta-lactamase found in Chryseobacterium indologenes. http://purl.obolibrary.org/obo/ARO_3002261 IND-5 http://purl.obolibrary.org/obo/ARO_3000060 IND beta-lactamase IND-5 is a beta-lactamase found in Chryseobacterium indologenes. http://purl.obolibrary.org/obo/ARO_3002262 IND-6 http://purl.obolibrary.org/obo/ARO_3000060 IND beta-lactamase IND-6 is a beta-lactamase found in Chryseobacterium indologenes. http://purl.obolibrary.org/obo/ARO_3002263 IND-7 http://purl.obolibrary.org/obo/ARO_3000060 IND beta-lactamase IND-7 is a beta-lactamase found in Chryseobacterium indologenes. http://purl.obolibrary.org/obo/ARO_3002264 IND-8 http://purl.obolibrary.org/obo/ARO_3000060 IND beta-lactamase IND-8 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002265 IND-9 http://purl.obolibrary.org/obo/ARO_3000060 IND beta-lactamase IND-9 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002266 IND-10 http://purl.obolibrary.org/obo/ARO_3000060 IND beta-lactamase IND-10 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002267 IND-11 http://purl.obolibrary.org/obo/ARO_3000060 IND beta-lactamase IND-11 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002268 IND-12 http://purl.obolibrary.org/obo/ARO_3000060 IND beta-lactamase IND-12 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002269 IND-14 http://purl.obolibrary.org/obo/ARO_3000060 IND beta-lactamase IND-14 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002270 IND-15 http://purl.obolibrary.org/obo/ARO_3000060 IND beta-lactamase IND-15 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002271 VIM-1 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-1 is a beta-lactamase found in Pseudomonas spp. http://purl.obolibrary.org/obo/ARO_3002272 VIM-2 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-2 is a beta-lactamase found in Pseudomonas spp. http://purl.obolibrary.org/obo/ARO_3002273 VIM-3 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-3 is a beta-lactamase found in Pseudomonas spp. http://purl.obolibrary.org/obo/ARO_3002274 VIM-4 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-4 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002275 VIM-5 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-5 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002276 VIM-6 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-6 is a beta-lactamase found in Pseudomonas spp. http://purl.obolibrary.org/obo/ARO_3002277 VIM-7 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-7 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002278 VIM-8 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-8 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002279 VIM-9 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-9 is a beta-lactamase found in Pseudomonas spp. http://purl.obolibrary.org/obo/ARO_3002280 VIM-10 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-10 is a beta-lactamase found in Pseudomonas spp. http://purl.obolibrary.org/obo/ARO_3002281 VIM-11 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-11 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002282 VIM-12 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-12 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002283 VIM-13 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-13 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002284 VIM-14 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-14 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002285 VIM-15 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-15 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002286 VIM-16 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-16 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002287 VIM-17 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-17 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002288 VIM-18 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-18 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002289 VIM-19 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-19 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3002290 VIM-20 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-20 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002291 VIM-21 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-21 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002292 VIM-22 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-22 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002293 VIM-23 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-23 is a beta-lactamase found in Enterobacter cloacae. http://purl.obolibrary.org/obo/ARO_3002294 VIM-24 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-24 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002295 VIM-25 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-25 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002296 VIM-26 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-26 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002297 VIM-27 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-27 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002298 VIM-28 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-28 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002299 VIM-29 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-29 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3002300 VIM-30 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-30 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3002301 VIM-31 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-31 is a beta-lactamase found in Enterobacter cloacae. http://purl.obolibrary.org/obo/ARO_3002302 VIM-32 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-32 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002303 VIM-33 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-33 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002304 VIM-34 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-34 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002305 VIM-35 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-35 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002306 VIM-36 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-36 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002307 VIM-37 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-37 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002308 VIM-38 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-38 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002309 VIM-39 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-39 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002310 VIM-40 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-40 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002311 VIM-41 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-41 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002312 KPC-2 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-2 is a beta-lactamase found in Klebsiella pneumoniae and Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002313 KPC-3 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-3 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002314 KPC-4 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-4 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002315 KPC-5 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-5 is a beta-lactamase found in Klebsiella pneumoniae and Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002316 KPC-6 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-6 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002317 KPC-7 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-7 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002318 KPC-8 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-8 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002319 KPC-9 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-9 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002320 KPC-10 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-10 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002321 KPC-11 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-11 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002322 KPC-12 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-12 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002323 KPC-13 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-13 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002324 KPC-14 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-14 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002325 KPC-15 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-15 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002326 KPC-16 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-16 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002327 KPC-17 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-17 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002328 KPC-18 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-18 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002329 KPC-19 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-19 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002330 GES-1 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-1 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002331 GES-2 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-2 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002332 GES-3 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-3 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002333 GES-4 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-4 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002334 GES-5 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-5 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3002335 GES-6 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-6 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3002336 GES-7 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-7 is a beta-lactamase found in Enterobacter cloacae. http://purl.obolibrary.org/obo/ARO_3002337 GES-8 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-8 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002338 GES-9 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-9 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002339 GES-10 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-10 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002340 GES-11 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-11 is a beta-lactamase found in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3002341 GES-12 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-12 is a beta-lactamase found in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3002342 GES-13 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-13 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002343 GES-14 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-14 is a beta-lactamase found in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3002344 GES-15 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-15 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002345 GES-16 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-16 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002346 GES-17 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-17 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002347 GES-18 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-18 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002348 GES-19 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-19 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3002349 GES-20 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-20 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3002350 GES-21 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-21 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002351 GES-22 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-22 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002352 GES-23 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-23 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002353 GES-24 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-24 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002354 NDM-3 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase NDM-3 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3002355 NDM-4 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase NDM-4 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002356 NDM-6 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase NDM-6 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3002357 NDM-7 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase NDM-7 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002358 NDM-8 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase NDM-8 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002359 NDM-9 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase NDM-9 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002360 NDM-10 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase NDM-10 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002361 NDM-11 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase NDM-11 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002362 NDM-12 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase NDM-12 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002363 PER-1 http://purl.obolibrary.org/obo/ARO_3000056 PER beta-lactamase PER-1 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002364 PER-2 http://purl.obolibrary.org/obo/ARO_3000056 PER beta-lactamase PER-2 is a beta-lactamase found in Salmonella typhimurium. http://purl.obolibrary.org/obo/ARO_3002365 PER-3 http://purl.obolibrary.org/obo/ARO_3000056 PER beta-lactamase PER-3 is a beta-lactamase found in Aeromonas spp. http://purl.obolibrary.org/obo/ARO_3002366 PER-4 http://purl.obolibrary.org/obo/ARO_3000056 PER beta-lactamase PER-4 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002367 PER-5 http://purl.obolibrary.org/obo/ARO_3000056 PER beta-lactamase PER-5 is a beta-lactamase found in the Enterobacteriaceae family. http://purl.obolibrary.org/obo/ARO_3002368 PER-6 http://purl.obolibrary.org/obo/ARO_3000056 PER beta-lactamase PER-6 is a beta-lactamase found in Aeromonas allosaccharophila. http://purl.obolibrary.org/obo/ARO_3002369 PER-7 http://purl.obolibrary.org/obo/ARO_3000056 PER beta-lactamase PER-7 is a beta-lactamase found in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3002370 VEB-1 http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase VEB-1 is a beta-lactamase found in Escherichia coli and Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002371 VEB-2 http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase VEB-2 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002372 VEB-3 http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase VEB-3 is a beta-lactamase found in Enterobacter cloacae. http://purl.obolibrary.org/obo/ARO_3002373 VEB-4 http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase VEB-4 is a beta-lactamase found in Proteus mirabilis. http://purl.obolibrary.org/obo/ARO_3002374 VEB-6 http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase VEB-6 is a beta-lactamase found in Proteus mirabilis. http://purl.obolibrary.org/obo/ARO_3002375 VEB-5 http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase VEB-5 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002376 VEB-7 http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase VEB-7 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002377 VEB-8 http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase VEB-8 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002378 VEB-9 http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase VEB-9 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002379 SME-1 http://purl.obolibrary.org/obo/ARO_3000055 SME beta-lactamase SME-1 is a beta-lactamase found in Serratia marcescens. http://purl.obolibrary.org/obo/ARO_3002380 SME-2 http://purl.obolibrary.org/obo/ARO_3000055 SME beta-lactamase SME-2 is a beta-lactamase found in Serratia marcescens. http://purl.obolibrary.org/obo/ARO_3002381 SME-3 http://purl.obolibrary.org/obo/ARO_3000055 SME beta-lactamase SME-3 is a beta-lactamase found in Serratia marcescens. http://purl.obolibrary.org/obo/ARO_3002382 SME-4 http://purl.obolibrary.org/obo/ARO_3000055 SME beta-lactamase SME-4 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002383 SME-5 http://purl.obolibrary.org/obo/ARO_3000055 SME beta-lactamase SME-5 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002384 BEL beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase BEL beta-lactamases are class A expanded-spectrum beta-lactamases that are inhibited by clavulanic acid. They are chromosomally encoded and hydrolyze most cephalosporins and aztreonam. http://purl.obolibrary.org/obo/ARO_3002385 BEL-1 http://purl.obolibrary.org/obo/ARO_3002384 BEL beta-lactamase BEL-1 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002386 BEL-2 http://purl.obolibrary.org/obo/ARO_3002384 BEL beta-lactamase BEL-2 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002387 BEL-3 http://purl.obolibrary.org/obo/ARO_3002384 BEL beta-lactamase BEL-3 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase OXY beta-lactamases are chromosomal class A beta-lactamases that are found in Klebsiella oxytoca. At constitutive low levels, OXY beta-lactamases confer resistance to aminopenicillins and carboxypenicillins. At high induced levels, OXY beta-lactamases confer resistance to penicillins, cephalosporins and aztreonam. http://purl.obolibrary.org/obo/ARO_3002389 OXY-1-1 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase OXY-1-1 is a beta-lactamase found in Klebsiella oxytoca. http://purl.obolibrary.org/obo/ARO_3002390 OXY-1-2 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase OXY-1-2 is a beta-lactamase found in Klebsiella oxytoca. http://purl.obolibrary.org/obo/ARO_3002391 OXY-1-3 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase OXY-1-3 is a beta-lactamase found in Klebsiella oxytoca. http://purl.obolibrary.org/obo/ARO_3002392 OXY-1-4 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase OXY-1-4 is a beta-lactamase found in Klebsiella oxytoca. http://purl.obolibrary.org/obo/ARO_3002394 OXY-1-6 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase OXY-1-6 is a beta-lactamase found in Klebsiella oxytoca. http://purl.obolibrary.org/obo/ARO_3002396 OXY-2-1 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase OXY-2-1 is a beta-lactamase found in Klebsiella oxytoca. http://purl.obolibrary.org/obo/ARO_3002397 OXY-2-2 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase OXY-2-2 is a beta-lactamase found in Klebsiella oxytoca. http://purl.obolibrary.org/obo/ARO_3002398 OXY-2-3 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase OXY-2-3 is a beta-lactamase found in Klebsiella oxytoca. http://purl.obolibrary.org/obo/ARO_3002399 OXY-2-4 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase OXY-2-4 is a beta-lactamase found in Klebsiella oxytoca. http://purl.obolibrary.org/obo/ARO_3002400 OXY-2-5 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase OXY-2-5 is a beta-lactamase found in Klebsiella oxytoca. http://purl.obolibrary.org/obo/ARO_3002401 OXY-2-6 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase OXY-2-6 is a beta-lactamase found in Klebsiella oxytoca. http://purl.obolibrary.org/obo/ARO_3002402 OXY-2-7 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase OXY-2-7 is a beta-lactamase found in Klebsiella oxytoca. http://purl.obolibrary.org/obo/ARO_3002403 OXY-2-8 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase OXY-2-8 is a beta-lactamase found in Klebsiella oxytoca. http://purl.obolibrary.org/obo/ARO_3002404 OXY-2-9 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase OXY-2-9 is a beta-lactamase found in Klebsiella oxytoca. http://purl.obolibrary.org/obo/ARO_3002405 OXY-2-10 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase OXY-2-10 is a beta-lactamase. From the Pasteur Institute (Genopole) list of OXY beta-lactamases. http://purl.obolibrary.org/obo/ARO_3002406 OXY-2-11 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase OXY-2-11 is a beta-lactamase. From the Pasteur Institute (Genopole) list of OXY beta-lactamases. http://purl.obolibrary.org/obo/ARO_3002407 OXY-2-12 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase OXY-2-12 is a beta-lactamase. From the Pasteur Institute (Genopole) list of OXY beta-lactamases. http://purl.obolibrary.org/obo/ARO_3002408 OXY-2-13 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase OXY-2-13 is a beta-lactamase. From the Pasteur Institute (Genopole) list of OXY beta-lactamases. http://purl.obolibrary.org/obo/ARO_3002409 OXY-3-1 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase OXY-3-1 is a beta-lactamase found in Klebsiella oxytoca. http://purl.obolibrary.org/obo/ARO_3002410 OXY-4-1 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase OXY-4-1 is a beta-lactamase found in Klebsiella oxytoca. http://purl.obolibrary.org/obo/ARO_3002411 OXY-5-1 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase OXY-5-1 is a beta-lactamase found in Klebsiella oxytoca. http://purl.obolibrary.org/obo/ARO_3002412 OXY-5-2 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase OXY-5-2 is a beta-lactamase found in Klebsiella oxytoca. http://purl.obolibrary.org/obo/ARO_3002413 OXY-6-1 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase OXY-6-1 is a beta-lactamase found in Klebsiella oxytoca. http://purl.obolibrary.org/obo/ARO_3002414 OXY-6-2 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase OXY-6-2 is a beta-lactamase found in Klebsiella oxytoca. http://purl.obolibrary.org/obo/ARO_3002415 OXY-6-3 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase OXY-6-3 is a beta-lactamase found in Klebsiella oxytoca. http://purl.obolibrary.org/obo/ARO_3002416 OXY-6-4 http://purl.obolibrary.org/obo/ARO_3002388 OXY beta-lactamase OXY-6-4 is a beta-lactamase found in Klebsiella oxytoca. http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase OKP beta-lactamases are chromosomal class A beta-lactamase that confer resistance to penicillins and early cephalosporins in Klebsiella pneumoniae. OKP beta-lactamases can be subdivided into two groups: OKP-A and OKP-B which diverge by about 4.2%. http://purl.obolibrary.org/obo/ARO_3002418 OKP-A-1 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-A-1 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002419 OKP-A-2 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-A-2 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002420 OKP-A-3 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-A-3 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002421 OKP-A-4 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-A-4 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002422 OKP-A-5 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-A-5 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002423 OKP-A-6 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-A-6 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002424 OKP-A-7 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-A-7 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002425 OKP-A-8 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-A-8 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002426 OKP-A-9 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-A-9 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002427 OKP-A-10 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-A-10 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002428 OKP-A-11 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-A-11 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002429 OKP-A-12 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-A-12 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002430 OKP-A-13 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-A-13 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002431 OKP-A-14 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-A-14 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002432 OKP-A-15 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-A-15 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002433 OKP-A-16 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-A-16 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002434 OKP-B-1 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-B-1 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002435 OKP-B-2 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-B-2 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002436 OKP-B-3 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-B-3 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002437 OKP-B-4 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-B-4 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002438 OKP-B-5 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-B-5 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002439 OKP-B-6 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-B-6 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002440 OKP-B-7 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-B-7 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002441 OKP-B-8 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-B-8 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002442 OKP-B-9 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-B-9 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002443 OKP-B-10 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-B-10 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002444 OKP-B-11 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-B-11 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002445 OKP-B-12 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-B-12 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002446 OKP-B-13 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-B-13 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002447 OKP-B-14 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-B-14 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002450 OKP-B-17 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-B-17 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002451 OKP-B-18 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-B-18 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002452 OKP-B-19 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-B-19 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002453 OKP-B-20 http://purl.obolibrary.org/obo/ARO_3002417 OKP beta-lactamase OKP-B-20 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002454 LEN-1 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase LEN-1 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002455 LEN-2 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase LEN-2 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002456 LEN-5 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase LEN-5 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002457 LEN-7 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase LEN-7 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002458 LEN-8 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase LEN-8 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002459 LEN-9 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase LEN-9 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002460 LEN-10 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase LEN-10 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002461 LEN-11 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase LEN-11 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002462 LEN-12 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase LEN-12 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002463 LEN-13 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase LEN-13 is a beta-lactamase found in Klebsiella pneumoniae and Klebsiella variicola. http://purl.obolibrary.org/obo/ARO_3002464 LEN-16 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase LEN-16 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002465 LEN-18 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase LEN-18 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002466 LEN-19 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase LEN-19 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002467 LEN-20 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase LEN-20 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002468 LEN-21 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase LEN-21 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002469 LEN-22 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase LEN-22 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002470 LEN-23 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase LEN-23 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002471 LEN-24 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase LEN-24 is a beta-lactamase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002472 LEN-4 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase LEN-4 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002473 LEN-17 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase LEN-17 is a beta-lactamase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002474 LEN-26 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase LEN-26 is a beta-lactamase found in Escherichia coli and Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002475 LEN-3 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase LEN-3 is a beta-lactamase. From the Pasteur Institute list of LEN beta-lactamases. http://purl.obolibrary.org/obo/ARO_3002476 LEN-6 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase LEN-6 is a beta-lactamase. From the Pasteur Institute list of LEN beta-lactamases. http://purl.obolibrary.org/obo/ARO_3002477 LEN-14 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase LEN-14 is a beta-lactamase. From the Pasteur Institute list of LEN beta-lactamases. http://purl.obolibrary.org/obo/ARO_3002478 LEN-15 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase LEN-15 is a beta-lactamase. From the Pasteur Institute list of LEN beta-lactamases. http://purl.obolibrary.org/obo/ARO_3002479 LEN-25 http://purl.obolibrary.org/obo/ARO_3000097 LEN beta-lactamase LEN-25 is a beta-lactamase. From the Pasteur Institute list of LEN beta-lactamases. http://purl.obolibrary.org/obo/ARO_3002480 OXA-144 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-144 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002481 AER-1 http://purl.obolibrary.org/obo/ARO_3000089 AER beta-lactamase AER-1 is a beta-lactamase found in Aeromonas hydrophila. http://purl.obolibrary.org/obo/ARO_3002482 LRA-1 http://purl.obolibrary.org/obo/ARO_3004228 class A LRA beta-lactamase LRA-1 is a beta-lactamase isolated from soil samples in Alaska. http://purl.obolibrary.org/obo/ARO_3002483 LRA-5 http://purl.obolibrary.org/obo/ARO_3004228 class A LRA beta-lactamase LRA-5 is a beta-lactamase isolated from soil samples in Alaska. http://purl.obolibrary.org/obo/ARO_3002484 LRA-13 http://purl.obolibrary.org/obo/ARO_3004241 class D LRA beta-lactamase LRA-13 is a class D/class C fusion bifunctional beta-lactamase isolated from soil samples in Alaska. http://purl.obolibrary.org/obo/ARO_3002485 LRA-2 http://purl.obolibrary.org/obo/ARO_3004226 subclass B3 LRA beta-lactamase LRA-2 is a beta-lactamase isolated from soil samples in Alaska. http://purl.obolibrary.org/obo/ARO_3002486 LRA-7 http://purl.obolibrary.org/obo/ARO_3004226 subclass B3 LRA beta-lactamase LRA-7 is a beta-lactamase isolated from soil samples in Alaska. http://purl.obolibrary.org/obo/ARO_3002487 LRA-8 http://purl.obolibrary.org/obo/ARO_3004226 subclass B3 LRA beta-lactamase LRA-8 is a beta-lactamase isolated from soil samples in Alaska. http://purl.obolibrary.org/obo/ARO_3002488 LRA-9 http://purl.obolibrary.org/obo/ARO_3004226 subclass B3 LRA beta-lactamase LRA-9 is a beta-lactamase isolated from soil samples in Alaska. http://purl.obolibrary.org/obo/ARO_3002489 LRA-10 http://purl.obolibrary.org/obo/ARO_3004231 class C LRA beta-lactamase LRA-10 is a beta-lactamase isolated from soil samples in Alaska. http://purl.obolibrary.org/obo/ARO_3002492 LRA-18 http://purl.obolibrary.org/obo/ARO_3004231 class C LRA beta-lactamase LRA-18 is a beta-lactamase isolated from soil samples in Alaska. http://purl.obolibrary.org/obo/ARO_3002493 SRT-1 http://purl.obolibrary.org/obo/ARO_3000095 SRT beta-lactamase SRT-1, isolated from Serratia marcescens, confers resistance to cephalosporins but not carbapenems, penems and monobactams. http://purl.obolibrary.org/obo/ARO_3002494 SRT-2 http://purl.obolibrary.org/obo/ARO_3000095 SRT beta-lactamase SRT-2, isolated from Serratia marcescens, is a chromosomal beta-lactamase that confers resistance to cefotaxime. http://purl.obolibrary.org/obo/ARO_3002495 CTX-M-85 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-85 is a beta-lactamase found in Salmonella enterica. http://purl.obolibrary.org/obo/ARO_3002496 OXA-418 http://purl.obolibrary.org/obo/ARO_3007709 OXA-229-like beta-lactamase OXA-418 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3002497 PDC-1 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-1 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002498 PDC-2 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-2 is a extended-spectrum beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002500 PDC-3 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-3 is a extended-spectrum beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002501 PDC-4 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-4 is a extended-spectrum beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002502 PDC-5 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-5 is a extended-spectrum beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002505 PDC-6 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-6 is a beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002506 PDC-7 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-7 is a extended-spectrum beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002507 PDC-8 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-8 is a extended-spectrum beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002508 PDC-9 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-9 is a extended-spectrum beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002509 PDC-10 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-10 is a extended-spectrum beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002510 LRA-3 http://purl.obolibrary.org/obo/ARO_3004226 subclass B3 LRA beta-lactamase LRA-3 is a beta-lactamase isolated from soil samples in Alaska. http://purl.obolibrary.org/obo/ARO_3002511 LRA-12 http://purl.obolibrary.org/obo/ARO_3004226 subclass B3 LRA beta-lactamase LRA-12 is a beta-lactamase isolated from soil samples in Alaska. http://purl.obolibrary.org/obo/ARO_3002512 LRA-17 http://purl.obolibrary.org/obo/ARO_3004226 subclass B3 LRA beta-lactamase LRA-17 is a beta-lactamase isolated from soil samples in Alaska. http://purl.obolibrary.org/obo/ARO_3002513 LRA-19 http://purl.obolibrary.org/obo/ARO_3004226 subclass B3 LRA beta-lactamase LRA-19 is a beta-lactamase isolated from soil samples in Alaska. http://purl.obolibrary.org/obo/ARO_3002514 OCH-1 http://purl.obolibrary.org/obo/ARO_3000094 OCH beta-lactamase OCH-1 beta-lactamase is an Ambler class C chromosomal-encoded beta-lactamases in Brucella anthropi. http://purl.obolibrary.org/obo/ARO_3002515 OCH-2 http://purl.obolibrary.org/obo/ARO_3000094 OCH beta-lactamase OCH-2 beta-lactamase is an Ambler class C chromosomal-encoded beta-lactamase in Brucella anthropi. http://purl.obolibrary.org/obo/ARO_3002516 OCH-3 http://purl.obolibrary.org/obo/ARO_3000094 OCH beta-lactamase OCH-3 beta-lactamase is an Ambler class C chromosomal-encoded beta-lactamases in Brucella anthropi. http://purl.obolibrary.org/obo/ARO_3002517 OCH-4 http://purl.obolibrary.org/obo/ARO_3000094 OCH beta-lactamase OCH-4 beta-lactamase is an Ambler class C chromosomal-encoded beta-lactamases in Brucella anthropi. http://purl.obolibrary.org/obo/ARO_3002518 OCH-5 http://purl.obolibrary.org/obo/ARO_3000094 OCH beta-lactamase OCH-5 beta-lactamase is an Ambler class C chromosomal-encoded beta-lactamases in Brucella anthropi. http://purl.obolibrary.org/obo/ARO_3002519 OCH-6 http://purl.obolibrary.org/obo/ARO_3000094 OCH beta-lactamase OCH-6 beta-lactamase is an Ambler class C chromosomal-encoded beta-lactamases in Brucella anthropi. http://purl.obolibrary.org/obo/ARO_3002520 OCH-7 http://purl.obolibrary.org/obo/ARO_3000094 OCH beta-lactamase OCH-7 beta-lactamase is an Ambler class C chromosomal-encoded beta-lactamase in Brucella anthropi. http://purl.obolibrary.org/obo/ARO_3002521 OCH-8 http://purl.obolibrary.org/obo/ARO_3000094 OCH beta-lactamase OCH-8 beta-lactamase is an Ambler class C chromosomal-encoded beta-lactamases in Brucella anthropi. http://purl.obolibrary.org/obo/ARO_3002522 novA http://purl.obolibrary.org/obo/ARO_0010001 ATP-binding cassette (ABC) antibiotic efflux pump A type III ABC transporter, identified on the novobiocin biosynthetic gene cluster, involved in the transport and resistance of novobiocin. http://purl.obolibrary.org/obo/ARO_3002523 AAC(2')-Ia http://purl.obolibrary.org/obo/ARO_3007393 AAC(2')-I AAC(2')-Ia is a chromosomal-encoded aminoglycoside acetyltransferase in P. stuartii. http://purl.obolibrary.org/obo/ARO_3002524 AAC(2')-Ib http://purl.obolibrary.org/obo/ARO_3007393 AAC(2')-I AAC(2')-Ib is a chromosomal-encoded aminoglycoside acetyltransferase in Mycolicibacterium fortuitum and A. baumannii. http://purl.obolibrary.org/obo/ARO_3002525 AAC(2')-Ic http://purl.obolibrary.org/obo/ARO_3007393 AAC(2')-I AAC(2')-Ic is a chromosomal-encoded aminoglycoside acetyltransferase in M. tuberculosis and Mycobacterium tuberculosis variant bovis. http://purl.obolibrary.org/obo/ARO_3002526 AAC(2')-Id http://purl.obolibrary.org/obo/ARO_3007393 AAC(2')-I AAC(2')-Id is a chromosomal-encoded aminoglycoside acetyltransferase in Mycolicibacterium smegmatis. http://purl.obolibrary.org/obo/ARO_3002527 AAC(2')-Ie http://purl.obolibrary.org/obo/ARO_3007393 AAC(2')-I AAC(2')-Ie is a chromosomal-encoded aminoglycoside acetyltransferase in M. leprae. http://purl.obolibrary.org/obo/ARO_3002528 AAC(3)-Ia http://purl.obolibrary.org/obo/ARO_3007384 AAC(3)-I AAC(3)-Ia is an aminoglycoside acetyltransferase encoded by plasmids, transposons, integrons in S. marcescens, E. coli, Acinetobacter baumannii, Klebsiella pneumoniae, Klebsiella oxytoca, P. aeruginosa, Salmonella typhimurium and Proteus mirabilis. http://purl.obolibrary.org/obo/ARO_3002529 AAC(3)-Id http://purl.obolibrary.org/obo/ARO_3007384 AAC(3)-I AAC(3)-Id is an aminoglycoside acetyltransferase encoded by genomic islands and integrons in S. enterica, P. mirabilis and Vibrio fluvialis. http://purl.obolibrary.org/obo/ARO_3002530 AAC(3)-Ib http://purl.obolibrary.org/obo/ARO_3007384 AAC(3)-I AAC(3)-Ib is an integron-encoded aminoglycoside acetyltransferase in P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3002531 AAC(3)-Ic http://purl.obolibrary.org/obo/ARO_3007384 AAC(3)-I AAC(3)-Ic is an integron-encoded aminoglycoside acetyltransferase in P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3002533 AAC(3)-IIa http://purl.obolibrary.org/obo/ARO_3007385 AAC(3)-II AAC(3)-IIa is a plasmid-encoded aminoglycoside acetyltransferase in K. pneumoniae, E. cloacae, Actinobacillus pleuropneumoniae, S. typhimurium, Citrobacter freundii, and P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3002534 AAC(3)-IIb http://purl.obolibrary.org/obo/ARO_3007385 AAC(3)-II AAC(3)-IIb is an aminoglycoside acetyltransferase in E. coli, A. faecalis and S. marcescens. http://purl.obolibrary.org/obo/ARO_3002535 AAC(3)-IIc http://purl.obolibrary.org/obo/ARO_3007385 AAC(3)-II AAC(3)-IIc is a plasmid-encoded aminoglycoside acetyltransferase in E. coli and P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3002536 AAC(3)-IIIa http://purl.obolibrary.org/obo/ARO_3007386 AAC(3)-III AAC(3)-IIIa is a chromosomal-encoded aminoglycoside acetyltransferase in P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3002537 AAC(3)-IIIb http://purl.obolibrary.org/obo/ARO_3007386 AAC(3)-III AAC(3)-IIIb is an aminoglycoside acetyltransferase in P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3002538 AAC(3)-IIIc http://purl.obolibrary.org/obo/ARO_3007386 AAC(3)-III AAC(3)-IIIc is an aminoglycoside acetyltransferase in P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3002539 AAC(3)-IVa http://purl.obolibrary.org/obo/ARO_3007387 AAC(3)-IV AAC(3)-IV is a plasmid-encoded aminoglycoside acetyltransferase in E. coli, C. jejuni and P. stutzeri. http://purl.obolibrary.org/obo/ARO_3002540 AAC(3)-VIa http://purl.obolibrary.org/obo/ARO_3007388 AAC(3)-VI AAC(3)-VIa is a plasmid-encoded aminoglycoside acetyltransferase in E. cloacae, S. enterica and E. coli. http://purl.obolibrary.org/obo/ARO_3002541 AAC(3)-VIIa http://purl.obolibrary.org/obo/ARO_3007389 AAC(3)-VII AAC(3)-VIIa is a chromosomal-encoded aminoglycoside acetyltransferase in Streptomyces rimosus. http://purl.obolibrary.org/obo/ARO_3002542 AAC(3)-VIIIa http://purl.obolibrary.org/obo/ARO_3007390 AAC(3)-VIII AAC(3)-VIIIa is a chromosomal-encoded aminoglycoside acetyltransferase in Streptomyces fradiae. http://purl.obolibrary.org/obo/ARO_3002543 AAC(3)-IXa http://purl.obolibrary.org/obo/ARO_3007391 AAC(3)-IX AAC(3)-IXa is a chromosomal-encoded aminoglycoside acetyltransferase in Micromonospora chalcea. http://purl.obolibrary.org/obo/ARO_3002544 AAC(3)-Xa http://purl.obolibrary.org/obo/ARO_3007392 AAC(3)-X AAC(3)-Xa is a chromosomal-encoded aminoglycoside acetyltransferase in Streptomyces griseus. http://purl.obolibrary.org/obo/ARO_3002545 AAC(6')-Ia http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Ia is an aminoglycoside acetyltransferase encoded by plasmids, transposons, integrons in Citrobacter diversus, E. coli, K. pneumoniae, Shigella sonnei, and P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3002546 AAC(6')-Ib http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Ib is an aminoglycoside acetyltransferase encoded by plasmids, transposons, integrons in K. pneumoniae, P. mirabilis, P. aeruginosa, S. enterica, K. oxytoca, S. maltophilia, E. cloacae and V. cholerae. http://purl.obolibrary.org/obo/ARO_3002547 AAC(6')-Ib-cr1 http://purl.obolibrary.org/obo/ARO_3005113 AAC(6')-Ib-cr AAC(6')-Ib-cr is an aminoglycoside acetyltransferase encoded by plasmids, transposons, integrons in Enterobacteriaceae. The aac(6')-Ib-cr variant gene can induce resistance against aminoglycoside and fluoroquinolone simultaneously. http://purl.obolibrary.org/obo/ARO_3002549 AAC(6')-Ic http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Ic is a chromosomal-encoded aminoglycoside acetyltransferase in S. marcescens. http://purl.obolibrary.org/obo/ARO_3002553 AAC(6')-If http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-If is a plasmid-encoded aminoglycoside acetyltransferase in E. cloacae. http://purl.obolibrary.org/obo/ARO_3002554 AAC(6')-Ig http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Ig is a chromosomal-encoded aminoglycoside acetyltransferase in Acinetobacter haemolyticus. http://purl.obolibrary.org/obo/ARO_3002555 AAC(6')-Ih http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Ih is a plasmid-encoded aminoglycoside acetyltransferase in A. baumannii. http://purl.obolibrary.org/obo/ARO_3002556 AAC(6')-Ii http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Ii is a chromosomal-encoded aminoglycoside acetyltransferase in Enterococcus spp. http://purl.obolibrary.org/obo/ARO_3002557 AAC(6')-Ij http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Ij is a chromosomal-encoded aminoglycoside acetyltransferase in Acinetobacter genomosp. 13. http://purl.obolibrary.org/obo/ARO_3002558 AAC(6')-Ik http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Ik is a chromosomal-encoded aminoglycoside acetyltransferase in Acinetobacter sp. http://purl.obolibrary.org/obo/ARO_3002559 AAC(6')-Ip http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Ip is an aminoglycoside acetyltransferase encoded by plasmids and integrons in C. freundii, E. coli, E. faecium and Klebsiella aerogenes. http://purl.obolibrary.org/obo/ARO_3002560 AAC(6')-Iq http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Iq is a aminoglycoside acetyltransferase encoded by plasmids and integrons in K. pneumoniae. http://purl.obolibrary.org/obo/ARO_3002561 AAC(6')-Ir http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Ir is a chromosomal-encoded aminoglycoside acetyltransferase in Acinetobacter colistiniresistens. http://purl.obolibrary.org/obo/ARO_3002562 AAC(6')-Is http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Is is a chromosomal-encoded aminoglycoside acetyltransferase in Acinetobacter variabilis. http://purl.obolibrary.org/obo/ARO_3002563 AAC(6')-Isa http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Isa is a plasmid-encoded aminoglycoside acetyltransferase in Streptomyces albulus. http://purl.obolibrary.org/obo/ARO_3002564 AAC(6')-It http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-It is a chromosomal-encoded aminoglycoside acetyltransferase in Acinetobacter genomosp. 16. http://purl.obolibrary.org/obo/ARO_3002565 AAC(6')-Iu http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Iu is a chromosomal-encoded aminoglycoside acetyltransferase in Acinetobacter genomosp. 17. http://purl.obolibrary.org/obo/ARO_3002566 AAC(6')-Iv http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Iv is a chromosomal-encoded aminoglycoside acetyltransferase in Acinetobacter sp. http://purl.obolibrary.org/obo/ARO_3002567 AAC(6')-Iw http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Iw is a chromosomal-encoded aminoglycoside acetyltransferase in Acinetobacter sp. http://purl.obolibrary.org/obo/ARO_3002568 AAC(6')-Ix http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Ix is a chromosomal-encoded aminoglycoside acetyltransferase in Acinetobacter sp. http://purl.obolibrary.org/obo/ARO_3002569 AAC(6')-Iy http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Iy is a chromosomal-encoded aminoglycoside acetyltransferase in S. enteritidis and S. enterica. Regulatory mutation required to increase expression of this chromosomally-encoded gene for resistance. In the specific system, aminoglycoside resistance was due to a transcriptional fusion secondary to a chromosomal deletion in which the downstream aac(6')-Iy gene was placed under the control of the upstream nmpC promoter. http://purl.obolibrary.org/obo/ARO_3002570 AAC(6')-Iz http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Iz is a chromosomal-encoded aminoglycoside acetyltransferase in S. maltophilia. http://purl.obolibrary.org/obo/ARO_3002571 AAC(6')-Iaa http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Iaa is a chromosomal-encoded aminoglycoside acetyltransferase in S. typhimurium. http://purl.obolibrary.org/obo/ARO_3002572 AAC(6')-Iad http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Iad is a plasmid-encoded aminoglycoside acetyltransferase in Acinetobacter genomosp. 3. http://purl.obolibrary.org/obo/ARO_3002573 AAC(6')-Iae http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Iae is an integron-encoded aminoglycoside acetyltransferase in P. aeruginosa and S. enterica. http://purl.obolibrary.org/obo/ARO_3002574 AAC(6')-Iaf http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Iaf is an aminoglycoside acetyltransferase encoded by plasmids and integrons in P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3002575 AAC(6')-Iai http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Iai is an aminoglycoside acetyltransferase encoded by plasmids and integrons in P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3002576 AAC(6')-Ib3 http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Ib3 is an integron-encoded aminoglycoside acetyltransferase in P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3002577 AAC(6')-Ib4 http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Ib4 is an aminoglycoside acetyltransferase in Serratia spp. http://purl.obolibrary.org/obo/ARO_3002578 AAC(6')-Ib7 http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Ib7 is a plasmid-encoded aminoglycoside acetyltransferase in E. cloacae and C. freundii. http://purl.obolibrary.org/obo/ARO_3002579 AAC(6')-Ib8 http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Ib8 is a plasmid-encoded aminoglycoside acetyltransferase in E. cloacae. http://purl.obolibrary.org/obo/ARO_3002580 AAC(6')-Ib9 http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Ib9 is an integron-encoded aminoglycoside acetyltransferase in P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3002581 AAC(6')-Ib10 http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Ib10 is an integron-encoded aminoglycoside acetyltransferase in P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3002582 AAC(6')-Ib11 http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Ib11 is an integron-encoded aminoglycoside acetyltransferase in S. enterica. http://purl.obolibrary.org/obo/ARO_3002583 AAC(6')-29a http://purl.obolibrary.org/obo/ARO_3000345 AAC(6') AAC(6')-29a is an integron-encoded aminoglycoside acetyltransferase in P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3002584 AAC(6')-29b http://purl.obolibrary.org/obo/ARO_3000345 AAC(6') AAC(6')-29b is an integron-encoded aminoglycoside acetyltransferase in P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3002585 AAC(6')-31 http://purl.obolibrary.org/obo/ARO_3000345 AAC(6') AAC(6')-31 is an integron-encoded aminoglycoside acetyltransferase in Pseudomonas putida, A. baumannii and K. pneumoniae. http://purl.obolibrary.org/obo/ARO_3002586 AAC(6')-32 http://purl.obolibrary.org/obo/ARO_3000345 AAC(6') AAC(6')-32 is an aminoglycoside acetyltransferase encoded by plasmids and integrons in P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3002587 AAC(6')-I33 http://purl.obolibrary.org/obo/ARO_3000345 AAC(6') AAC(6')-I33 is an integron-encoded aminoglycoside acetyltransferase in P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3002588 AAC(6')-I30 http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-I30 is an integron-encoded aminoglycoside acetyltransferase in S. enterica. http://purl.obolibrary.org/obo/ARO_3002589 AAC(6')-Iid http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Iid is a chromosomal-encoded aminoglycoside acetyltransferase in Enterococcus durans. http://purl.obolibrary.org/obo/ARO_3002590 AAC(6')-Iih http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Iih is a chromosomal-encoded aminoglycoside acetyltransferase in Enterococcus hirae. http://purl.obolibrary.org/obo/ARO_3002591 AAC(6')-Ib-Suzhou http://purl.obolibrary.org/obo/ARO_3000345 AAC(6') AAC(6')-Ib-Suzhou is an aminoglycoside acetyltransferase in E. cloacae and K. pneumoniae. http://purl.obolibrary.org/obo/ARO_3002592 AAC(6')-Ib-Hangzhou http://purl.obolibrary.org/obo/ARO_3000345 AAC(6') AAC(6')-Ib-Hangzhou is an aminoglycoside acetyltransferase in A. baumannii. http://purl.obolibrary.org/obo/ARO_3002593 AAC(6')-Ib-SK http://purl.obolibrary.org/obo/ARO_3000345 AAC(6') AAC(6')-Ib-SK is a chromosomal-encoded aminoglycoside acetyltransferase in Streptomyces kanamyceticus. http://purl.obolibrary.org/obo/ARO_3002594 AAC(6')-IIa http://purl.obolibrary.org/obo/ARO_3007396 AAC(6')-II AAC(6')-IIa is an aminoglycoside acetyltransferase encoded by plasmids and integrons in P. aeruginosa and S. enterica. http://purl.obolibrary.org/obo/ARO_3002595 AAC(6')-IIb http://purl.obolibrary.org/obo/ARO_3007396 AAC(6')-II AAC(6')-IIb is an integron-encoded aminoglycoside acetyltransferase in P. fluorescens. http://purl.obolibrary.org/obo/ARO_3002596 AAC(6')-IIc http://purl.obolibrary.org/obo/ARO_3007396 AAC(6')-II AAC(6')-IIc is an aminoglycoside acetyltransferase encoded by plasmids and integrons in E. cloacae. http://purl.obolibrary.org/obo/ARO_3002597 AAC(6')-Ie-APH(2'')-Ia bifunctional protein http://purl.obolibrary.org/obo/ARO_3007419 aminoglycoside bifunctional resistance protein AAC(6')-Ie-APH(2'')-Ia is an aminoglycoside acetyltransferase encoded by plasmids and transposons in S. aureus, E. faecalis, E. faecium and Staphylococcus warneri. http://purl.obolibrary.org/obo/ARO_3002598 ANT(3'')-II-AAC(6')-IId bifunctional protein http://purl.obolibrary.org/obo/ARO_3007419 aminoglycoside bifunctional resistance protein ANT(3'')-II-AAC(6')-IId is an integron-encoded aminoglycoside acetyltransferase in S. marcescens. http://purl.obolibrary.org/obo/ARO_3002599 AAC(6')-30/AAC(6')-Ib' bifunctional protein http://purl.obolibrary.org/obo/ARO_3007419 aminoglycoside bifunctional resistance protein AAC(6')-30/AAC(6')-Ib' is an integron-encoded aminoglycoside acetyltransferase in P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3002600 AAC(3)-Ib/AAC(6')-Ib3 bifunctional protein http://purl.obolibrary.org/obo/ARO_3007419 aminoglycoside bifunctional resistance protein AAC(3)-Ib/AAC(6')-Ib3 is an integron-encoded aminoglycoside acetyltransferase in P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3002601 aadA http://purl.obolibrary.org/obo/ARO_3000232 ANT(3'')-Ia ANT(3'')-Ia is an aminoglycoside nucleotidyltransferase gene encoded by plasmids, transposons, integrons in Enterobacteriaceae, A. baumannii, P. aeruginosa and Vibrio cholerae. http://purl.obolibrary.org/obo/ARO_3002602 aadA2 http://purl.obolibrary.org/obo/ARO_3000232 ANT(3'')-Ia aadA2 is an aminoglycoside nucleotidyltransferase gene encoded by plasmids and integrons in K. pneumoniae, Salmonella spp., Corynebacterium glutamicum, C. freundii and Aeromonas spp. http://purl.obolibrary.org/obo/ARO_3002603 aadA3 http://purl.obolibrary.org/obo/ARO_3000232 ANT(3'')-Ia aadA3 is an aminoglycoside nucleotidyltransferase gene encoded by plasmids, transposons and integrons in E. coli. http://purl.obolibrary.org/obo/ARO_3002604 aadA4 http://purl.obolibrary.org/obo/ARO_3000232 ANT(3'')-Ia aadA4 is an aminoglycoside nucleotidyltransferase gene encoded by plasmids and chromosomes in Bordetella parapertussis and E. coli. http://purl.obolibrary.org/obo/ARO_3002605 aadA5 http://purl.obolibrary.org/obo/ARO_3000232 ANT(3'')-Ia aadA5 is an aminoglycoside nucleotidyltransferase gene encoded by plasmids, transposons and integrons in E. coli, K. pneumoniae, Kluyvera georgiana, P. aeruginosa and E. cloacae. http://purl.obolibrary.org/obo/ARO_3002606 aadA6 http://purl.obolibrary.org/obo/ARO_3000232 ANT(3'')-Ia aadA6 is an integron-encoded aminoglycoside nucleotidyltransferase gene in P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3002607 aadA7 http://purl.obolibrary.org/obo/ARO_3000232 ANT(3'')-Ia aadA7 is an integron-encoded aminoglycoside nucleotidyltransferase gene in V. fluvialis, P. aeruginosa, E. coli, V. cholerae and S. enterica. http://purl.obolibrary.org/obo/ARO_3002608 aadA8 http://purl.obolibrary.org/obo/ARO_3000232 ANT(3'')-Ia aadA8 is an aminoglycoside nucleotidyltransferase gene encoded by plasmids and integrons in V. cholerae, K. pneumoniae and Bacillus endophyticus. http://purl.obolibrary.org/obo/ARO_3002609 aadA9 http://purl.obolibrary.org/obo/ARO_3000232 ANT(3'')-Ia aadA9 is a plasmid-encoded aminoglycoside nucleotidyltransferase gene in C. glutamicum. http://purl.obolibrary.org/obo/ARO_3002611 aadA11 http://purl.obolibrary.org/obo/ARO_3000232 ANT(3'')-Ia aadA11 is an integron-encoded aminoglycoside nucleotidyltransferase gene in E. coli and P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3002612 aadA12 http://purl.obolibrary.org/obo/ARO_3000232 ANT(3'')-Ia aadA12 is an integron-encoded aminoglycoside nucleotidyltransferase gene in E. coli, Yersinia enterocolitica and S. enterica. http://purl.obolibrary.org/obo/ARO_3002613 aadA13 http://purl.obolibrary.org/obo/ARO_3000232 ANT(3'')-Ia aadA13 is an aminoglycoside nucleotidyltransferase gene encoded by plasmids and integrons in Pseudomonas rettgeri, P. aeruginosa, Y. enterocolitica and E. coli. http://purl.obolibrary.org/obo/ARO_3002614 aadA14 http://purl.obolibrary.org/obo/ARO_3000232 ANT(3'')-Ia aadA14 is a plasmid-encoded aminoglycoside nucleotidyltransferase gene in Pasteurella multocida. http://purl.obolibrary.org/obo/ARO_3002615 aadA15 http://purl.obolibrary.org/obo/ARO_3000232 ANT(3'')-Ia aadA15 is an integron-encoded aminoglycoside nucleotidyltransferase gene in P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3002616 aadA16 http://purl.obolibrary.org/obo/ARO_3000232 ANT(3'')-Ia aadA16 is an aminoglycoside nucleotidyltransferase gene encoded by plasmids and integrons in E. coli, V. cholerae and K. pneumoniae. http://purl.obolibrary.org/obo/ARO_3002617 aadA17 http://purl.obolibrary.org/obo/ARO_3000232 ANT(3'')-Ia aadA17 is an integron-encoded aminoglycoside nucleotidyltransferase gene in Aeromonas media. http://purl.obolibrary.org/obo/ARO_3002618 aadA21 http://purl.obolibrary.org/obo/ARO_3000232 ANT(3'')-Ia aadA21 is an integron-encoded aminoglycoside nucleotidyltransferase gene in Salmonella spp. http://purl.obolibrary.org/obo/ARO_3002619 aadA22 http://purl.obolibrary.org/obo/ARO_3000232 ANT(3'')-Ia aadA22 is an aminoglycoside nucleotidyltransferase gene encoded by plasmids and integrons in S. enterica and E. coli. http://purl.obolibrary.org/obo/ARO_3002620 aadA23 http://purl.obolibrary.org/obo/ARO_3000232 ANT(3'')-Ia aadA23 is an integron-encoded aminoglycoside nucleotidyltransferase gene in S. enterica. http://purl.obolibrary.org/obo/ARO_3002621 aadA24 http://purl.obolibrary.org/obo/ARO_3000232 ANT(3'')-Ia aadA24 is an integron-encoded aminoglycoside nucleotidyltransferase gene in Salmonella spp. http://purl.obolibrary.org/obo/ARO_3002622 aadA6/aadA10 http://purl.obolibrary.org/obo/ARO_3000232 ANT(3'')-Ia aadA6/aadA10 is an integron-encoded aminoglycoside nucleotidyltransferase gene cassette in P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3002623 ANT(4')-Ia http://purl.obolibrary.org/obo/ARO_3007403 ANT(4')-I ANT(4')-Ia is a plasmid-encoded aminoglycoside nucleotidyltransferase in S. epidermidis, S. aureus, Enterococcus spp. and Bacillus spp. http://purl.obolibrary.org/obo/ARO_3002624 ANT(4')-IIa http://purl.obolibrary.org/obo/ARO_3007404 ANT(4')-II ANT(4')-IIa is a plasmid-encoded aminoglycoside nucleotidyltransferase in P. aeruginosa and Enterobacteriaceae. http://purl.obolibrary.org/obo/ARO_3002625 ANT(4')-IIb http://purl.obolibrary.org/obo/ARO_3007404 ANT(4')-II ANT(4')-IIb is a transposon-encoded aminoglycoside nucleotidyltransferase in P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3002626 ANT(6)-Ia http://purl.obolibrary.org/obo/ARO_3007399 ANT(6)-I ANT(6)-Ia is an aminoglycoside nucleotidyltransferase gene encoded by plasmids and chromosomes in Staphylococcus epidermidis, E. faecium, Streptococcus suis, S. aureus, E. faecalis and Streptococcus mitis. http://purl.obolibrary.org/obo/ARO_3002627 aadK http://purl.obolibrary.org/obo/ARO_3007399 ANT(6)-I aadK is a chromosomal-encoded aminoglycoside nucleotidyltransferase gene in B. subtilis and Bacillus spp. This enzyme confers low-level resistance to streptomycin. http://purl.obolibrary.org/obo/ARO_3002628 aad(6) http://purl.obolibrary.org/obo/ARO_3007399 ANT(6)-I ANT(6)-Ia/aad(6) is a plasmid-encoded aminoglycoside nucleotidyltransferase gene in E. faecalis and Streptococcus oralis. http://purl.obolibrary.org/obo/ARO_3002629 ANT(6)-Ib http://purl.obolibrary.org/obo/ARO_3007399 ANT(6)-I ANT(6)-Ib is an aminoglycoside nucleotidyltransferase gene encoded by transferable pathogenicity islands in C. fetus subsp. fetus and B. subtilis. http://purl.obolibrary.org/obo/ARO_3002630 ANT(9)-Ia http://purl.obolibrary.org/obo/ARO_3007400 ANT(9)-I ANT(9)-Ia is an aminoglycoside nucleotidyltransferase encoded by plasmids and transposons in S. aureus, Enterococcus spp., Mammaliicoccus sciuri, and E. faecalis. http://purl.obolibrary.org/obo/ARO_3002631 spd http://purl.obolibrary.org/obo/ARO_3007400 ANT(9)-I spd is a plasmid-encoded aminoglycoside nucleotidyltransferase gene in S. aureus. http://purl.obolibrary.org/obo/ARO_3002634 APH(2'')-Ie http://purl.obolibrary.org/obo/ARO_3000128 APH(2'') APH(2'')-Ie is a plasmid or transposon-encoded aminoglycoside phosphotransferase in E. faecium and E. casseliflavus. http://purl.obolibrary.org/obo/ARO_3002635 APH(2'')-IIa http://purl.obolibrary.org/obo/ARO_3000128 APH(2'') APH(2'')-IIa is a chromosomal-encoded aminoglycoside phosphotransferase in E. faecium and E. coli. http://purl.obolibrary.org/obo/ARO_3002636 APH(2'')-IIIa http://purl.obolibrary.org/obo/ARO_3000128 APH(2'') APH(2'')-IIIa is a plasmid-encoded aminoglycoside phosphotransferase in Enterococcus gallinarum. http://purl.obolibrary.org/obo/ARO_3002637 APH(2'')-IVa http://purl.obolibrary.org/obo/ARO_3000128 APH(2'') APH(2'')-IVa is a chromosomal-encoded aminoglycoside phosphotransferase in E. casseliflavus. http://purl.obolibrary.org/obo/ARO_3002638 APH(3'')-Ia http://purl.obolibrary.org/obo/ARO_3007414 APH(3'')-I APH(3'')-Ia is a chromosomal-encoded aminoglycoside phosphotransferase in S. griseus. http://purl.obolibrary.org/obo/ARO_3002639 APH(3'')-Ib http://purl.obolibrary.org/obo/ARO_3007414 APH(3'')-I APH(3'')-Ib is an aminoglycoside phosphotransferase encoded by plasmids, transposons, integrative conjugative elements and chromosomes in Enterobacteriaceae and Pseudomonas spp. http://purl.obolibrary.org/obo/ARO_3002640 APH(3'')-Ic http://purl.obolibrary.org/obo/ARO_3007414 APH(3'')-I APH(3'')-Ic is a chromosomal-encoded aminoglycoside phosphotransferase in Mycolicibacterium fortuitum. http://purl.obolibrary.org/obo/ARO_3002641 APH(3')-Ia http://purl.obolibrary.org/obo/ARO_3007406 APH(3')-I APH(3')-Ia is a transposon-encoded aminoglycoside phosphotransferase in E. coli and S. enterica. It is identical at the protein sequence to APH(3')-Ic, an aminoglycoside phosphotransferase encoded by plasmids, transposons and genomic islands in K. pneumoniae, A. baumannii, S. marcescens, Corynebacterium spp., Photobacterium spp. and Citrobacter spp. http://purl.obolibrary.org/obo/ARO_3002642 APH(3')-Ib http://purl.obolibrary.org/obo/ARO_3007406 APH(3')-I APH(3')-Ib is a plasmid-encoded aminoglycoside phosphotransferase in E. coli. http://purl.obolibrary.org/obo/ARO_3002644 APH(3')-IIa http://purl.obolibrary.org/obo/ARO_3007408 APH(3')-II APH(3')-IIa is a transposon-encoded aminoglycoside phosphotransferase in E. coli. http://purl.obolibrary.org/obo/ARO_3002645 APH(3')-IIb http://purl.obolibrary.org/obo/ARO_3007408 APH(3')-II APH(3')-IIb is a chromosomal-encoded aminoglycoside phosphotransferase in P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3002646 APH(3')-IIc http://purl.obolibrary.org/obo/ARO_3007408 APH(3')-II APH(3')-IIc is a chromosomal-encoded aminoglycoside phosphotransferase in S. maltophilia. http://purl.obolibrary.org/obo/ARO_3002647 APH(3')-IIIa http://purl.obolibrary.org/obo/ARO_3007409 APH(3')-III APH(3')-IIIa is a plasmid-encoded aminoglycoside phosphotransferase in S. aureus and Enterococcus spp. http://purl.obolibrary.org/obo/ARO_3002648 APH(3')-IVa http://purl.obolibrary.org/obo/ARO_3007410 APH(3')-IV APH(3')-IVa is a chromosomal-encoded aminoglycoside phosphotransferase in Niallia circulans. http://purl.obolibrary.org/obo/ARO_3002649 APH(3')-Va http://purl.obolibrary.org/obo/ARO_3007411 APH(3')-V APH(3')-Va is a chromosomal-encoded aminoglycoside phosphotransferase in Streptomyces fradiae. http://purl.obolibrary.org/obo/ARO_3002650 APH(3')-Vb http://purl.obolibrary.org/obo/ARO_3007411 APH(3')-V APH(3')-Vb is a chromosomal-encoded aminoglycoside phosphotransferase in Streptomyces ribosidificus. http://purl.obolibrary.org/obo/ARO_3002651 APH(3')-Vc http://purl.obolibrary.org/obo/ARO_3007411 APH(3')-V APH(3')-Vc is a chromosomal-encoded aminoglycoside phosphotransferase in M. chalcea. http://purl.obolibrary.org/obo/ARO_3002652 APH(3')-VIa http://purl.obolibrary.org/obo/ARO_3007412 APH(3')-VI APH(3')-VIa is a plasmid-encoded aminoglycoside phosphotransferase in A. baumannii. http://purl.obolibrary.org/obo/ARO_3002653 APH(3')-VIb http://purl.obolibrary.org/obo/ARO_3007412 APH(3')-VI APH(3')-VIb is a plasmid-encoded aminoglycoside phosphotransferase in K. pneumoniae and S. marcescens. http://purl.obolibrary.org/obo/ARO_3002654 APH(3')-VIIa http://purl.obolibrary.org/obo/ARO_3007413 APH(3')-VII APH(3')-VIIa is a plasmid-encoded aminoglycoside phosphotransferase in C. jejuni. http://purl.obolibrary.org/obo/ARO_3002655 APH(4)-Ia http://purl.obolibrary.org/obo/ARO_3007418 APH(4)-I APH(4)-Ia is a plasmid-encoded aminoglycoside phosphotransferase in E. coli. http://purl.obolibrary.org/obo/ARO_3002656 APH(4)-Ib http://purl.obolibrary.org/obo/ARO_3007418 APH(4)-I APH(4)-Ib is a chromosomal-encoded aminoglycoside phosphotransferase in Pseudomonas pseudomallei. http://purl.obolibrary.org/obo/ARO_3002657 APH(6)-Ia http://purl.obolibrary.org/obo/ARO_3007415 APH(6)-I APH(6)-Ia is a chromosomal-encoded aminoglycoside phosphotransferase in S. griseus. http://purl.obolibrary.org/obo/ARO_3002658 APH(6)-Ib http://purl.obolibrary.org/obo/ARO_3007415 APH(6)-I APH(6)-Ib is a chromosomal-encoded aminoglycoside phosphotransferase in S. glaucescens. http://purl.obolibrary.org/obo/ARO_3002659 APH(6)-Ic http://purl.obolibrary.org/obo/ARO_3007415 APH(6)-I APH(6)-Ic is a transposon-encoded aminoglycoside phosphotransferase in S. enterica, P. aeruginosa and E. coli. http://purl.obolibrary.org/obo/ARO_3002660 APH(6)-Id http://purl.obolibrary.org/obo/ARO_3007415 APH(6)-I APH(6)-Id is an aminoglycoside phosphotransferase encoded by plasmids, integrative conjugative elements and chromosomal genomic islands in K. pneumoniae, Salmonella spp., E. coli, Shigella flexneri, Providencia alcalifaciens, Pseudomonas spp., V. cholerae, Edwardsiella tarda, Pasteurella multocida and Aeromonas bestiarum. http://purl.obolibrary.org/obo/ARO_3002661 APH(7'')-Ia http://purl.obolibrary.org/obo/ARO_3007417 APH(7'')-I APH(7'')-Ia is a chromosomal-encoded aminoglycoside phosphotransferase in S. hygroscopicus. http://purl.obolibrary.org/obo/ARO_3002662 APH(9)-Ia http://purl.obolibrary.org/obo/ARO_3007416 APH(9)-I APH(9)-Ia is a chromosomal-encoded aminoglycoside phosphotransferase in L. pneumophila. http://purl.obolibrary.org/obo/ARO_3002663 APH(9)-Ib http://purl.obolibrary.org/obo/ARO_3007416 APH(9)-I APH(9)-Ib is a chromosomal-encoded aminoglycoside phosphotransferase in S. flavopersicus. http://purl.obolibrary.org/obo/ARO_3002665 npmA http://purl.obolibrary.org/obo/ARO_3004272 16S rRNA methyltransferase (A1408) NpmA is a plasmid-mediated aminoglycoside-resistance 16S rRNA methyltransferase by interfering with aminoglycoside binding with the A site of 16S rRNA through N-1 methylation at position A1408. http://purl.obolibrary.org/obo/ARO_3002666 rmtF http://purl.obolibrary.org/obo/ARO_3004271 16S rRNA methyltransferase (G1405) RmtF is a 16S rRNA methyltransferase found in Pseudomonas aeruginosa which methylates G1405 of the 16S rRNA. It confers high level resistance to many aminoglycosides. http://purl.obolibrary.org/obo/ARO_3002667 rmtD http://purl.obolibrary.org/obo/ARO_3004271 16S rRNA methyltransferase (G1405) RmtD is a 16S rRNA methyltransferase found in Pseudomonas aeruginosa which methylates G1405 of the 16S rRNA. It confers high level resistance to many aminoglycosides. http://purl.obolibrary.org/obo/ARO_3002668 rmtG http://purl.obolibrary.org/obo/ARO_3004271 16S rRNA methyltransferase (G1405) RmtG is a 16S rRNA methyltransferase found in Pseudomonas aeruginosa which methylates G1405 of the 16S rRNA. It confers high level resistance to many aminoglycosides. http://purl.obolibrary.org/obo/ARO_3002669 APH(2'')-Ig http://purl.obolibrary.org/obo/ARO_3000128 APH(2'') APH('')-Ig is a plasmid-encoded aminoglycoside phosphotransferase in Campylobacter coli. http://purl.obolibrary.org/obo/ARO_3002670 cat http://purl.obolibrary.org/obo/ARO_3000122 chloramphenicol acetyltransferase (CAT) cat is used to describe many variants of the chloramphenicol acetyltransferase gene in a range of organisms including Acinetobacter calcoaceticus, Agrobacterium tumefaciens, Alkalihalobacillus clausii, Bacillus subtilis, Campylobacter coli, Enterococcus faecalis, Enterococcus faecium, Lactococcus lactis, Listeria monocytogenes, Listonella anguillarum Morganella morganii, Photobacterium damselae subsp. piscicida, Proteus mirabilis, Salmonella typhi, Serratia marcescens, Shigella flexneri, Staphylococcus aureus, Staphylococcus haemolyticus, Staphylococcus intermedius, Streptococcus agalactiae, Streptococcus suis and Streptomyces acrimycini. http://purl.obolibrary.org/obo/ARO_3002671 Limosilactobacillus reuteri cat-TC http://purl.obolibrary.org/obo/ARO_3000122 chloramphenicol acetyltransferase (CAT) cat-TC is a plasmid-encoded variant of the cat gene found in Limosilactobacillus reuteri. http://purl.obolibrary.org/obo/ARO_3002672 Bacillus pumilus cat86 http://purl.obolibrary.org/obo/ARO_3000122 chloramphenicol acetyltransferase (CAT) cat86 is a chromosome-encoded variant of the cat gene found in Bacillus pumilus. http://purl.obolibrary.org/obo/ARO_3002674 Clostridium butyricum catB http://purl.obolibrary.org/obo/ARO_3000122 chloramphenicol acetyltransferase (CAT) catB is a chromosome-encoded variant of the cat gene found in Clostridium butyricum. http://purl.obolibrary.org/obo/ARO_3002675 catB2 http://purl.obolibrary.org/obo/ARO_3000122 chloramphenicol acetyltransferase (CAT) catB2 is a plasmid-encoded variant of the cat gene found in Escherichia coli, Salmonella enteritidis and Pasteurella multocida. http://purl.obolibrary.org/obo/ARO_3002676 catB3 http://purl.obolibrary.org/obo/ARO_3000122 chloramphenicol acetyltransferase (CAT) catB3 is a plasmid or chromosome-encoded variant of the cat gene found in Salmonella typhimurium, Acinetobacter baumannii and Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002678 Pseudomonas aeruginosa catB6 http://purl.obolibrary.org/obo/ARO_3000122 chloramphenicol acetyltransferase (CAT) catB6 is a plasmid-encoded variant of the cat gene found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002679 Pseudomonas aeruginosa catB7 http://purl.obolibrary.org/obo/ARO_3000122 chloramphenicol acetyltransferase (CAT) catB7 is a chromosome-encoded variant of the cat gene found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002680 catB8 http://purl.obolibrary.org/obo/ARO_3000122 chloramphenicol acetyltransferase (CAT) catB8 is a plasmid or integron-encoded variant of the cat gene found in Klebsiella pneumoniae, Salmonella typhi and Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002681 catB9 http://purl.obolibrary.org/obo/ARO_3000122 chloramphenicol acetyltransferase (CAT) catB9 is a chromosome-encoded variant of the cat gene found in Vibrio cholerae. http://purl.obolibrary.org/obo/ARO_3002682 catD http://purl.obolibrary.org/obo/ARO_3000122 chloramphenicol acetyltransferase (CAT) catD is a chromosome and transposon-encoded variant of the cat gene found in Clostridioides difficile. http://purl.obolibrary.org/obo/ARO_3002683 catA1 http://purl.obolibrary.org/obo/ARO_3000122 chloramphenicol acetyltransferase (CAT) catA1 (formerly in CARD as catI) is a chromosome and transposon-encoded variant of the cat gene found in Escherichia coli and Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3002684 catII http://purl.obolibrary.org/obo/ARO_3000122 chloramphenicol acetyltransferase (CAT) catII is a plasmid-encoded variant of the cat gene found in Haemophilus influenzae, Agrobacterium tumefaciens and Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002685 catIII http://purl.obolibrary.org/obo/ARO_3000122 chloramphenicol acetyltransferase (CAT) catIII is a plasmid-encoded variant of the cat gene found in Shigella flexneri. http://purl.obolibrary.org/obo/ARO_3002686 catP http://purl.obolibrary.org/obo/ARO_3000122 chloramphenicol acetyltransferase (CAT) catP is a transposon and chromosome-encoded variant of the cat gene found in Clostridium perfringens and Neisseria meningitidis. http://purl.obolibrary.org/obo/ARO_3002687 catQ http://purl.obolibrary.org/obo/ARO_3000122 chloramphenicol acetyltransferase (CAT) catQ is a chromosome-encoded variant of the cat gene found in Clostridium perfringens. http://purl.obolibrary.org/obo/ARO_3002688 catS http://purl.obolibrary.org/obo/ARO_3000122 chloramphenicol acetyltransferase (CAT) catS is a chromosome-encoded variant of the cat gene found in Streptococcus pyogenes. http://purl.obolibrary.org/obo/ARO_3002689 Plasmid-encoded cat (pp-cat) http://purl.obolibrary.org/obo/ARO_3000122 chloramphenicol acetyltransferase (CAT) Plasmid-encoded cat, or pp-cat, is a plasmid-encoded variant of the cat gene found in Photobacterium damselae subsp. piscicida. http://purl.obolibrary.org/obo/ARO_3002690 Streptomyces lividans cmlR http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump cmlR is a plasmid or chromosome-encoded chloramphenicol resistance determinant (putative transmembrane protein) that is found in Escherichia coli and Streptomyces lividans. http://purl.obolibrary.org/obo/ARO_3002691 Salmonella enterica cmlA http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump cmlA is a plasmid-encoded chloramphenicol exporter that is found in Salmonella typhimurium. http://purl.obolibrary.org/obo/ARO_3002693 cmlA1 http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump cmlA1 is a plasmid or transposon-encoded chloramphenicol exporter that is found in Pseudomonas aeruginosa and Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002694 cmlA4 http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump cmlA4 is a plasmid-encoded chloramphenicol exporter that is found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002695 cmlA5 http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump cmlA5 is a plasmid or transposon-encoded chloramphenicol exporter that is found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002696 cmlA6 http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump cmlA6 is a plasmid-encoded chloramphenicol exporter that is found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002698 cmlB http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump cmlB is a plasmid-encoded chloramphenicol exporter that is found in Klebsiella aerogenes. http://purl.obolibrary.org/obo/ARO_3002699 cmlB1 http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump cmlB1 is a plasmid-encoded chloramphenicol exporter that is found in Bordetella bronchiseptica. http://purl.obolibrary.org/obo/ARO_3002700 cmlv http://purl.obolibrary.org/obo/ARO_3000249 chloramphenicol phosphotransferase cmlv is a chromosome-encoded chloramphenicol phoshotransferase that is found in Streptomyces venezuelae. http://purl.obolibrary.org/obo/ARO_3002701 Rhodococcus fascians cmr http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump cmr is a plasmid-encoded chloramphenicol exporter that is found in Rhodococcus fascians and Corynebacterium glutamicum. http://purl.obolibrary.org/obo/ARO_3002702 cmrA http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump cmrA is a transposon-encoded chloramphenicol exporter that is found in Rhodococcus rhodochrous. http://purl.obolibrary.org/obo/ARO_3002703 cmx http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump cmx is a plasmid or transposon-encoded chloramphenicol exporter that is found in Corynebacterium striatum and Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002704 fexA http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump fexA is a plasmid-encoded chloramphenicol exporter that is found in Mammaliicoccus lentus. http://purl.obolibrary.org/obo/ARO_3002705 floR http://purl.obolibrary.org/obo/ARO_3003963 flo floR is a plasmid or chromosome-encoded chloramphenicol exporter that is found in Bordetella bronchiseptica, Escherichia coli, Klebsiella pneumoniae, Salmonella enterica subsp. enterica serovar Typhimurium str. DT104 and Vibrio cholerae. http://purl.obolibrary.org/obo/ARO_3002706 ethambutol resistant embC http://purl.obolibrary.org/obo/ARO_3005005 antibiotic-resistant emb arabinosyltransferase Mycobacterium tuberculosis embC mutations at codon 270 confer resistance to ethambutol. http://purl.obolibrary.org/obo/ARO_3002707 QnrA1 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrA1 is a plasmid-mediated quinolone resistance protein found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002708 QnrA2 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrA2 is a plasmid-mediated quinolone resistance protein found in Klebsiella oxytoca. http://purl.obolibrary.org/obo/ARO_3002709 QnrA3 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrA3 is a plasmid-mediated quinolone resistance protein found in Shewanella algae. http://purl.obolibrary.org/obo/ARO_3002710 QnrA4 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrA4 is a plasmid-mediated quinolone resistance protein found in Shewanella algae. http://purl.obolibrary.org/obo/ARO_3002711 QnrA5 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrA5 is a plasmid-mediated quinolone resistance protein found in Shewanella algae. http://purl.obolibrary.org/obo/ARO_3002712 QnrA6 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrA6 is a plasmid-mediated quinolone resistance protein found in Proteus mirabilis. http://purl.obolibrary.org/obo/ARO_3002713 QnrA7 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrA7 is a plasmid-mediated quinolone resistance protein found in Shewanella algae. http://purl.obolibrary.org/obo/ARO_3002714 QnrB1 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB1 is a plasmid-mediated quinolone resistance protein found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002715 QnrB2 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB2 is a plasmid-mediated quinolone resistance protein found in Citrobacter koseri. http://purl.obolibrary.org/obo/ARO_3002716 QnrB3 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB3 is a plasmid-mediated quinolone resistance protein found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002718 QnrB4 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB4 is a plasmid-mediated quinolone resistance protein found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002719 QnrB5 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB5 is a plasmid-mediated quinolone resistance protein found in Salmonella enterica. http://purl.obolibrary.org/obo/ARO_3002720 QnrB6 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB6 is a plasmid-mediated quinolone resistance protein found in Pantoea agglomerans. http://purl.obolibrary.org/obo/ARO_3002721 QnrB7 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB7 is a plasmid-mediated quinolone resistance protein found in Enterobacter cloacae. http://purl.obolibrary.org/obo/ARO_3002722 QnrB8 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB8 is a plasmid-mediated quinolone resistance protein found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3002723 QnrB9 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB9 is a plasmid-mediated quinolone resistance protein found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3002724 QnrB10 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB10 is a plasmid-mediated quinolone resistance protein found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3002725 QnrB11 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB11 is a plasmid-mediated quinolone resistance protein found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3002726 QnrB12 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB12 is a plasmid-mediated quinolone resistance protein found in Citrobacter werkmanii. http://purl.obolibrary.org/obo/ARO_3002727 QnrB13 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB13 is a plasmid-mediated quinolone resistance protein found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3002728 QnrB14 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB14 is a plasmid-mediated quinolone resistance protein found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3002730 QnrB15 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB15 is a plasmid-mediated quinolone resistance protein found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3002731 QnrB16 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB16 is a plasmid-mediated quinolone resistance protein found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3002732 QnrB17 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB17 is a plasmid-mediated quinolone resistance protein found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3002733 QnrB18 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB18 is a plasmid-mediated quinolone resistance protein found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3002734 QnrB19 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB19 is a plasmid-mediated quinolone resistance protein found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002735 QnrB20 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB20 is a plasmid-mediated quinolone resistance protein found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002736 QnrB21 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB21 is a plasmid-mediated quinolone resistance protein found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002737 QnrB22 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB22 is a plasmid-mediated quinolone resistance protein found in Citrobacter werkmanii. http://purl.obolibrary.org/obo/ARO_3002738 QnrB23 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB23 is a plasmid-mediated quinolone resistance protein found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3002739 QnrB24 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB24 is a plasmid-mediated quinolone resistance protein found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3002740 QnrB25 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB25 is a plasmid-mediated quinolone resistance protein found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3002741 QnrB26 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB26 is a plasmid-mediated quinolone resistance protein found in Proteus vulgaris. http://purl.obolibrary.org/obo/ARO_3002742 QnrB27 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB27 is a plasmid-mediated quinolone resistance protein found in Citrobacter braakii. http://purl.obolibrary.org/obo/ARO_3002743 QnrB28 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB28 is a plasmid-mediated quinolone resistance protein found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3002744 QnrB29 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB29 is a plasmid-mediated quinolone resistance protein found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3002745 QnrB30 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB30 is a plasmid-mediated quinolone resistance protein found in Citrobacter braakii. http://purl.obolibrary.org/obo/ARO_3002746 QnrB31 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB31 is a plasmid-mediated quinolone resistance protein found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002747 QnrB32 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB32 is a plasmid-mediated quinolone resistance protein found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3002748 QnrB33 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB33 is a plasmid-mediated quinolone resistance protein found in Citrobacter braakii. http://purl.obolibrary.org/obo/ARO_3002749 QnrB34 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB34 is a plasmid-mediated quinolone resistance protein found in Citrobacter werkmanii. http://purl.obolibrary.org/obo/ARO_3002750 QnrB35 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB35 is a plasmid-mediated quinolone resistance protein found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3002751 QnrB36 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB36 is a plasmid-mediated quinolone resistance protein found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3002752 QnrB37 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB37 is a plasmid-mediated quinolone resistance protein found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3002753 QnrB38 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB38 is a plasmid-mediated quinolone resistance protein found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3002754 QnrB39 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB39 is a chromosome-mediated quinolone resistance protein found in Citrobacter youngae. http://purl.obolibrary.org/obo/ARO_3002755 QnrB40 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB40 is a plasmid-mediated quinolone resistance protein found in Citrobacter braakii. http://purl.obolibrary.org/obo/ARO_3002756 QnrB41 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB41 is a plasmid-mediated quinolone resistance protein found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3002757 QnrB42 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB42 is a plasmid-mediated quinolone resistance protein found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002758 QnrB43 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB43 is a plasmid-mediated quinolone resistance protein found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002759 QnrB44 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB44 is a plasmid-mediated quinolone resistance protein found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002760 QnrB45 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB45 is a plasmid-mediated quinolone resistance protein found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002761 QnrB46 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB46 is a plasmid-mediated quinolone resistance protein found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002762 QnrB47 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB47 is a plasmid-mediated quinolone resistance protein found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002763 QnrB48 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB48 is a plasmid-mediated quinolone resistance protein found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3002764 QnrB49 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB49 is a plasmid-mediated quinolone resistance protein found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3002765 QnrB50 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB50 is a plasmid-mediated quinolone resistance protein found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3002767 QnrB54 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB54 is a plasmid-mediated quinolone resistance protein found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3002768 QnrB55 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB55 is a plasmid-mediated quinolone resistance protein found in Raoultella terrigena. http://purl.obolibrary.org/obo/ARO_3002769 QnrB56 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB56 is a plasmid-mediated quinolone resistance protein found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3002770 QnrB57 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB57 is a plasmid-mediated quinolone resistance protein found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3002771 QnrB58 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB58 is a plasmid-mediated quinolone resistance protein found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3002772 QnrB59 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB59 is a plasmid-mediated quinolone resistance protein found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3002773 QnrB60 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB60 is a plasmid-mediated quinolone resistance protein found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3002774 QnrB61 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB61 is a plasmid-mediated quinolone resistance protein found in Citrobacter braakii. http://purl.obolibrary.org/obo/ARO_3002775 QnrB62 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB62 is a plasmid-mediated quinolone resistance protein found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3002776 QnrB64 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB64 is a plasmid-mediated quinolone resistance protein found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3002777 QnrB65 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB65 is a plasmid-mediated quinolone resistance protein found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3002778 QnrB66 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB66 is a plasmid-mediated quinolone resistance protein found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3002779 QnrB67 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB67 is a plasmid-mediated quinolone resistance protein found in Citrobacter braakii. http://purl.obolibrary.org/obo/ARO_3002780 QnrB68 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB68 is a plasmid-mediated quinolone resistance protein found in Citrobacter braakii. http://purl.obolibrary.org/obo/ARO_3002781 QnrB69 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB69 is a plasmid-mediated quinolone resistance protein found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3002782 QnrB70 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB70 is a plasmid-mediated quinolone resistance protein found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3002783 QnrB71 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB71 is a plasmid-mediated quinolone resistance protein found in Citrobacter braakii. http://purl.obolibrary.org/obo/ARO_3002784 QnrB72 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB72 is a plasmid-mediated quinolone resistance protein found in Citrobacter sp. TR21_24. http://purl.obolibrary.org/obo/ARO_3002785 QnrB73 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB73 is a plasmid-mediated quinolone resistance protein found in Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3002786 QnrB74 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB74 is a plasmid-mediated quinolone resistance protein found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002787 QnrC http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrC is a plasmid-mediated quinolone resistance protein found in Proteus mirabilis. http://purl.obolibrary.org/obo/ARO_3002788 QnrD1 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrD1 is a plasmid-mediated quinolone resistance protein found in Salmonella enterica. http://purl.obolibrary.org/obo/ARO_3002789 QnrD2 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrD2 is a plasmid-mediated quinolone resistance protein found in Salmonella enterica. http://purl.obolibrary.org/obo/ARO_3002790 QnrS1 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrS1 is a plasmid-mediated quinolone resistance protein found in Shigella flexneri. http://purl.obolibrary.org/obo/ARO_3002791 QnrS2 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrS2 is a plasmid-mediated quinolone resistance protein found in Salmonella enterica. http://purl.obolibrary.org/obo/ARO_3002792 QnrS3 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrS3 is a plasmid-mediated quinolone resistance protein found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002793 QnrS4 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrS4 is a plasmid-mediated quinolone resistance protein found in Salmonella enterica. http://purl.obolibrary.org/obo/ARO_3002794 QnrS5 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrS5 is a plasmid-mediated quinolone resistance protein found in Aeromonas sobria. http://purl.obolibrary.org/obo/ARO_3002795 QnrS6 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrS6 is a plasmid-mediated quinolone resistance protein found in Aeromonas hydrophila. http://purl.obolibrary.org/obo/ARO_3002796 QnrS7 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrS7 is a plasmid-mediated quinolone resistance protein found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002797 QnrS8 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrS8 is a plasmid-mediated quinolone resistance protein found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002798 QnrS9 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrS9 is a plasmid-mediated quinolone resistance protein found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3002799 QnrVC1 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrVC1 is an integron-mediated quinolone resistance protein found in Vibrio cholerae. http://purl.obolibrary.org/obo/ARO_3002800 QnrVC3 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrVC3 is an integron-mediated quinolone resistance protein found in Vibrio cholerae. http://purl.obolibrary.org/obo/ARO_3002801 QnrVC4 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrVC4 is an integron-mediated quinolone resistance protein found in Aeromonas punctata. http://purl.obolibrary.org/obo/ARO_3002802 QnrVC5 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrVC5 is an integron-mediated quinolone resistance protein found in Vibrio fluvialis. http://purl.obolibrary.org/obo/ARO_3002803 QnrVC6 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrVC6 is an integron-mediated quinolone resistance protein found in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3002804 FosA2 http://purl.obolibrary.org/obo/ARO_3000133 fosfomycin thiol transferase An enzyme that confers resistance to fosfomycin in Enterobacter cloacae by breaking the epoxide ring of the molecule. It depends on the cofactors Manganese (II) and Potassium and uses Glutathione (GSH) as the nucleophilic molecule. http://purl.obolibrary.org/obo/ARO_3002811 antibiotic-resistant murA transferase http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant murA or UDP-N-acetylglucosamine enolpyruvyl transferase catalyses the initial step in peptidoglycan biosynthesis and is inhibited by fosfomycin. Overexpression of murA through mutations confers fosfomycin resistance. http://purl.obolibrary.org/obo/ARO_3002812 pp-flo http://purl.obolibrary.org/obo/ARO_3003963 flo pp-flo is a plasmid chloramphenicol exporter that is found in Photobacterium damselae subsp. piscicida. http://purl.obolibrary.org/obo/ARO_3002813 lmrB http://purl.obolibrary.org/obo/ARO_0010001 ATP-binding cassette (ABC) antibiotic efflux pump lmrB is a chromosomally-encoded efflux pump that confers resistance to lincosamides in Bacillus subtilis. http://purl.obolibrary.org/obo/ARO_3002814 clbA http://purl.obolibrary.org/obo/ARO_3004607 Cfr Group clbA is a plasmid-encoded cfr gene found in Bacillus velezensis (Bacillus amyloliquefaciens subsp. plantarum). http://purl.obolibrary.org/obo/ARO_3002815 clbB http://purl.obolibrary.org/obo/ARO_3004609 cfr(B) Group clbB is a plasmid-encoded cfr gene found in Bacillus brevis. http://purl.obolibrary.org/obo/ARO_3002816 clbC http://purl.obolibrary.org/obo/ARO_3004607 Cfr Group clbC is a plasmid-encoded cfr gene found in Alkalihalobacillus clausii. http://purl.obolibrary.org/obo/ARO_3002817 carA http://purl.obolibrary.org/obo/ARO_3007068 Miscellaneous ABC-F subfamily ATP-binding cassette ribosomal protection proteins carA is an ABC-F subfamily protein involved in macrolide resistance. It is found in Streptomyces thermotolerans. http://purl.obolibrary.org/obo/ARO_3002818 msrB http://purl.obolibrary.org/obo/ARO_3004471 msr-type ABC-F protein MsrB is an ABC-F subfamily protein expressed to Staphylococcus species that confers resistance to erythromycin and streptogramin B antibiotics. It is associated with plasmid DNA. http://purl.obolibrary.org/obo/ARO_3002819 msrC http://purl.obolibrary.org/obo/ARO_3004471 msr-type ABC-F protein msrC is a chromosomal-encoded ABC-F subfamily protein expressed in Enterococcus faecium that confers resistance to erythromycin and other macrolide and streptogramin B antibiotics. http://purl.obolibrary.org/obo/ARO_3002823 ErmH http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase ErmH is a plasmid-mediated methyltransferase found in Streptomyces thermotolerans. http://purl.obolibrary.org/obo/ARO_3002824 ErmV http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase ErmV is a plasmid-mediated methyltransferase found in Streptomyces viridochromogenes. http://purl.obolibrary.org/obo/ARO_3002825 ErmY http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase ErmY is a plasmid-mediated methyltransferase found in Staphylococcus aureus. http://purl.obolibrary.org/obo/ARO_3002826 EreA2 http://purl.obolibrary.org/obo/ARO_3000320 macrolide esterase EreA2 is an integron-encoded erythromycin esterase that hydrolyses the drug's lactone ring. EreA2 is found in Providencia stuartii. http://purl.obolibrary.org/obo/ARO_3002827 tlrC http://purl.obolibrary.org/obo/ARO_3007068 Miscellaneous ABC-F subfamily ATP-binding cassette ribosomal protection proteins tlrC is an ABC-F subfamily protein found in Streptomyces fradiae and confers resistance to mycinamicin, tylosin and lincosamides. tlrC is found in the tylosin biosynthetic cluster and is one mechanism by which S. fradiae protects itself from self-destruction when producing this macrolide. http://purl.obolibrary.org/obo/ARO_3002828 srmB http://purl.obolibrary.org/obo/ARO_3007068 Miscellaneous ABC-F subfamily ATP-binding cassette ribosomal protection proteins srmB is an ABC-F subfamily protein found in Streptomyces ambofaciens that confers resistance to spiramycin. http://purl.obolibrary.org/obo/ARO_3002829 vgaA http://purl.obolibrary.org/obo/ARO_3000113 vga-type ABC-F protein vgaA is an ABC-F subfamily protein expressed in staphylococci that confers resistance to streptogramin A antibiotics and related compounds. It is associated with plasmid DNA. http://purl.obolibrary.org/obo/ARO_3002830 vgaALC http://purl.obolibrary.org/obo/ARO_3000113 vga-type ABC-F protein vgaALC is an ABC-F subfamily protein expressed in staphylococci that confers resistance to streptogramin A antibiotics and related compounds. It is associated with plasmid DNA. http://purl.obolibrary.org/obo/ARO_3002831 vgaC http://purl.obolibrary.org/obo/ARO_3000113 vga-type ABC-F protein vgaC is an ABC-F subfamily protein expressed in staphylococci that confers resistance to streptogramin A antibiotics and related compounds. It is associated with plasmid DNA. http://purl.obolibrary.org/obo/ARO_3002832 vgaD http://purl.obolibrary.org/obo/ARO_3000113 vga-type ABC-F protein vgaD is an ABC-F subfamily protein expressed in Enterococcus faecium that confers resistance to streptogramin A antibiotics and related compounds. It is associated with plasmid DNA. http://purl.obolibrary.org/obo/ARO_3002833 vgaE http://purl.obolibrary.org/obo/ARO_3000113 vga-type ABC-F protein vgaE is an ABC-F subfamily protein expressed in staphylococci that confers resistance to streptogramin A antibiotics and related compounds. It is associated with transposon DNA. http://purl.obolibrary.org/obo/ARO_3002835 lnuA http://purl.obolibrary.org/obo/ARO_3000221 lincosamide nucleotidyltransferase (LNU) lnuA is a plasmid-mediated nucleotidyltransferase found in Staphylococcus chromogenes. http://purl.obolibrary.org/obo/ARO_3002836 lnuB http://purl.obolibrary.org/obo/ARO_3000221 lincosamide nucleotidyltransferase (LNU) lnuB is a plasmid-mediated nucleotidyltransferase found in Streptococcus lutetiensis. http://purl.obolibrary.org/obo/ARO_3002837 lnuC http://purl.obolibrary.org/obo/ARO_3000221 lincosamide nucleotidyltransferase (LNU) lnuC is a transposon-mediated nucleotidyltransferase found in Streptococcus agalactiae. http://purl.obolibrary.org/obo/ARO_3002838 lnuD http://purl.obolibrary.org/obo/ARO_3000221 lincosamide nucleotidyltransferase (LNU) lnuD is a plasmid-mediated nucleotidyltransferase found in Streptococcus uberis. http://purl.obolibrary.org/obo/ARO_3002839 lnuF http://purl.obolibrary.org/obo/ARO_3000221 lincosamide nucleotidyltransferase (LNU) lnuF is an integron-mediated nucleotidyltransferase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002840 vatA http://purl.obolibrary.org/obo/ARO_3000453 streptogramin vat acetyltransferase vatA is a plasmid-mediated acetyltransferase found in Staphylococcus aureus. http://purl.obolibrary.org/obo/ARO_3002841 vatB http://purl.obolibrary.org/obo/ARO_3000453 streptogramin vat acetyltransferase vatB is a plasmid-mediated acetyltransferase found in Staphylococcus aureus. http://purl.obolibrary.org/obo/ARO_3002842 vatC http://purl.obolibrary.org/obo/ARO_3000453 streptogramin vat acetyltransferase vatC is a plasmid-mediated acetyltransferase found in Staphylococcus cohnii. http://purl.obolibrary.org/obo/ARO_3002843 vatD http://purl.obolibrary.org/obo/ARO_3000453 streptogramin vat acetyltransferase vatD is a transposon-mediated acetyltransferase found in Enterococcus faecium. http://purl.obolibrary.org/obo/ARO_3002844 vatE http://purl.obolibrary.org/obo/ARO_3000453 streptogramin vat acetyltransferase vatE is a transposon-mediated acetyltransferase found in Enterococcus faecium. http://purl.obolibrary.org/obo/ARO_3002845 vatH http://purl.obolibrary.org/obo/ARO_3000453 streptogramin vat acetyltransferase vatH is a plasmid-mediated acetyltransferase found in Enterococcus faecium. http://purl.obolibrary.org/obo/ARO_3002846 arr-1 http://purl.obolibrary.org/obo/ARO_3000390 rifampin ADP-ribosyltransferase (Arr) arr-1 is a chromosome-encoded ribosyltransferase found in Mycolicibacterium smegmatis. http://purl.obolibrary.org/obo/ARO_3002847 arr-2 http://purl.obolibrary.org/obo/ARO_3000390 rifampin ADP-ribosyltransferase (Arr) arr-2 is an integron-encoded ribosyltransferase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002848 arr-3 http://purl.obolibrary.org/obo/ARO_3000390 rifampin ADP-ribosyltransferase (Arr) arr-3 is a plasmid-encoded ribosyltransferase found in Vibrio fluvialis. http://purl.obolibrary.org/obo/ARO_3002849 arr-4 http://purl.obolibrary.org/obo/ARO_3000390 rifampin ADP-ribosyltransferase (Arr) arr-4 is an integron-encoded ribosyltransferase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002850 arr-5 http://purl.obolibrary.org/obo/ARO_3000390 rifampin ADP-ribosyltransferase (Arr) arr-5 is an integron-encoded ribosyltransferase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002852 arr-7 http://purl.obolibrary.org/obo/ARO_3000390 rifampin ADP-ribosyltransferase (Arr) arr-7 is an integron-encoded ribosyltransferase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002853 arr-8 http://purl.obolibrary.org/obo/ARO_3000390 rifampin ADP-ribosyltransferase (Arr) arr-8 is an integron-encoded ribosyltransferase found in Klebsiella oxytoca. http://purl.obolibrary.org/obo/ARO_3002854 dfrA1 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr dfrA1 is an integron-encoded dihydrofolate reductase. http://purl.obolibrary.org/obo/ARO_3002856 dfrA24 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr dfrA24 is an integron-encoded dihydrofolate reductase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002857 dfrA26 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr dfrA26 is an integron-encoded dihydrofolate reductase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002858 dfrA12 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr dfrA12 is an integron-encoded dihydrofolate reductase found in Vibrio cholerae. http://purl.obolibrary.org/obo/ARO_3002859 dfrA14 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr dfrA14 is an integron-encoded dihydrofolate reductase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002860 dfrA17 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr dfrA17 is an integron-encoded dihydrofolate reductase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002861 dfrA5 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr dfrA5 is an integron-encoded dihydrofolate reductase found in Vibrio cholerae. http://purl.obolibrary.org/obo/ARO_3002862 dfrA7 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr dfrA7 is an integron-encoded dihydrofolate reductase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002863 dfrA8 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr dfrA8 is a transposon-encoded dihydrofolate reductase found in Salmonella enterica. http://purl.obolibrary.org/obo/ARO_3002864 dfrB1 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr A plasmid-associated trimethoprim-resistant dihydrofolate reductase detected in Bordetella bronchispetica on pKBB958. http://purl.obolibrary.org/obo/ARO_3002865 dfrC http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr dfrC is a chromosome-encoded dihydrofolate reductase found in Staphylococcus aureus. http://purl.obolibrary.org/obo/ARO_3002866 dfrD http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr dfrD is a plasmid-encoded dihydrofolate reductase found in Listeria monocytogenes. http://purl.obolibrary.org/obo/ARO_3002867 dfrF http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr dfrF is a chromosome-encoded dihydrofolate reductase found in Streptococcus pyogenes. http://purl.obolibrary.org/obo/ARO_3002868 dfrG http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr dfrG is a plasmid-encoded dihydrofolate reductase found in Staphylococcus aureus. http://purl.obolibrary.org/obo/ARO_3002869 dfrK http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr dfrK is a plasmid-encoded dihydrofolate reductase found in Staphylococcus aureus. http://purl.obolibrary.org/obo/ARO_3002870 tet(34) http://purl.obolibrary.org/obo/ARO_3000036 tetracycline inactivation enzyme tet(34) causes the activation of Mg2+-dependent purine nucleotide synthesis, which protects the protein synthesis pathway. It is found in Gram-negative Vibrio. http://purl.obolibrary.org/obo/ARO_3002871 tet(37) http://purl.obolibrary.org/obo/ARO_3000036 tetracycline inactivation enzyme tet(37) is a chromosome-encoded oxidoreductase isolated from an uncultured bacterium that confers resistance to tetracycline. http://purl.obolibrary.org/obo/ARO_3002872 FosA3 http://purl.obolibrary.org/obo/ARO_3000133 fosfomycin thiol transferase An enzyme that confers resistance to fosfomycin in Escherichia coli by breaking the epoxide ring of the molecule. It depends on the cofactors Manganese (II) and Potassium and uses Glutathione (GSH) as the nucleophilic molecule. http://purl.obolibrary.org/obo/ARO_3002873 FosB3 http://purl.obolibrary.org/obo/ARO_3000133 fosfomycin thiol transferase A thiol transferase that leads to the resistance of fosfomycin in Enterococcus faecium. Contrasting FosA, FosB is dependent on the cofactor Magnesium (II) and uses either bacillithiol to open up the epoxide ring of fosfomycin. http://purl.obolibrary.org/obo/ARO_3002874 FosC2 http://purl.obolibrary.org/obo/ARO_3004245 fosC phosphotransferase family FosC2 is an enzyme that phosphorylates fosfomycin to confer resistance in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3002875 dfrE http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr dfrE is a chromosome-encoded dihydrofolate reductase found in Enterococcus faecalis. http://purl.obolibrary.org/obo/ARO_3002876 ethambutol resistant aftA http://purl.obolibrary.org/obo/ARO_3003422 antibiotic resistant aftA Arabinofuranosyltransferases allow for the polymerization of arabinose to form arabinan. Arabinan is required for formation of mycobacterial cell walls and arabinosyltransferases are targets of the drug ethambutol. Mutations in these genes can confer resistance to ethambutol. http://purl.obolibrary.org/obo/ARO_3002877 BcI http://purl.obolibrary.org/obo/ARO_3007100 class A Bacillus cereus Bc beta-lactamase Bacillus cereus beta-lactamase I is a class A beta-lactamase that breaks down a number of penicillins and cephalosporins in the Bacillus cereus strain 569/H/9. http://purl.obolibrary.org/obo/ARO_3002878 BcII http://purl.obolibrary.org/obo/ARO_3000577 subclass B1 Bacillus cereus Bc beta-lactamase Bacillus cereus beta-lactamase II is a zinc metallo-beta-lactamase that hydrolyzes a large number of penicillins and cephalosporins in the Bacillus cereus strain 5/B/6. http://purl.obolibrary.org/obo/ARO_3002879 linG http://purl.obolibrary.org/obo/ARO_3000221 lincosamide nucleotidyltransferase (LNU) linG is an integron-associated gene cassette, with aadA2, encoding a lincosomide nucleotidyltransferase found in Salmonella enterica. linG confers resistance to lincosomide antibiotics. http://purl.obolibrary.org/obo/ARO_3002881 lmrC http://purl.obolibrary.org/obo/ARO_3007068 Miscellaneous ABC-F subfamily ATP-binding cassette ribosomal protection proteins lmrC is an ABC-F subfamily protein that confers resistance to lincosamides in Streptomyces lincolnensis and Lactococcus lactis. It can dimerize with lmrD. http://purl.obolibrary.org/obo/ARO_3002882 lmrD http://purl.obolibrary.org/obo/ARO_0010001 ATP-binding cassette (ABC) antibiotic efflux pump lmrD is a chromosomally-encoded efflux pump that confers resistance to lincosamides in Streptomyces lincolnensis and Lactococcus lactis. It can dimerize with lmrC. http://purl.obolibrary.org/obo/ARO_3002883 rgt1438 http://purl.obolibrary.org/obo/ARO_3000443 rifampin glycosyltransferase rgt1438 is a glycosyltransferase that confers rifampin resistance in Streptomyces. http://purl.obolibrary.org/obo/ARO_3002884 iri http://purl.obolibrary.org/obo/ARO_3000445 rifampin monooxygenase iri is a monooxygenase that confers resistance to rifampin found in Rhodococcus hoagii. http://purl.obolibrary.org/obo/ARO_3002891 Streptomyces rimosus otr(A) http://purl.obolibrary.org/obo/ARO_0000002 tetracycline-resistant ribosomal protection protein Streptomyces rimosus otr(A) is an oxytetracycline resistance ribosomal protection protein found in Streptomyces rimosus. http://purl.obolibrary.org/obo/ARO_3002892 otr(B) http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump otr(B) is a tetracycline resistance efflux pump found in Streptomyces rimosus. http://purl.obolibrary.org/obo/ARO_3002893 tcr3 http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump tcr3 is a tetracycline efflux pump that confers self-resistance to Kitasatospora aureofaciens. http://purl.obolibrary.org/obo/ARO_3002894 otr(C) http://purl.obolibrary.org/obo/ARO_0010001 ATP-binding cassette (ABC) antibiotic efflux pump otr(C) is a tetracycline resistance efflux pump found in Streptomyces rimosus. http://purl.obolibrary.org/obo/ARO_3002895 SAT-2 http://purl.obolibrary.org/obo/ARO_3000869 streptothricin acetyltransferase (SAT) SAT-2 is a plasmid-mediated streptothricin acetyltransferase, which confers resistance to streptothricin, a nucleoside antibiotic. Originally described from an E. coli plasmid sequence by Heim et al., 1989. http://purl.obolibrary.org/obo/ARO_3002897 SAT-4 http://purl.obolibrary.org/obo/ARO_3000869 streptothricin acetyltransferase (SAT) SAT-4 is a plasmid-mediated streptothricin acetyltransferase and streptothricin (a nucleoside antibiotic) resistant determinant. Originally described from a Campylobacter coli BE/G4 plasmid gene sequence by Jacob et al, 1994. http://purl.obolibrary.org/obo/ARO_3002898 SAT-3 http://purl.obolibrary.org/obo/ARO_3000869 streptothricin acetyltransferase (SAT) SAT-3 is a plasmid-mediated streptothricin acetyltransferase and streptothricin resistance determinant. Originally described from an E. coli plasmid gene by Tietze and Brevet, 1995. http://purl.obolibrary.org/obo/ARO_3002905 VanS-VanR two-component regulatory system http://purl.obolibrary.org/obo/ARO_3002976 gene(s) or protein(s) associated with a glycopeptide resistance cluster These genes are involved in activating and regulating transcription of gene clusters. http://purl.obolibrary.org/obo/ARO_3002906 Van ligase http://purl.obolibrary.org/obo/ARO_3002976 gene(s) or protein(s) associated with a glycopeptide resistance cluster Van ligases synthesize alternative substrates for peptidoglycan synthesis that reduce vancomycin binding affinity. http://purl.obolibrary.org/obo/ARO_3002907 vanE http://purl.obolibrary.org/obo/ARO_3002979 D-Ala-D-Ser ligase VanE is a D-Ala-D-Ala ligase homolog that can synthesize D-Ala-D-Ser, an alternative substrate for peptidoglycan synthesis that reduces vancomycin binding affinity in Enterococcus faecalis. http://purl.obolibrary.org/obo/ARO_3002908 vanF http://purl.obolibrary.org/obo/ARO_3002978 D-Ala-D-Lac ligase VanF is a D-Ala-D-Ala ligase homolog that can synthesize D-Ala-D-Lac, an alternative substrate for peptidoglycan synthesis that reduces vancomycin binding affinity. It is associated with both vancomycin and teicoplanin resistance in Paenibacillus popilliae. http://purl.obolibrary.org/obo/ARO_3002909 vanG http://purl.obolibrary.org/obo/ARO_3002979 D-Ala-D-Ser ligase VanG is a D-Ala-D-Ala ligase homolog that can synthesize D-Ala-D-Ser, an alternative substrate for peptidoglycan synthesis that reduces vancomycin binding affinity in Enterococcus faecalis. http://purl.obolibrary.org/obo/ARO_3002910 vanL http://purl.obolibrary.org/obo/ARO_3002979 D-Ala-D-Ser ligase VanL is a D-Ala-D-Ala ligase homolog that can synthesize D-Ala-D-Ser, an alternative substrate for peptidoglycan synthesis that reduces vancomycin binding affinity in Enterococcus faecalis. http://purl.obolibrary.org/obo/ARO_3002911 vanM http://purl.obolibrary.org/obo/ARO_3002978 D-Ala-D-Lac ligase VanM is a D-Ala-D-Ala ligase homolog that can synthesize D-Ala-D-Lac, an alternative substrate for peptidoglycan synthesis that reduces vancomycin binding affinity. It is associated with both vancomycin and teicoplanin resistance. http://purl.obolibrary.org/obo/ARO_3002912 vanN http://purl.obolibrary.org/obo/ARO_3002979 D-Ala-D-Ser ligase VanN is a D-Ala-D-Ala ligase homolog that can synthesize D-Ala-D-Ser, an alternative substrate for peptidoglycan synthesis that reduces vancomycin binding affinity in Enterococcus faecium. http://purl.obolibrary.org/obo/ARO_3002913 vanO http://purl.obolibrary.org/obo/ARO_3002978 D-Ala-D-Lac ligase VanO is a D-Ala-D-Ala ligase homolog that can synthesize D-Ala-D-Lac, an alternative substrate for peptidoglycan synthesis that reduces vancomycin binding affinity. It is associated with both vancomycin and teicoplanin resistance. http://purl.obolibrary.org/obo/ARO_3002914 vanJ http://purl.obolibrary.org/obo/ARO_3004255 vanJ membrane protein vanJ is a novel membrane protein that confers resistance to teicoplanin and its derivatives in Streptomyces coelicolor by recycling undecaprenol pyrophosphate during cell wall biosynthesis. http://purl.obolibrary.org/obo/ARO_3002915 vanK http://purl.obolibrary.org/obo/ARO_3002976 gene(s) or protein(s) associated with a glycopeptide resistance cluster VanK is a member of the Fem family of enzymes that add the cross-bridge amino acids to the stem pentapeptide of cell wall precursors in Streptomyces coelicolor that confers inducible, high-level vancomycin resistance. http://purl.obolibrary.org/obo/ARO_3002916 vanV http://purl.obolibrary.org/obo/ARO_3002976 gene(s) or protein(s) associated with a glycopeptide resistance cluster vanV is an accessory protein of van operons, first identified in the vanB operon. It is not required for vancomycin resistance. http://purl.obolibrary.org/obo/ARO_3002917 glycopeptide resistance gene cluster VanN http://purl.obolibrary.org/obo/ARO_3000234 glycopeptide resistance gene cluster Homologous to vanC, contains a D-Ala-D-Ser ligase. The plasmid-located vanM gene cluster is inducible and confers low resistance to vancomycin. vanN organisms remain susceptible to teicoplanin. Gene orientation: N(XY)TRS. http://purl.obolibrary.org/obo/ARO_3002918 glycopeptide resistance gene cluster VanO http://purl.obolibrary.org/obo/ARO_3000234 glycopeptide resistance gene cluster Homologous to vanA, contains a D-Ala-D-Lac ligase. The chromosome-located vanO gene cluster is inducible. Not much is known about the biochemistry about the vanO gene cluster. Gene orientation: orf1 RS orf2 HOX. http://purl.obolibrary.org/obo/ARO_3002919 vanR gene in vanA cluster http://purl.obolibrary.org/obo/ARO_3000574 vanR Also known as vanRA, is a vanR variant found in the vanA gene cluster. http://purl.obolibrary.org/obo/ARO_3002921 vanR gene in vanB cluster http://purl.obolibrary.org/obo/ARO_3000574 vanR Also known as vanRB, is a vanR variant found in the vanB gene cluster. http://purl.obolibrary.org/obo/ARO_3002922 vanR gene in vanC cluster http://purl.obolibrary.org/obo/ARO_3000574 vanR Also known as vanRC, is a vanR variant found in the vanC gene cluster. http://purl.obolibrary.org/obo/ARO_3002923 vanR gene in vanD cluster http://purl.obolibrary.org/obo/ARO_3000574 vanR Also known as vanRD, is a mutated vanR variant found in the vanD gene cluster that caused constitutive expression of vanD peptidoglycan synthesis. http://purl.obolibrary.org/obo/ARO_3002924 vanR gene in vanE cluster http://purl.obolibrary.org/obo/ARO_3000574 vanR Also known as vanRE, is a vanR variant found in the vanE gene cluster. http://purl.obolibrary.org/obo/ARO_3002925 vanR gene in vanF cluster http://purl.obolibrary.org/obo/ARO_3000574 vanR Also known as vanRF, is a vanR variant found in the vanF gene cluster. http://purl.obolibrary.org/obo/ARO_3002926 vanR gene in vanG cluster http://purl.obolibrary.org/obo/ARO_3000574 vanR Also known as vanRG, is a vanR variant found in the vanG gene cluster. http://purl.obolibrary.org/obo/ARO_3002927 vanR gene in vanL cluster http://purl.obolibrary.org/obo/ARO_3000574 vanR Also known as vanRL, is a vanR variant found in the vanL gene cluster. http://purl.obolibrary.org/obo/ARO_3002928 vanR gene in vanM cluster http://purl.obolibrary.org/obo/ARO_3000574 vanR Also known as vanRM, is a vanR variant found in the vanM gene cluster. http://purl.obolibrary.org/obo/ARO_3002929 vanR gene in vanN cluster http://purl.obolibrary.org/obo/ARO_3000574 vanR Also known as vanRN, is a vanR variant found in the vanN gene cluster. http://purl.obolibrary.org/obo/ARO_3002930 vanR gene in vanO cluster http://purl.obolibrary.org/obo/ARO_3000574 vanR Also known as vanRO, is a vanR variant found in the vanO gene cluster. http://purl.obolibrary.org/obo/ARO_3002931 vanS gene in vanA cluster http://purl.obolibrary.org/obo/ARO_3000071 vanS Also known as vanSA, is a vanS variant found in the vanA gene cluster. http://purl.obolibrary.org/obo/ARO_3002932 vanS gene in vanB cluster http://purl.obolibrary.org/obo/ARO_3000071 vanS Also known as vanSB, is a vanS variant found in the vanB gene cluster. http://purl.obolibrary.org/obo/ARO_3002933 vanS gene in vanC cluster http://purl.obolibrary.org/obo/ARO_3000071 vanS Also known as vanSC, is a vanS variant found in the vanC gene cluster. http://purl.obolibrary.org/obo/ARO_3002934 vanS gene in vanD cluster http://purl.obolibrary.org/obo/ARO_3000071 vanS Also known as vanSD, is a mutated vanS variant found in the vanD gene cluster that caused constitutive expression of vanD peptidoglycan synthesis. http://purl.obolibrary.org/obo/ARO_3002935 vanS gene in vanE cluster http://purl.obolibrary.org/obo/ARO_3000071 vanS Also known as vanSE, is a vanS variant found in the vanE gene cluster. http://purl.obolibrary.org/obo/ARO_3002936 vanS gene in vanF cluster http://purl.obolibrary.org/obo/ARO_3000071 vanS Also known as vanSF, is a vanS variant found in the vanF gene cluster. http://purl.obolibrary.org/obo/ARO_3002937 vanS gene in vanG cluster http://purl.obolibrary.org/obo/ARO_3000071 vanS Also known as vanSG, is a vanS variant found in the vanG gene cluster. http://purl.obolibrary.org/obo/ARO_3002938 vanS gene in vanL cluster http://purl.obolibrary.org/obo/ARO_3000071 vanS Also known as vanSL, is a vanS variant found in the vanL gene cluster. http://purl.obolibrary.org/obo/ARO_3002939 vanS gene in vanM cluster http://purl.obolibrary.org/obo/ARO_3000071 vanS Also known as vanSM, is a vanS variant found in the vanM gene cluster. http://purl.obolibrary.org/obo/ARO_3002940 vanS gene in vanN cluster http://purl.obolibrary.org/obo/ARO_3000071 vanS Also known as vanSN, is a vanS variant found in the vanN gene cluster. http://purl.obolibrary.org/obo/ARO_3002941 vanS gene in vanO cluster http://purl.obolibrary.org/obo/ARO_3000071 vanS Also known as vanSO, is a vanS variant found in the vanO gene cluster. http://purl.obolibrary.org/obo/ARO_3002942 vanH gene in vanA cluster http://purl.obolibrary.org/obo/ARO_3000006 vanH Also known as vanHA, is a vanH variant in the vanA gene cluster. http://purl.obolibrary.org/obo/ARO_3002943 vanH gene in vanB cluster http://purl.obolibrary.org/obo/ARO_3000006 vanH Also known as vanHB, is a vanH variant in the vanB gene cluster. http://purl.obolibrary.org/obo/ARO_3002944 vanH gene in vanD cluster http://purl.obolibrary.org/obo/ARO_3000006 vanH Also known as vanHD, is a vanH variant in the vanD gene cluster. http://purl.obolibrary.org/obo/ARO_3002945 vanH gene in vanF cluster http://purl.obolibrary.org/obo/ARO_3000006 vanH Also known as vanHF, is a vanH variant in the vanF gene cluster. http://purl.obolibrary.org/obo/ARO_3002947 vanH gene in vanM cluster http://purl.obolibrary.org/obo/ARO_3000006 vanH Also known as vanHM, is a vanH variant in the vanM gene cluster. http://purl.obolibrary.org/obo/ARO_3002948 vanH gene in vanO cluster http://purl.obolibrary.org/obo/ARO_3000006 vanH Also known as vanHO, is a vanH variant in the vanO gene cluster. http://purl.obolibrary.org/obo/ARO_3002949 vanX gene in vanA cluster http://purl.obolibrary.org/obo/ARO_3000011 vanX Also known as vanXA, is a vanX variant found in the vanA gene cluster. http://purl.obolibrary.org/obo/ARO_3002950 vanX gene in vanB cluster http://purl.obolibrary.org/obo/ARO_3000011 vanX Also known as vanXB, is a vanX variant found in the vanB gene cluster. http://purl.obolibrary.org/obo/ARO_3002952 vanX gene in vanF cluster http://purl.obolibrary.org/obo/ARO_3000011 vanX Also known as vanXF, is a vanX variant found in the vanF gene cluster. http://purl.obolibrary.org/obo/ARO_3002953 vanX gene in vanM cluster http://purl.obolibrary.org/obo/ARO_3000011 vanX Also known as vanXM, is a vanX variant found in the vanM gene cluster. http://purl.obolibrary.org/obo/ARO_3002954 vanX gene in vanO cluster http://purl.obolibrary.org/obo/ARO_3000011 vanX Also known as vanXO, is a vanX variant found in the vanO gene cluster. http://purl.obolibrary.org/obo/ARO_3002955 vanY gene in vanA cluster http://purl.obolibrary.org/obo/ARO_3000077 vanY Also known as vanYA, is a vanY variant found in the vanA gene cluster. http://purl.obolibrary.org/obo/ARO_3002956 vanY gene in vanB cluster http://purl.obolibrary.org/obo/ARO_3000077 vanY Also known as vanYB, is a vanY variant found in the vanB gene cluster. http://purl.obolibrary.org/obo/ARO_3002957 vanY gene in vanD cluster http://purl.obolibrary.org/obo/ARO_3000077 vanY Also known as vanYD, is a vanY variant found in the vanD gene cluster. http://purl.obolibrary.org/obo/ARO_3002958 vanY gene in vanF cluster http://purl.obolibrary.org/obo/ARO_3000077 vanY Also known as vanYF, is a vanY variant found in the vanF gene cluster. http://purl.obolibrary.org/obo/ARO_3002959 vanY gene in vanG cluster http://purl.obolibrary.org/obo/ARO_3000077 vanY Also known as vanYG, is a vanY variant found in the vanG gene cluster. http://purl.obolibrary.org/obo/ARO_3002961 vanY gene in vanM cluster http://purl.obolibrary.org/obo/ARO_3000077 vanY Also known as vanYM, is a vanY variant found in the vanM gene cluster. http://purl.obolibrary.org/obo/ARO_3002962 vanZ gene in vanA cluster http://purl.obolibrary.org/obo/ARO_3000116 vanZ Also known as vanZA, is a vanZ variant found in the vanA gene cluster. http://purl.obolibrary.org/obo/ARO_3002963 vanZ gene in vanF cluster http://purl.obolibrary.org/obo/ARO_3000116 vanZ Also known as vanZF, is a vanZ variant found in the vanF gene cluster. http://purl.obolibrary.org/obo/ARO_3002964 vanW gene in vanB cluster http://purl.obolibrary.org/obo/ARO_3000002 vanW Also known as vanWB, is a vanW variant found in the vanB gene cluster. http://purl.obolibrary.org/obo/ARO_3002965 vanW gene in vanG cluster http://purl.obolibrary.org/obo/ARO_3000002 vanW Also known as vanWG, is a vanW variant found in the vanG gene cluster. http://purl.obolibrary.org/obo/ARO_3002966 vanXY gene in vanC cluster http://purl.obolibrary.org/obo/ARO_3000496 vanXY Also known as vanXYC, is a vanXY variant found in the vanC gene cluster. http://purl.obolibrary.org/obo/ARO_3002967 vanXY gene in vanE cluster http://purl.obolibrary.org/obo/ARO_3000496 vanXY Also known as vanXY, is a vanXY variant found in the vanE gene cluster. http://purl.obolibrary.org/obo/ARO_3002968 vanXY gene in vanL cluster http://purl.obolibrary.org/obo/ARO_3000496 vanXY Also known as vanXYL, is a vanXY variant found in the vanL gene cluster. http://purl.obolibrary.org/obo/ARO_3002969 vanXY gene in vanN cluster http://purl.obolibrary.org/obo/ARO_3000496 vanXY Also known as vanXYN, is a vanXY variant found in the vanN gene cluster. http://purl.obolibrary.org/obo/ARO_3002970 vanT gene in vanC cluster http://purl.obolibrary.org/obo/ARO_3000372 vanT Also known as vanTC, is a vanT variant found in the vanC gene cluster. http://purl.obolibrary.org/obo/ARO_3002971 vanT gene in vanE cluster http://purl.obolibrary.org/obo/ARO_3000372 vanT Also known as vanTE, is a vanT variant found in the vanE gene cluster. http://purl.obolibrary.org/obo/ARO_3002972 vanT gene in vanG cluster http://purl.obolibrary.org/obo/ARO_3000372 vanT Also known as vanTG, is a vanT variant found in the vanG gene cluster. http://purl.obolibrary.org/obo/ARO_3002973 vanTm gene in vanL cluster http://purl.obolibrary.org/obo/ARO_3000372 vanT Also known as vanTmL, is a vanT variant found in the vanL gene cluster. vanTmL codes for the membrane-binding domain of vanTL. http://purl.obolibrary.org/obo/ARO_3002974 vanTr gene in vanL cluster http://purl.obolibrary.org/obo/ARO_3000372 vanT Also known as vanTrL, is a vanT variant found in the vanL gene cluster. vanTrL codes for the racemase component of vanT. http://purl.obolibrary.org/obo/ARO_3002975 vanT gene in vanN cluster http://purl.obolibrary.org/obo/ARO_3000372 vanT Also known as vanTN, is a vanT variant found in the vanN gene cluster. http://purl.obolibrary.org/obo/ARO_3002976 gene(s) or protein(s) associated with a glycopeptide resistance cluster http://purl.obolibrary.org/obo/ARO_3000012 protein(s) conferring antibiotic resistance via molecular bypass Van genes encode for various proteins that are involved in conferring vancomycin and teicoplanin resistance. http://purl.obolibrary.org/obo/ARO_3002978 D-Ala-D-Lac ligase http://purl.obolibrary.org/obo/ARO_3002906 Van ligase A van ligase that synthesizes D-Ala-D-Lac, an alternative peptidoglycan substrate that confers resistance to vancomycin. http://purl.obolibrary.org/obo/ARO_3002979 D-Ala-D-Ser ligase http://purl.obolibrary.org/obo/ARO_3002906 Van ligase A van ligase that synthesizes D-Ala-D-Ser, an alternative peptidoglycan substrate that confers resistance to vancomycin. http://purl.obolibrary.org/obo/ARO_3002980 aspergillomarasmine A http://purl.obolibrary.org/obo/ARO_3007136 unclassified metallo-beta-lactamase inhibitor Aspergillomarasmine A, a fungal natural product, has been shown to inhibit the NDM-1 and VIM-2 enzymes, restoring of the activity of meropenem against carbapenem-resistant pathogens possessing either NDM-1 or VIM-2. http://purl.obolibrary.org/obo/ARO_3002981 AmrAB-OprM http://purl.obolibrary.org/obo/ARO_0010004 resistance-nodulation-cell division (RND) antibiotic efflux pump AmrAB is an RND efflux system that impairs aminoglycoside accumulation in clinical Burkholderia vietnamiensis strains. http://purl.obolibrary.org/obo/ARO_3002982 amrA http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance amrA is the efflux pump subunit of the AmrAB-OprM multidrug efflux complex. amrA corresponds to 1 locus in Pseudomonas aeruginosa PAO1 and 1 locus in Pseudomonas aeruginosa LESB58. http://purl.obolibrary.org/obo/ARO_3002983 amrB http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance amrB is the membrane fusion protein of the AmrAB-OprM multidrug efflux complex. http://purl.obolibrary.org/obo/ARO_3002985 arnA http://purl.obolibrary.org/obo/ARO_3004269 pmr phosphoethanolamine transferase arnA modifies lipid A with 4-amino-4-deoxy-L-arabinose (Ara4N) which allows gram-negative bacteria to resist the antimicrobial activity of cationic antimicrobial peptides and antibiotics such as polymyxin. arnA is found in E. coli and P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3002986 bacA http://purl.obolibrary.org/obo/ARO_3003398 undecaprenyl pyrophosphate related proteins The bacA gene product (BacA) recycles undecaprenyl pyrophosphate during cell wall biosynthesis which confers resistance to bacitracin. http://purl.obolibrary.org/obo/ARO_3002987 bcrA http://purl.obolibrary.org/obo/ARO_0010001 ATP-binding cassette (ABC) antibiotic efflux pump bcrA is an ABC transporter found in Bacillus licheniformis that confers bacitracin resistance. http://purl.obolibrary.org/obo/ARO_3002988 bcrB http://purl.obolibrary.org/obo/ARO_0010001 ATP-binding cassette (ABC) antibiotic efflux pump bcrB is an ABC transporter found in Bacillus licheniformis that confers bacitracin resistance. http://purl.obolibrary.org/obo/ARO_3002992 AQU beta-lactamase http://purl.obolibrary.org/obo/ARO_3000076 class C beta-lactamase AQU beta-lactamases are chromosomal class C beta-lactamases that confer resistance to cephalosporins. http://purl.obolibrary.org/obo/ARO_3002993 AQU-1 http://purl.obolibrary.org/obo/ARO_3002992 AQU beta-lactamase AQU-1 is a chromosomal class C beta-lactamase found in clinical Aeromonas dhakensis isolates. http://purl.obolibrary.org/obo/ARO_3002994 ROB beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase ROB beta-lactamases are a class A beta-lactamases. http://purl.obolibrary.org/obo/ARO_3002995 ROB-1 http://purl.obolibrary.org/obo/ARO_3002994 ROB beta-lactamase ROB-1 is a beta-lactamase found in Pasteurella and Haemophilus. http://purl.obolibrary.org/obo/ARO_3002996 LCR beta-lactamase http://purl.obolibrary.org/obo/ARO_3000075 class D beta-lactamase LCR beta-lactamases are a class D beta-lactamase that hydrolyze a variety of penams and some cephalosporins. http://purl.obolibrary.org/obo/ARO_3002997 LCR-1 http://purl.obolibrary.org/obo/ARO_3002996 LCR beta-lactamase LCR-1 is a class D beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3002998 CblA beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase CblA beta-lactamases are class A beta-lactamases that confer resistance to cephalosporins. http://purl.obolibrary.org/obo/ARO_3002999 CblA-1 http://purl.obolibrary.org/obo/ARO_3002998 CblA beta-lactamase CblA-1 beta-lactamase is a class A beta-lactamase found in Bacteroides uniformis that is species-specific. http://purl.obolibrary.org/obo/ARO_3003000 CfxA beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase CfxA beta-lactamases are class A beta-lactamases. http://purl.obolibrary.org/obo/ARO_3003001 CfxA http://purl.obolibrary.org/obo/ARO_3003000 CfxA beta-lactamase CfxA beta-lactamase is a class A beta-lactamase found in Bacteroides vulgatus. http://purl.obolibrary.org/obo/ARO_3003002 CfxA2 http://purl.obolibrary.org/obo/ARO_3003000 CfxA beta-lactamase CfxA2 beta-lactamase is a class A beta-lactamase found in Prevotella intermedia. http://purl.obolibrary.org/obo/ARO_3003003 CfxA3 http://purl.obolibrary.org/obo/ARO_3003000 CfxA beta-lactamase CfxA3 beta-lactamase is a class A beta-lactamase found in Capnocytophaga ochracea. http://purl.obolibrary.org/obo/ARO_3003005 CfxA4 http://purl.obolibrary.org/obo/ARO_3003000 CfxA beta-lactamase cfxA4 beta-lactamase is a class A beta-lactamase found in Bacteroides fragilis. http://purl.obolibrary.org/obo/ARO_3003006 blt http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump blt is an MFS efflux pump that confers resistance to multiple drugs such as rhodamine and acridine dyes, and fluoroquinolone antibiotics. http://purl.obolibrary.org/obo/ARO_3003007 bmr http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump bmr is an MFS antibiotic efflux pump that confers resistance to multiple drugs including acridine dyes, fluoroquinolone antibiotics, chloramphenicol, and puromycin. http://purl.obolibrary.org/obo/ARO_3003008 CeoAB-OpcM http://purl.obolibrary.org/obo/ARO_0010004 resistance-nodulation-cell division (RND) antibiotic efflux pump CeoAB is an RND efflux system that confers multidrug resistance in Burkholderia cenocepacia. http://purl.obolibrary.org/obo/ARO_3003009 ceoA http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance ceoA is a periplasmic linker subunit of the CeoAB-OpcM efflux pump. http://purl.obolibrary.org/obo/ARO_3003010 ceoB http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance ceoB is a cytoplasmic membrane component of the CeoAB-OpcM efflux pump. http://purl.obolibrary.org/obo/ARO_3003011 dfrA10 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr dfrA10 is an integron-encoded dihydrofolate reductase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3003012 dfrA13 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr dfrA13 is an integron-encoded dihydrofolate reductase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3003013 dfrA15 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr dfrA15 is an integron-encoded dihydrofolate reductase found in Vibrio cholerae. http://purl.obolibrary.org/obo/ARO_3003014 dfrA16 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr dfrA16 is an integron-encoded dihydrofolate reductase found in Salmonella enterica. http://purl.obolibrary.org/obo/ARO_3003015 dfrA19 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr dfrA19 is an integron-encoded dihydrofolate reductase found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3003016 dfrA20 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr dfrA20 is a plasmid-encoded dihydrofolate reductase found in Pasteurella multocida. http://purl.obolibrary.org/obo/ARO_3003017 dfrA21 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr dfrA21 is an integron-encoded dihydrofolate reductase found in Salmonella enterica. http://purl.obolibrary.org/obo/ARO_3003018 dfrA22 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr dfrA22 is an integron-encoded dihydrofolate reductase found in Salmonella enterica. http://purl.obolibrary.org/obo/ARO_3003019 dfrA23 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr dfrA23 is an integron-encoded dihydrofolate reductase found in Salmonella enterica. http://purl.obolibrary.org/obo/ARO_3003020 dfrA25 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr dfrA25 is an integron-encoded dihydrofolate reductase found in Salmonella agona. http://purl.obolibrary.org/obo/ARO_3003021 dfrB2 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr dfrB2 is an integron-encoded dihydrofolate reductase found in an uncultured bacterium from a wastewater treatment plant. http://purl.obolibrary.org/obo/ARO_3003022 dfrB3 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr dfrB3 is an integron-encoded dihydrofolate reductase found in Klebsiella oxytoca. http://purl.obolibrary.org/obo/ARO_3003023 dfrB6 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr dfrB6 is an integron-encoded dihydrofolate reductase found in Salmonella enterica. http://purl.obolibrary.org/obo/ARO_3003025 fusidic acid inactivation enzyme http://purl.obolibrary.org/obo/ARO_3000557 antibiotic inactivation enzyme Enzymes that confer resistance to fusidic acid by inactivation. http://purl.obolibrary.org/obo/ARO_3003026 fusH http://purl.obolibrary.org/obo/ARO_3003025 fusidic acid inactivation enzyme fusH is a highly specific fusidic acid esterase found in Streptomyces lividans. http://purl.obolibrary.org/obo/ARO_3003027 lmrAB Operon http://purl.obolibrary.org/obo/ARO_0010001 ATP-binding cassette (ABC) antibiotic efflux pump lmrAB operon is involved in lincosamide resistance in Bacillus subtilis. http://purl.obolibrary.org/obo/ARO_3003028 lmrA http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux lmrA is the repressor to the lmrAB operon in Bacillus subtilis. lmrA mutations result in lincomycin resistance. http://purl.obolibrary.org/obo/ARO_3003029 MexVW-OprM http://purl.obolibrary.org/obo/ARO_0010004 resistance-nodulation-cell division (RND) antibiotic efflux pump MexVW-OprM is a multidrug efflux protein expressed in Pseudomonas aeruginosa. MexV is the membrane fusion protein; MexW is the RND-type membrane protein; and OprM is the outer membrane channel. MexVW-OprM is associated with resistance to fluoroquinolones, tetracycline, chloramphenicol, erythromycin and acriflavine. http://purl.obolibrary.org/obo/ARO_3003030 MexV http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MexV is the membrane fusion protein of the MexVW-OprM multidrug efflux complex. http://purl.obolibrary.org/obo/ARO_3003031 MexW http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MexW is the RND-type membrane protein of the efflux complex MexVW-OprM. http://purl.obolibrary.org/obo/ARO_3003032 MexXY-OprM http://purl.obolibrary.org/obo/ARO_0010004 resistance-nodulation-cell division (RND) antibiotic efflux pump MexXY-OprM is a multidrug efflux protein expressed in Pseudomonas aeruginosa. MexY is the membrane fusion protein; MexX is the RND-type membrane protein; and OprM is the outer membrane channel. MexXY-OprM is associated with resistance to acriflavine, erythromycin, norfloxacin and ofloxacin. The efflux system may also be involved in acquisition of higher resistance, in particular when bacteria are repeatedly exposed to subinhibitory doses of AGs. http://purl.obolibrary.org/obo/ARO_3003033 mexY http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MexY is the RND-type membrane protein of the efflux complex MexXY-OprM. http://purl.obolibrary.org/obo/ARO_3003034 mexX http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MexX is the membrane fusion protein of the MexXY-OprM multidrug efflux complex. http://purl.obolibrary.org/obo/ARO_3003035 mfpA http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) mfpA is a qnr homolog and a pentapeptide repeat protein that confers resistance to fluoroquinolones in Mycolicibacterium smegmatis. http://purl.obolibrary.org/obo/ARO_3003036 oleB http://purl.obolibrary.org/obo/ARO_3007068 Miscellaneous ABC-F subfamily ATP-binding cassette ribosomal protection proteins oleB is an ABC-F subfamily protein in Streptomyces antibioticus and is involved in oleandomycin secretion. http://purl.obolibrary.org/obo/ARO_3003037 opcM http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance OpcM is an outer membrane factor protein found in Burkholderia cepacia. It is part of the CeoAB-OpcM complex. http://purl.obolibrary.org/obo/ARO_3003038 MexXY-OprA http://purl.obolibrary.org/obo/ARO_0010004 resistance-nodulation-cell division (RND) antibiotic efflux pump MexXY-OprA is a multidrug efflux protein expressed in Pseudomonas aeruginosa. MexY is the membrane fusion protein; MexX is the RND-type membrane protein; and OprA is the outer membrane channel. MexXY-OprA is associated with resistance to aminoglycosides. http://purl.obolibrary.org/obo/ARO_3003039 OprA http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance OprA is an outer membrane factor protein found in Pseudomonas aeruginosa. It is part of the MexXY-OprA complex. http://purl.obolibrary.org/obo/ARO_3003040 beta-lactam resistant penicillin-binding proteins http://purl.obolibrary.org/obo/ARO_3000000 determinant of antibiotic resistance Pencillin-binding proteins are transpeptidase proteins essential for cell wall synthesis. PBPs bind to penicillin antibiotics, which inactivates the enzyme and therefore disrupts cell wall synthesis. Multiple mechanisms and determinants are implicated in antibiotic resistant PBP. http://purl.obolibrary.org/obo/ARO_3003041 Streptococcus pneumoniae PBP1a conferring resistance to amoxicillin http://purl.obolibrary.org/obo/ARO_3003938 Penicillin-binding protein mutations conferring resistance to beta-lactam antibiotics PBP1a is a penicillin-binding protein found in Streptococcus pneumoniae. http://purl.obolibrary.org/obo/ARO_3003042 Streptococcus pneumoniae PBP2b conferring resistance to amoxicillin http://purl.obolibrary.org/obo/ARO_3003938 Penicillin-binding protein mutations conferring resistance to beta-lactam antibiotics PBP2b is a penicillin-binding protein found in Streptococcus pneumoniae. http://purl.obolibrary.org/obo/ARO_3003043 Streptococcus pneumoniae PBP2x conferring resistance to amoxicillin http://purl.obolibrary.org/obo/ARO_3003938 Penicillin-binding protein mutations conferring resistance to beta-lactam antibiotics PBP2x is a penicillin-binding protein found in Streptococcus pneumoniae. http://purl.obolibrary.org/obo/ARO_3003046 qacA http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump qacA is a subunit of the qac multidrug efflux pump. http://purl.obolibrary.org/obo/ARO_3003047 qacB http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump qacB is a subunit of the qac multidrug efflux pump. http://purl.obolibrary.org/obo/ARO_3003048 rosA http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance rosA is part of an efflux pump/potassium antiporter system (RosAB) in Yersinia that confers resistance to cationic antimicrobial peptides such as polymyxin B. http://purl.obolibrary.org/obo/ARO_3003049 rosB http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance rosB is part of an efflux pump/potassium antiporter system (RosAB) in Yersinia that confers resistance to cationic antimicrobial peptides such as polymyxin B. http://purl.obolibrary.org/obo/ARO_3003050 SmeABC http://purl.obolibrary.org/obo/ARO_0010004 resistance-nodulation-cell division (RND) antibiotic efflux pump SmeABC is a multidrug resistance efflux pump that confers resistance to aminoglycosides, beta-lactams, and fluoroquinolones in Stenotrophomonas maltophilia. http://purl.obolibrary.org/obo/ARO_3003051 smeA http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance smeA is the membrane fusion protein of the smeABC multidrug efflux complex in Stenotrophomonas maltophilia. http://purl.obolibrary.org/obo/ARO_3003052 smeB http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance smeB is the inner membrane multidrug exporter of the efflux complex smeABC in Stenotrophomonas maltophilia. http://purl.obolibrary.org/obo/ARO_3003053 smeC http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance smeC is an outer membrane multidrug efflux protein of the smeABC complex in Stenotrophomonas maltophilia. http://purl.obolibrary.org/obo/ARO_3003054 SmeDEF http://purl.obolibrary.org/obo/ARO_0010004 resistance-nodulation-cell division (RND) antibiotic efflux pump SmeDEF is a multidrug resistance efflux pump that confers resistance to quinolones, tetracyclines, macrolides, chloramphenicol, and novobiocin in Stenotrophomonas maltophilia. http://purl.obolibrary.org/obo/ARO_3003055 smeD http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance smeD is the membrane fusion protein of the smeDEF multidrug efflux complex in Stenotrophomonas maltophilia. http://purl.obolibrary.org/obo/ARO_3003056 smeE http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance smeE is the RND protein of the efflux complex smeDEF in Stenotrophomonas maltophilia. http://purl.obolibrary.org/obo/ARO_3003057 smeF http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance smeF is an outer membrane multidrug efflux protein of the smeDEF complex in Stenotrophomonas maltophilia. http://purl.obolibrary.org/obo/ARO_3003059 tmrB http://purl.obolibrary.org/obo/ARO_3004285 tunicamycin resistance protein tmrB is an ATP-binding tunicamycin resistance protein found in Bacillus subtilis. http://purl.obolibrary.org/obo/ARO_3003060 tsnR http://purl.obolibrary.org/obo/ARO_3003065 non-erm 23S ribosomal RNA methyltransferase (A1067) tsnR is a 23S ribosomal RNA methyltransferase that methylates adenosine-1067 to confer resistance to thiostrepton. http://purl.obolibrary.org/obo/ARO_3003061 vph http://purl.obolibrary.org/obo/ARO_3004261 viomycin phosphotransferase vph is a phosphotransferase that confers resistance to viomycin in Streptomyces vinaceus. http://purl.obolibrary.org/obo/ARO_3003062 ykkCD http://purl.obolibrary.org/obo/ARO_0010003 small multidrug resistance (SMR) antibiotic efflux pump ykkCD is a multidrug efflux pump with two SMR-type protein subunits that confers resistance to cationic drugs, chloramphenicol, streptomycin and tetracycline. http://purl.obolibrary.org/obo/ARO_3003063 ykkC http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance ykkC is an SMR-type protein that is a subunit of the ykkCD efflux pump. http://purl.obolibrary.org/obo/ARO_3003064 ykkD http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance ykkD is an SMR-type protein that is a subunit of the ykkCD efflux pump. http://purl.obolibrary.org/obo/ARO_3003065 non-erm 23S ribosomal RNA methyltransferase (A1067) http://purl.obolibrary.org/obo/ARO_3004274 23S ribosomal RNA methyltransferase Non-erm 23S ribosomal RNA methyltransferases modify adenosine 1067 to confer resistance to peptide antibiotics. http://purl.obolibrary.org/obo/ARO_3003066 smeR http://purl.obolibrary.org/obo/ARO_3000750 protein of two-component regulatory system modulating antibiotic efflux smeR is the responder component of a two component signal transduction system that includes smeS. http://purl.obolibrary.org/obo/ARO_3003067 smeS http://purl.obolibrary.org/obo/ARO_3000750 protein of two-component regulatory system modulating antibiotic efflux smeS is the protein kinase sensor component of a two component signal transduction system that includes smeR. http://purl.obolibrary.org/obo/ARO_3003068 smeRS http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux smeRS is a two component regulatory system for smeABC where smeR is a response regulator, while smeS is a sensor kinase. http://purl.obolibrary.org/obo/ARO_3003069 vanXY gene in vanG cluster http://purl.obolibrary.org/obo/ARO_3000496 vanXY Also known as vanXYG, is a vanXY variant found in the vanG gene cluster. http://purl.obolibrary.org/obo/ARO_3003070 vanX gene in vanD cluster http://purl.obolibrary.org/obo/ARO_3000011 vanX Also known as vanXD, is a vanX variant found in the vanD gene cluster. http://purl.obolibrary.org/obo/ARO_3003071 mphF http://purl.obolibrary.org/obo/ARO_3000333 macrolide phosphotransferase (MPH) mphF is a macrolide phosphotransferase and resistance gene identified on the IncP plasmid pRSB111. http://purl.obolibrary.org/obo/ARO_3003072 mphL http://purl.obolibrary.org/obo/ARO_3000333 macrolide phosphotransferase (MPH) mphL is a chromosomally-encoded macrolide phosphotransferases that inactivate 14- and 15-membered macrolides such as erythromycin, clarithromycin, azithromycin. http://purl.obolibrary.org/obo/ARO_3003074 Staphylococcus aureus cls conferring resistance to daptomycin http://purl.obolibrary.org/obo/ARO_3003272 daptomycin resistant cls Cardiolipin synthetase (cls) is an inner membrane protein that is involved in membrane synthesis. Specific mutations in S. aureus can confer resistance to daptomycin. http://purl.obolibrary.org/obo/ARO_3003076 daptomycin resistant liaFSR http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux liaFSR is a two-component signal transduction pathway in B. subtilis that responds to peptide and lipopeptide antibiotics. The liaFSR two-component system consists of a histidine kinase liaS and the response regulator liaR as well as the accessory protein liaF, which acts as a negative regulator of liaRS-dependent signal transduction. Mutations confer resistance to daptomycin. http://purl.obolibrary.org/obo/ARO_3003077 Enterococcus faecalis liaF mutant conferring daptomycin resistance http://purl.obolibrary.org/obo/ARO_3004262 daptomycin resistant liaF liaF is an accessory protein that acts as a negative regulator of liaRS signal transduction pathway. Mutations confer daptomycin resistance. http://purl.obolibrary.org/obo/ARO_3003078 Enterococcus faecium liaR mutant conferring daptomycin resistance http://purl.obolibrary.org/obo/ARO_3004263 daptomycin resistant liaR liaR is a response regulator found in the liaFSR signal transduction pathway. Mutations confer daptomycin resistance. http://purl.obolibrary.org/obo/ARO_3003079 Enterococcus faecium liaS mutant conferring daptomycin resistance http://purl.obolibrary.org/obo/ARO_3004264 daptomycin resistant liaS liaS is a histidine kinase found in the liaFSR signal transduction pathway. Mutations confer daptomycin resistance. http://purl.obolibrary.org/obo/ARO_3003080 daptomycin resistant pgsA http://purl.obolibrary.org/obo/ARO_3003420 antibiotic resistant pgsA pgsA or phosphatidylglycerophosphate synthetase is an integral membrane protein involved in phospholipid biosynthesis. It is a CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase. Laboratory experiments have detected mutations conferring daptomycin resistance in Entercoccus. http://purl.obolibrary.org/obo/ARO_3003090 daptomycin-resistant beta-subunit of RNA polymerase (rpoB) http://purl.obolibrary.org/obo/ARO_3003276 antibiotic resistant rpoB Daptomycin-resistant RNA polymerases include amino acids substitutions which alter expression of the dlt operon, which increases the cell surface positive charge. Known from S. aureus. http://purl.obolibrary.org/obo/ARO_3003091 daptomycin resistant mprF http://purl.obolibrary.org/obo/ARO_3003421 antibiotic resistant mprF MprF is a integral membrane protein that modifies the negatively-charged phosphatidylglycerol on the membrane surface of both Gram-positive and Gram-negative bacteria. This confers resistance to cationic peptides that disrupt the cell membrane, including defensins. Mutations in mprF can additionally confer resistance to daptomycin in S. aureus. http://purl.obolibrary.org/obo/ARO_3003092 Enterococcus faecium cls conferring resistance to daptomycin http://purl.obolibrary.org/obo/ARO_3003272 daptomycin resistant cls cls or cardiolipin synthetase is an inner membrane protein that is involved in membrane synthesis. Specific mutations in Enterococcus can confer resistance to daptomycin. http://purl.obolibrary.org/obo/ARO_3003093 cphA3 http://purl.obolibrary.org/obo/ARO_3000581 CphA beta-lactamase CEPH-A3 is an Ambler Class B MBL; subclass B2 originally isolated from Aeromonas veronii. This enzyme has specific activity against carbapenems and is active as a mono-zinc protein. http://purl.obolibrary.org/obo/ARO_3003094 imiH http://purl.obolibrary.org/obo/ARO_3000581 CphA beta-lactamase imiH is an Ambler Class B MBL; subclass B2 originally isolated from Aeromonas hydrophila. This enzyme has specific activity against carbapenems. http://purl.obolibrary.org/obo/ARO_3003095 imiS http://purl.obolibrary.org/obo/ARO_3000581 CphA beta-lactamase imiS is an Ambler Class B MBL; subclass B2 originally isolated from Aeromonas veronii. This enzyme has specific activity against carbapenems. http://purl.obolibrary.org/obo/ARO_3003096 CfxA5 http://purl.obolibrary.org/obo/ARO_3003000 CfxA beta-lactamase CfxA5 beta-lactamase is a class A beta-lactamase found in Bacteroides distasonis. http://purl.obolibrary.org/obo/ARO_3003097 CfxA6 http://purl.obolibrary.org/obo/ARO_3003000 CfxA beta-lactamase CfxA6 beta-lactamase is a class A beta-lactamase found in an uncultured bacterium. http://purl.obolibrary.org/obo/ARO_3003099 cphA2 http://purl.obolibrary.org/obo/ARO_3000581 CphA beta-lactamase CphA2 is an Ambler Class B MBL; subclass B2 originally isolated from Aeromonas hydrophila. This enzyme has specific activity against carbapenems and is active as a mono-zinc protein. http://purl.obolibrary.org/obo/ARO_3003100 cphA4 http://purl.obolibrary.org/obo/ARO_3000581 CphA beta-lactamase CphA4 is an Ambler Class B MBL; subclass B2 originally isolated from Aeromonas allosaccharophila. This enzyme has specific activity against carbapenems and is active as a mono-zinc protein. http://purl.obolibrary.org/obo/ARO_3003101 cphA5 http://purl.obolibrary.org/obo/ARO_3000581 CphA beta-lactamase cphA5 is an Ambler Class B MBL; subclass B2 originally isolated from Aeromonas salmonicida. This enzyme has specific activity against carbapenems and is active as a mono-zinc protein. http://purl.obolibrary.org/obo/ARO_3003102 cphA6 http://purl.obolibrary.org/obo/ARO_3000581 CphA beta-lactamase cphA6 is an Ambler Class B MBL; subclass B2 originally isolated from Aeromonas veronii. This enzyme has specific activity against carbapenems and is active as a mono-zinc protein. http://purl.obolibrary.org/obo/ARO_3003103 cphA7 http://purl.obolibrary.org/obo/ARO_3000581 CphA beta-lactamase cphA7 is an Ambler Class B MBL; subclass B2 originally isolated from Aeromonas jandaei. This enzyme has specific activity against carbapenems and is active as a mono-zinc protein. http://purl.obolibrary.org/obo/ARO_3003104 cphA8 http://purl.obolibrary.org/obo/ARO_3000581 CphA beta-lactamase cphA8 is an Ambler Class B MBL; subclass B2 originally isolated from Aeromonas sobria. This enzyme has specific activity against carbapenems and is active as a mono-zinc protein. http://purl.obolibrary.org/obo/ARO_3003105 dfrA3 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr dfrA3 is an integron-encoded dihydrofolate reductase found in Escherichia coli. http://purl.obolibrary.org/obo/ARO_3003106 Erm(42) http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase Erm42 confers MLSb phenotype in Pasteurella multocida. http://purl.obolibrary.org/obo/ARO_3003107 mef(B) http://purl.obolibrary.org/obo/ARO_3000747 mef mef(B) is a macrolide efflux gene located in the vicinity of sul3 in Escherichia coli. There is also a mefB found in Streptococcus agalactiae that confers resistance to macrolides. http://purl.obolibrary.org/obo/ARO_3003109 msrE http://purl.obolibrary.org/obo/ARO_3004471 msr-type ABC-F protein MsrE is an ABC-F subfamily protein expressed to Klebsiella pneumoniae that confers resistance to erythromycin and streptogramin B antibiotics. It is associated with plasmid DNA. It is also 100% identical to ABC-F type ribosomal protection protein Msr(E) which is in multiple species. http://purl.obolibrary.org/obo/ARO_3003110 catB10 http://purl.obolibrary.org/obo/ARO_3000122 chloramphenicol acetyltransferase (CAT) catB10 is an integron-encoded variant of the cat gene found in P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3003111 lsaB http://purl.obolibrary.org/obo/ARO_3004472 lsa-type ABC-F protein LsaB is an ABC-F subfamily protein expressed in Mammaliicoccus sciuri. It confers resistance to clindamycin. http://purl.obolibrary.org/obo/ARO_3003112 lsaC http://purl.obolibrary.org/obo/ARO_3004472 lsa-type ABC-F protein LsaC is an ABC-F subfamily protein expressed in Streptococcus agalactiae. It confers resistance to lincomycin, clindamycin, dalfopristin, and tiamulin. http://purl.obolibrary.org/obo/ARO_3003113 TEM-221 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-221 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003114 TEM-222 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-222 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003115 OXA-427 http://purl.obolibrary.org/obo/ARO_3007719 OXA-427-like beta-lactamase OXA-427 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003116 OXA-420 http://purl.obolibrary.org/obo/ARO_3007728 OXA-58-like beta-lactamase OXA-420 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003117 OXA-421 http://purl.obolibrary.org/obo/ARO_3007706 OXA-213-like beta-lactamase OXA-421 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003119 OXA-428 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-428 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003120 OXA-429 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-429 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003121 OXA-430 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-430 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003124 OXA-431 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-431 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003125 OXA-432 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-432 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003126 OXA-433 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-433 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003127 OXA-434 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-434 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003128 OXA-436 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase An OXA-48-like plasmid-encoded beta-lactamase shown to confer resistance to carbapenems through hydrolysis. Identified in multiple Enterobacteriaceae isolates from several patients in Denmark. Beta-lactamase activity against carbapenems and penicillins but little to no activity against cephalosporin antibiotics. Described by Samuelsen et al. 2017. http://purl.obolibrary.org/obo/ARO_3003129 CMY-121 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-121 is a beta-lactamase found in Escherichia coli. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3003130 CMY-122 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-122 is a beta-lactamase found in Citrobacter freundii. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3003131 CMY-123 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-123 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003132 CMY-124 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-124 is a beta-lactamase found in Citrobacter freundii. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3003133 CMY-125 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-125 is a beta-lactamase found in Citrobacter freundii. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3003134 CMY-126 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-126 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003135 CMY-127 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-127 is a beta-lactamase found in Citrobacter freundii. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3003136 CMY-128 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-128 is a beta-lactamase found in Citrobacter freundii. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3003137 CMY-129 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-129 is a beta-lactamase found in Citrobacter freundii. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3003138 CMY-130 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-130 is a beta-lactamase found in Escherichia coli. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3003139 MIR-18 http://purl.obolibrary.org/obo/ARO_3000058 MIR beta-lactamase MIR-18 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003140 MOX-10 http://purl.obolibrary.org/obo/ARO_3000083 MOX beta-lactamase MOX-10 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003141 MOX-11 http://purl.obolibrary.org/obo/ARO_3000083 MOX beta-lactamase MOX-11 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003142 IMI-8 http://purl.obolibrary.org/obo/ARO_3000018 IMI beta-lactamase IMI-8 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003143 IMI-9 http://purl.obolibrary.org/obo/ARO_3000018 IMI beta-lactamase IMI-9 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003144 KPC-20 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-20 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003145 KPC-21 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-21 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003146 VEB-10 http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase VEB-10 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003147 OXA-424 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-424 is a beta-lactamase found in clinical isolates of Acinetobacter baumannii found in China. It is carbapenem resistant. http://purl.obolibrary.org/obo/ARO_3003148 OXA-425 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-425 is a beta-lactamase found in clinical isolates of Acinetobacter baumannii. It is carbapenem-resistant. http://purl.obolibrary.org/obo/ARO_3003149 OXA-426 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-426 is a beta-lactamase found in clinical isolates of Acinetobacter baumannii. It is carbapenem resistant. http://purl.obolibrary.org/obo/ARO_3003150 CARB-20 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-20 is a beta-lactamase found worldwide in Vibrio parahaemolyticus. http://purl.obolibrary.org/obo/ARO_3003151 CARB-22 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-22 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003152 SHV-185 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-185 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003153 SHV-186 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-186 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003154 SHV-187 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-187 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003155 SHV-188 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-188 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003156 SHV-189 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-189 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003157 TEM-219 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-219 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003158 TEM-220 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-220 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003159 OXA-419 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-419 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003160 OXA-422 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-422 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003161 OXA-423 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-423 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003162 OXA-435 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-435 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003163 CTX-M-155 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-155 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003164 CTX-M-156 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-156 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003165 CTX-M-157 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-157 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003166 CTX-M-158 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-158 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003167 CTX-M-159 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-159 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003168 CTX-M-160 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-160 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003169 CTX-M-161 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-161 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003170 CMY-131 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-131 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003171 ACT-36 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-36 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003172 ACT-37 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase ACT-37 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003173 MIR-17 http://purl.obolibrary.org/obo/ARO_3000058 MIR beta-lactamase MIR-17 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003174 CARB-18 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-18 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003175 CARB-19 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-19 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003176 CARB-21 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-21 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003177 IMI-7 http://purl.obolibrary.org/obo/ARO_3000018 IMI beta-lactamase IMI-7 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003178 VIM-42 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-42 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003179 VIM-43 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-43 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003180 KPC-22 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-22 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003181 GES-26 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-26 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003182 NDM-13 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase Beta-lactamase found in Escherichia coli clinical isolates in Nepal. http://purl.obolibrary.org/obo/ARO_3003183 NDM-14 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase NDM-14 is a beta-lactamase found in Acinetobacter lwoffii. http://purl.obolibrary.org/obo/ARO_3003184 PER-8 http://purl.obolibrary.org/obo/ARO_3000056 PER beta-lactamase PER-8 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003185 GES-25 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-25 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003186 CARB-23 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-23 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003187 QnrB75 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB75 is a fluoroquinolone resistance gene in Lahey's list of qnr genes. http://purl.obolibrary.org/obo/ARO_3003188 QnrB76 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB76 is a fluoroquinolone resistance gene in Lahey's list of qnr genes. http://purl.obolibrary.org/obo/ARO_3003189 QnrB77 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB77 is a fluoroquinolone resistance gene in Lahey's list of qnr genes. http://purl.obolibrary.org/obo/ARO_3003190 QnrB78 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB78 is a fluoroquinolone resistance gene in Lahey's list of qnr genes. http://purl.obolibrary.org/obo/ARO_3003192 QnrB80 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrB80 is a fluoroquinolone resistance gene in Lahey's list of qnr genes. http://purl.obolibrary.org/obo/ARO_3003193 QnrVC7 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrVC7 is a fluoroquinolone resistance gene in Lahey's list of qnr genes. http://purl.obolibrary.org/obo/ARO_3003194 GIM-2 http://purl.obolibrary.org/obo/ARO_3003195 GIM beta-lactamase GIM-2 is a metallo-beta-lactamase present on an integron found in clinical isolates of Enterobacter cloacae in Germany. http://purl.obolibrary.org/obo/ARO_3003195 GIM beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase GIM beta-lactamase enzymes isolated from Pseudomonas aeruginosa, and found to confer broad-spectrum resistance to beta-lactam antibiotics. http://purl.obolibrary.org/obo/ARO_3003196 tet(45) http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump Tet45 is a tetracycline efflux pump found in Bhargavaea cecembensis strain previously isolated from a poultry-litter-impacted soil. http://purl.obolibrary.org/obo/ARO_3003197 aadA25 http://purl.obolibrary.org/obo/ARO_3000232 ANT(3'')-Ia Streptomycin/spectinomycin resistance gene found in Pasteurella multocida isolated from bovine respiratory tract. http://purl.obolibrary.org/obo/ARO_3003198 rmtH http://purl.obolibrary.org/obo/ARO_3004271 16S rRNA methyltransferase (G1405) rmtH is a 16s ribosomal RNA methyltransferase found in Klebsiella pneumoniae strain MRSN2404 that was isolated from the chronic wound of a soldier wounded in Iraq in 2006. It confers high resistance to aminoglycosides. http://purl.obolibrary.org/obo/ARO_3003199 AAC(6')-Iak http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Iak is a 6'-N-aminoglycoside acetyltransferase-encoding gene isolated from a multidrug-resistant clinical isolate of Stenotrophomonas maltophilia. http://purl.obolibrary.org/obo/ARO_3003200 AAC(6')-Ian http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Ian is an amikacin acetyltransferase gene found on a transferable plasmid of the Serratia marcescens strain NUBL-11663. It catalyzes the transfer of an acetyl group from acetyl coenzyme A onto an amine at the 6'-position of various aminoglycosides. http://purl.obolibrary.org/obo/ARO_3003201 TLA beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase The TLA beta-lactamases are resistant to expanded-spectrum cephalosporins, and aztreonam but was susceptible to amikacin, cefotetan, and imipenem. http://purl.obolibrary.org/obo/ARO_3003202 TLA-1 http://purl.obolibrary.org/obo/ARO_3003201 TLA beta-lactamase TLA-1 is a beta-lactamase found in plasmids of clinical isolates of Escherichia coli strain R170 in Latin America. It preferentially hydrolyzed cephaloridine, cefotaxime, cephalothin, benzylpenicillin, and ceftazidime. The enzyme was markedly inhibited by sulbactam, tazobactam, and clavulanic acid. http://purl.obolibrary.org/obo/ARO_3003203 TLA-2 http://purl.obolibrary.org/obo/ARO_3003201 TLA beta-lactamase TLA-2 is a beta-lactamase is present on a plasmid isolated from an unidentified bacterial strain from a waste water treatment plant. The enzyme mostly hydrolyzes cephalosporins. http://purl.obolibrary.org/obo/ARO_3003204 TLA-3 http://purl.obolibrary.org/obo/ARO_3003201 TLA beta-lactamase TLA-3 is a beta-lactamase found in a transferable plasmid of Serratia marcescens clinical isolate. It confers resistance to ceftazidime, cefotaxime and cefepime, but not to cefmetazole and meropenem. http://purl.obolibrary.org/obo/ARO_3003205 Erm(43) http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase Erm(43) is a macrolide, lincosamide, and streptogramin B resistance gene found in Mammaliicoccus lentus chromosome isolated from human, dog and chicken. http://purl.obolibrary.org/obo/ARO_3003206 lsaE http://purl.obolibrary.org/obo/ARO_3004472 lsa-type ABC-F protein lsaE is an ABC-F subfamily protein found in porcine MRSA isolates. It confers resistance to pleuromutilin, lincosamide, and streptogramin A. http://purl.obolibrary.org/obo/ARO_3003207 FosK http://purl.obolibrary.org/obo/ARO_3000133 fosfomycin thiol transferase FosK is a fosfomycin thiol transferase isolated from Acinetobacter soli. It is integrin-mediated. It confers a high level of resistance to fosfomycin. http://purl.obolibrary.org/obo/ARO_3003208 FosXCC http://purl.obolibrary.org/obo/ARO_3000133 fosfomycin thiol transferase fosXCC is a fosfomycin resistance gene that modifies MurA isolated from Campylobacter species. It is highly resistant to fosfomycin. http://purl.obolibrary.org/obo/ARO_3003209 fosA5 http://purl.obolibrary.org/obo/ARO_3000133 fosfomycin thiol transferase fosA5 is a fosfomycin resistance gene isolated from clinical strain of Escherichia coli E265. It is susceptible to amikacin, tetracycline and imipenem, and resistant to sulphonamide, cephalosporins, gentamicin, ciprofloxacin, chloramphenicol and streptomycin. http://purl.obolibrary.org/obo/ARO_3003210 FosA4 http://purl.obolibrary.org/obo/ARO_3000133 fosfomycin thiol transferase FosA4 is an enzyme that confers resistance to fosfomycin in Escherichia coli by breaking the epoxide ring of the molecule. http://purl.obolibrary.org/obo/ARO_3003211 16S rRNA with mutation conferring antibiotic resistance http://purl.obolibrary.org/obo/ARO_3000328 rRNA with mutation conferring antibiotic resistance Many antibiotics inhibit the growth of bacteria by blocking protein synthesis on the ribosome. The antibiotic-binding sites are located within functionally important structures in the ribosomal RNA. Antibiotic resistance is often conferred by base substitutions or methylations at these sites in the rRNA. Point mutations in the bacterial 16S ribosomal RNA in the small 30S subunit can confer resistance to antibiotics. http://purl.obolibrary.org/obo/ARO_3003223 Escherichia coli 16S rRNA mutation conferring resistance to edeine http://purl.obolibrary.org/obo/ARO_3003667 16s rRNA with mutation conferring resistance to peptide antibiotics Point mutations in the 3' minor domain of the 16S rRNA in Escherichia coli can confer resistance to edeine. http://purl.obolibrary.org/obo/ARO_3003231 Lipid II http://purl.obolibrary.org/obo/ARO_3000721 cell wall component targeted by antibiotic Precursor molecule during the synthesis of bacterial cell wall. Lipid II anchors itself onto the cell and it's disaccharide-peptide subunit is used in PG polymer assembly by peptidoglycan glycosyltransferases. Due to it's importance in cell wall synthesis, it is the target of antibiotics. http://purl.obolibrary.org/obo/ARO_3003232 Lipid III http://purl.obolibrary.org/obo/ARO_3000721 cell wall component targeted by antibiotic Lipid III is the precursor to the wall teichoic acid. It's inhibition leads to bacterial death as teichoic acid is required to anchor autolysins which control the hydrolysis of peptidoglycan cell wall. http://purl.obolibrary.org/obo/ARO_3003236 Mycobacteroides abscessus 16S rRNA mutation conferring resistance to kanamycin http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in the 16S rRNA of Mycobacteroides abscessus conferring resistance to kanamycin. http://purl.obolibrary.org/obo/ARO_3003237 Mycobacteroides abscessus 16S rRNA mutation conferring resistance to tobramycin http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in the 16S rRNA of Mycobacteroides abscessus conferring resistance to tobramycin. http://purl.obolibrary.org/obo/ARO_3003238 Mycobacteroides abscessus 16S rRNA mutation conferring resistance to neomycin http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in the 16S rRNA of Mycobacteroides abscessus conferring resistance to neomycin. http://purl.obolibrary.org/obo/ARO_3003239 Mycobacteroides abscessus 16S rRNA mutation conferring resistance to amikacin http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in the 16S rRNA of Mycobacteroides abscessus conferring resistance to amikacin. http://purl.obolibrary.org/obo/ARO_3003240 Mycobacteroides abscessus 16S rRNA mutation conferring resistance to gentamicin http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in the 16S rRNA of Mycobacteroides abscessus conferring resistance to gentamicin. http://purl.obolibrary.org/obo/ARO_3003241 teixobactin http://purl.obolibrary.org/obo/ARO_3000053 peptide antibiotic Teixobactin is a peptide antibiotic isolated from the Gram-negative bacteria, Eleftheria terrae. It inhibits the synthesis of peptidoglycan by interacting with peptidoglycan precursor, Lipid II and Lipid III. http://purl.obolibrary.org/obo/ARO_3003250 bcrC http://purl.obolibrary.org/obo/ARO_3003398 undecaprenyl pyrophosphate related proteins The bcrC gene product (BcrC) is an undecaprenyl pyrophosphate phosphatase originally isolated from Bacillus subtilis. When overexpressed it can confer resistance to bacitracin. http://purl.obolibrary.org/obo/ARO_3003251 undecaprenyl pyrophosphate http://purl.obolibrary.org/obo/ARO_3000721 cell wall component targeted by antibiotic Undecaprenyl pyrophosphate is a precursor to a cell wall polymer carrier. It's activation requires a phosphatase. http://purl.obolibrary.org/obo/ARO_3003253 aminocoumarin sensitive parY http://purl.obolibrary.org/obo/ARO_3003258 Antibiotic sensitive DNA topoisomerase subunit parY Subunit of topoisomerase IV sensitive to aminocourmarins. http://purl.obolibrary.org/obo/ARO_3003254 antibiotic sensitive DNA topoisomerase subunit gyrA http://purl.obolibrary.org/obo/ARO_3000766 antibiotic sensitive topoisomerase subunit DNA gyrase is responsible for DNA supercoiling and consists of two alpha and two beta subunits. Binding the alpha-subunit is sufficient to inhibit DNA supercoiling. http://purl.obolibrary.org/obo/ARO_3003256 antibiotic sensitive DNA topoisomerase subunit parC http://purl.obolibrary.org/obo/ARO_3000766 antibiotic sensitive topoisomerase subunit ParC is a subunit of topoisomerase IV, which decatenates and relaxes DNA to allow access to genes for transcription or translation. Targeting topoisomerase IV inhibits DNA synthesis, and may also lead to double-stranded cell breaks. http://purl.obolibrary.org/obo/ARO_3003258 Antibiotic sensitive DNA topoisomerase subunit parY http://purl.obolibrary.org/obo/ARO_3000766 antibiotic sensitive topoisomerase subunit parY is a subunit of the topoisomerase IV. It decatenates and relaxes DNA to allow for transcription or translation. http://purl.obolibrary.org/obo/ARO_3003259 antibiotic sensitive DNA topoisomerase subunit parE http://purl.obolibrary.org/obo/ARO_3000766 antibiotic sensitive topoisomerase subunit ParE is a subunit of topoisomerase IV, which decatenates and relaxes DNA to allow access to genes for transcription or translation. Targeting topoisomerase IV inhibits DNA synthesis, and may also lead to double-stranded cell breaks. http://purl.obolibrary.org/obo/ARO_3003260 aminocoumarin sensitive gyrB http://purl.obolibrary.org/obo/ARO_3000734 antibiotic sensitive DNA topoisomerase subunit gyrB Beta-subunit of DNA gyrase sensitive to inhibition by aminocoumarins. http://purl.obolibrary.org/obo/ARO_3003261 fluoroquinolone sensitive gyrB http://purl.obolibrary.org/obo/ARO_3000734 antibiotic sensitive DNA topoisomerase subunit gyrB Beta-subunit of DNA gyrase sensitive to inhibition by fluoroquinolones. http://purl.obolibrary.org/obo/ARO_3003262 Antibiotic sensitive Escherichia coli 16S rRNA http://purl.obolibrary.org/obo/ARO_3000755 antibiotic sensitive 16S rRNA Sensitive form of 16s susceptable to antibiotics. http://purl.obolibrary.org/obo/ARO_3003263 Antibiotic sensitive Mycobacteroides abscessus 16S rRNA http://purl.obolibrary.org/obo/ARO_3000755 antibiotic sensitive 16S rRNA Sensitive form of 16s susceptible to antibiotics. http://purl.obolibrary.org/obo/ARO_3003264 Aminoglycosides sensitive Mycobacteroides abscessus 16S rRNA http://purl.obolibrary.org/obo/ARO_3003263 Antibiotic sensitive Mycobacteroides abscessus 16S rRNA Sensitive form of 16s susceptible to antibiotics. http://purl.obolibrary.org/obo/ARO_3003265 Amikacin sensitive Mycobacteroides abscessus 16S rRNA mutation http://purl.obolibrary.org/obo/ARO_3003264 Aminoglycosides sensitive Mycobacteroides abscessus 16S rRNA Sensitive form of 16s susceptible to antibiotics. http://purl.obolibrary.org/obo/ARO_3003272 daptomycin resistant cls http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Cardiolipin synthetase catalyzes the formation of cardiolipin from two phosphatidylglycerol molecules. Cardiolipin is important in membrane translocation and permeabilization. Current known mutations on the enzyme confer resistance to daptomycin. http://purl.obolibrary.org/obo/ARO_3003273 cell membrane component enzymes targeted by antibiotic http://purl.obolibrary.org/obo/ARO_3000708 antibiotic target Interaction with the cell membrane phospholipids interferes with membrane permeability and integrity, leading to the leakage of cell contents. The outer membrane of Gram-negative bacteria is particularly sensitive. http://purl.obolibrary.org/obo/ARO_3003274 antibiotic sensitive cls http://purl.obolibrary.org/obo/ARO_3003273 cell membrane component enzymes targeted by antibiotic Cardiolipin synthetase catalyzes the formation of cardiolipin from two phosphatidylglycerol molecules. Cardiolipin is important in membrane translocation and permeabilization. The inactivation of this enzyme by antibiotics leads to cell death. http://purl.obolibrary.org/obo/ARO_3003275 Daptomycin sensitive cardiolipin synthetase http://purl.obolibrary.org/obo/ARO_3003274 antibiotic sensitive cls Cardiolipin synthetase catalyzes the formation of cardiolipin from two phosphatidylglycerol molecules. Cardiolipin is important in membrane translocation and permeabilization. Mutations on the enzyme confers resistance to Daptomycin. http://purl.obolibrary.org/obo/ARO_3003276 antibiotic resistant rpoB http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant RNA polymerase is a multisubunit enzyme that is necessary for transcription. The beta-subunit of RNA polymerase forms the active center of the enzyme and template/transcript binding sites. Mutations in rpoB gene confers antibiotic resistance. http://purl.obolibrary.org/obo/ARO_3003277 antibiotic sensitive beta-subunit of RNA polymerase (rpoB) http://purl.obolibrary.org/obo/ARO_3000712 nucleic acid synthesis machinery targeted by antibiotic RNA polymerase is a multisubunit enzyme that is necessary for transcription. The beta-subunit of RNA polymerase forms the active center of the enzyme and template/transcript binding sites. This enzyme can be inactivated by antibiotics leading to cell death. http://purl.obolibrary.org/obo/ARO_3003278 daptomycin sensitive beta-subunit of RNA polymerase (rpoB) http://purl.obolibrary.org/obo/ARO_3003277 antibiotic sensitive beta-subunit of RNA polymerase (rpoB) Daptomycin binds to the cytoplasmic membrane of Gram-positive. It's lipopeptide tail servers as a ion channel for potassium. This causes a rapid depolarization that result in failures in DNA/RNA/Protein synthesis. Eventually cell death. http://purl.obolibrary.org/obo/ARO_3003279 antibiotic resistant liaFSR system http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant The liaFSR system regulates the cell envelope stress response. It is transcriptionally activated by exposure to alkaline shock, detergents, and particularly antibiotics with lipid II inhibition properties. http://purl.obolibrary.org/obo/ARO_3003280 antibiotic sensitive mprF http://purl.obolibrary.org/obo/ARO_3003273 cell membrane component enzymes targeted by antibiotic MprF is a integral membrane protein that modifies the negatively-charged phosphatidylglycerol on the membrane surface of both Gram-positive and Gram-negative bacteria. This confers resistance to cationic peptides that disrupt the cell membrane, including defensins. Mutations in this enzyme can confer additional resistances. http://purl.obolibrary.org/obo/ARO_3003281 antibiotic sensitive pgsA http://purl.obolibrary.org/obo/ARO_3003273 cell membrane component enzymes targeted by antibiotic pgsA or phosphatidylglycerophosphate synthetase is an integral membrane protein involved in phospholipid biosynthesis. Inhibition of this enzyme leads to cell death via the inability to form the plasma membrane. http://purl.obolibrary.org/obo/ARO_3003283 Mycobacterium tuberculosis rpoB with mutations conferring resistance to rifampicin http://purl.obolibrary.org/obo/ARO_3000210 rifamycin-resistant beta-subunit of RNA polymerase (rpoB) Point mutations that occurs in Mycobacterium tuberculosis rpoB resulting in resistance to rifampicin. http://purl.obolibrary.org/obo/ARO_3003284 Mycobacterium leprae rpoB mutations conferring resistance to rifampicin http://purl.obolibrary.org/obo/ARO_3000210 rifamycin-resistant beta-subunit of RNA polymerase (rpoB) Point mutations that occurs in Mycobacterium leprae rpoB resulting in resistance to rifampicin. http://purl.obolibrary.org/obo/ARO_3003285 Staphylococcus aureus rpoB mutants conferring resistance to rifampicin http://purl.obolibrary.org/obo/ARO_3000210 rifamycin-resistant beta-subunit of RNA polymerase (rpoB) Point mutations that occurs in Staphylococcus aureus rpoB resulting in resistance to rifampicin. http://purl.obolibrary.org/obo/ARO_3003287 Staphylococcus aureus rpoB mutants conferring resistance to daptomycin http://purl.obolibrary.org/obo/ARO_3003090 daptomycin-resistant beta-subunit of RNA polymerase (rpoB) Point mutations that occurs in Staphylococcus aureus rpoB resulting in resistance to daptomycin. http://purl.obolibrary.org/obo/ARO_3003288 Escherichia coli rpoB mutants conferring resistance to rifampicin http://purl.obolibrary.org/obo/ARO_3000210 rifamycin-resistant beta-subunit of RNA polymerase (rpoB) Point mutations that occurs in Escherichia coli rpoB resulting in resistance to rifampicin. http://purl.obolibrary.org/obo/ARO_3003289 antibiotic resistant rpoC http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant RNA polymerase is a multisubunit enzyme that is necessary for transcription. The beta prime subunit of RNA polymerase forms the active center of the enzyme and template/transcript binding sites. Mutations in rpoC gene confers antibiotic resistance. http://purl.obolibrary.org/obo/ARO_3003290 daptomycin-resistant beta prime subunit of RNA polymerase (rpoC) http://purl.obolibrary.org/obo/ARO_3003289 antibiotic resistant rpoC Daptomycin resistant RNA polymerases include amino acids substitutions which alter the binding affinity of daptomycin to the protein, resulting in antibiotic resistance. http://purl.obolibrary.org/obo/ARO_3003291 Staphylococcus aureus rpoC conferring resistance to daptomycin http://purl.obolibrary.org/obo/ARO_3003290 daptomycin-resistant beta prime subunit of RNA polymerase (rpoC) Point mutations that occurs in Staphylococcus aureus rpoC resulting in resistance to daptomycin. http://purl.obolibrary.org/obo/ARO_3003292 fluoroquinolone resistant gyrA http://purl.obolibrary.org/obo/ARO_3000452 fluoroquinolone resistant DNA topoisomerase DNA gyrase is responsible for DNA supercoiling and consists of two alpha and two beta subunits. GyrA point mutations confer resistance by preventing fluoroquinolone antibiotics from binding the alpha-subunit. http://purl.obolibrary.org/obo/ARO_3003294 Escherichia coli gyrA conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3003292 fluoroquinolone resistant gyrA Point mutation of Escherichia coli gyrA resulted in the lowered affinity between fluoroquinolones and gyrA. Thus, conferring resistance. http://purl.obolibrary.org/obo/ARO_3003295 Mycobacterium tuberculosis gyrA conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3003292 fluoroquinolone resistant gyrA Point mutation of Mycobacterium tuberculosis gyrA resulted in the lowered affinity between fluoroquinolones and gyrA. Thus, conferring resistance. http://purl.obolibrary.org/obo/ARO_3003296 Staphylococcus aureus gyrA conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3003292 fluoroquinolone resistant gyrA Point mutation of Staphylococcus aureus gyrA resulted in the lowered affinity between fluoroquinolones and gyrA. Thus, conferring resistance. http://purl.obolibrary.org/obo/ARO_3003297 Bartonella bacilliformis gyrA conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3003292 fluoroquinolone resistant gyrA Point mutation of Bartonella bacilliformis gyrA resulted in the lowered affinity between fluoroquinolones and gyrA. Thus, conferring resistance. http://purl.obolibrary.org/obo/ARO_3003298 Mycobacterium leprae gyrA conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3003292 fluoroquinolone resistant gyrA Point mutation of Mycobacterium leprae gyrA resulted in the lowered affinity between fluoroquinolones and gyrA. Thus, conferring resistance. http://purl.obolibrary.org/obo/ARO_3003301 Staphylococcus aureus gyrB conferring resistance to aminocoumarin http://purl.obolibrary.org/obo/ARO_3000479 aminocoumarin resistant gyrB Point mutation in Staphylococcus aureus resulting in aminocoumarin resistance. http://purl.obolibrary.org/obo/ARO_3003302 Bartonella bacilliformis gyrB conferring resistance to aminocoumarin http://purl.obolibrary.org/obo/ARO_3000479 aminocoumarin resistant gyrB Point mutation in Bartonella bacilliformis resulting in aminocoumarin resistance. http://purl.obolibrary.org/obo/ARO_3003303 Escherichia coli gyrB conferring resistance to aminocoumarin http://purl.obolibrary.org/obo/ARO_3000479 aminocoumarin resistant gyrB Point mutation in Escherichia coli resulting in aminocoumarin resistance. http://purl.obolibrary.org/obo/ARO_3003304 Mycobacterium leprae gyrB conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3000864 fluoroquinolone resistant gyrB Point mutation in Mycobacterium leprae gyrB resulting in fluoroquinolone resistance. http://purl.obolibrary.org/obo/ARO_3003305 Ureaplasma urealyticum gyrB conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3000864 fluoroquinolone resistant gyrB Point mutation in Ureaplasma urealyticum resulting in fluoroquinolone resistance. http://purl.obolibrary.org/obo/ARO_3003306 Morganella morganii gyrB conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3000864 fluoroquinolone resistant gyrB Point mutation in Morganella morganii resulting in fluoroquinolone resistance. http://purl.obolibrary.org/obo/ARO_3003307 Salmonella serovars gyrB conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3000864 fluoroquinolone resistant gyrB Point mutation in Salmonella serovars resulting in fluoroquinolone resistance. http://purl.obolibrary.org/obo/ARO_3003308 Escherichia coli parC conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3000619 fluoroquinolone resistant parC Point mutation in Escherichia coli parC resulting in fluoroquinolone resistance. http://purl.obolibrary.org/obo/ARO_3003309 Ureaplasma urealyticum parC conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3000619 fluoroquinolone resistant parC Point mutation in Ureaplasma urealyticum parC resulting in fluoroquinolone resistance. http://purl.obolibrary.org/obo/ARO_3003310 Mycoplasma hominis parC conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3000619 fluoroquinolone resistant parC Point mutation in Mycoplasma hominis parC resulting in fluoroquinolone resistance. http://purl.obolibrary.org/obo/ARO_3003311 Streptococcus pneumoniae parC conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3000619 fluoroquinolone resistant parC Point mutation in Streptococcus pneumoniae parC resulting in fluoroquinolone resistance. http://purl.obolibrary.org/obo/ARO_3003312 Staphylococcus aureus parC conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3000619 fluoroquinolone resistant parC Point mutation in Staphylococcus aureus parC resulting in fluoroquinolone resistance. http://purl.obolibrary.org/obo/ARO_3003313 fluoroquinolone resistant parE http://purl.obolibrary.org/obo/ARO_3000452 fluoroquinolone resistant DNA topoisomerase ParE is a subunit of topoisomerase IV, necessary for cell survival. Point mutations in ParE prevent fluoroquinolones from inhibiting DNA synthesis, thus conferring resistance. http://purl.obolibrary.org/obo/ARO_3003314 Staphylococcus aureus parE conferring resistance to aminocoumarin http://purl.obolibrary.org/obo/ARO_3000457 aminocoumarin resistant parE Point mutation in Staphylococcus aureus parE resulting in aminocoumarin resistance. http://purl.obolibrary.org/obo/ARO_3003315 Staphylococcus aureus parE conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3003313 fluoroquinolone resistant parE Point mutation in Staphylococcus aureus parE resulting in fluoroquinolones resistance. http://purl.obolibrary.org/obo/ARO_3003316 Escherichia coli parE conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3003313 fluoroquinolone resistant parE Point mutation in Escherichia coli parE resulting in fluoroquinolones resistance. http://purl.obolibrary.org/obo/ARO_3003317 Salmonella serovars parE conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3003313 fluoroquinolone resistant parE Point mutation in Salmonella serovars parE resulting in fluoroquinolones resistance. http://purl.obolibrary.org/obo/ARO_3003318 Streptomyces rishiriensis parY mutant conferring resistance to aminocoumarin http://purl.obolibrary.org/obo/ARO_3000480 aminocoumarin resistant parY Intrinsically aminocoumarin-resistant parY variant found in Streptomyces, an aminocoumarin-producing genus. http://purl.obolibrary.org/obo/ARO_3003319 Staphylococcus aureus mprF with mutation conferring resistance to daptomycin http://purl.obolibrary.org/obo/ARO_3003091 daptomycin resistant mprF Point mutations that occur within Staphylococcus aureus mprF gene resulting in resistance to daptomycin. http://purl.obolibrary.org/obo/ARO_3003323 Staphylococcus aureus pgsA mutations conferring resistance to daptomycin http://purl.obolibrary.org/obo/ARO_3003080 daptomycin resistant pgsA Point mutations that occur within Staphylococcus aureus pgsA gene resulting in resistance to daptomycin. http://purl.obolibrary.org/obo/ARO_3003324 Bacillus subtilis mprF http://purl.obolibrary.org/obo/ARO_3000863 defensin resistant mprF MprF is a integral membrane protein that modifies the negatively-charged phosphatidylglycerol on the membrane surface. This confers resistance to cationic peptides that disrupt the cell membrane, including defensins. Additionally, large-scale mutations causing loss of function of the gene result in increased susceptibility to daptomycin. http://purl.obolibrary.org/obo/ARO_3003325 Mycobacterium tuberculosis variant bovis embB with mutation conferring resistance to ethambutol http://purl.obolibrary.org/obo/ARO_3000235 ethambutol resistant embB Point mutations that occur within Mycobacterium tuberculosis variant bovis embB gene resulting in resistance to ethambutol. http://purl.obolibrary.org/obo/ARO_3003326 Mycobacterium tuberculosis embB mutant conferring resistance to ethambutol http://purl.obolibrary.org/obo/ARO_3000235 ethambutol resistant embB Point mutations that occur within Mycobacterium tuberculosis embB gene resulting in resistance to ethambutol. http://purl.obolibrary.org/obo/ARO_3003327 Mycobacterium tuberculosis embC mutant conferring resistance to ethambutol http://purl.obolibrary.org/obo/ARO_3002706 ethambutol resistant embC Point mutations in Mycobacterium tuberculosis embC that result in lower affinity between ethambutol and EmbC, resulting in resistance. http://purl.obolibrary.org/obo/ARO_3003333 Escherichia coli 16S rRNA (rrsC) mutation conferring resistance to kasugamicin http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in the 3' minor, 3' major, and central domains in the rrsC 16S rRNA gene of Escherichia coli can confer resistance to kasugamicin. http://purl.obolibrary.org/obo/ARO_3003356 Antibiotic resistant EF-Tu http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Sequence variants of elongation factor Tu that confer resistance to different classes of antibiotics. http://purl.obolibrary.org/obo/ARO_3003357 Clostridioides difficile EF-Tu mutants conferring resistance to elfamycin http://purl.obolibrary.org/obo/ARO_3001312 elfamycin resistant EF-Tu Sequence variants of Clostridioides difficile elongation factor Tu that confer resistance to elfamycin antibiotics. http://purl.obolibrary.org/obo/ARO_3003358 Escherichia coli EF-Tu mutants conferring resistance to elfamycin http://purl.obolibrary.org/obo/ARO_3001312 elfamycin resistant EF-Tu Sequence variants of Escherichia coli elongation factor Tu that confer resistance to elfamycin antibiotics. http://purl.obolibrary.org/obo/ARO_3003359 Streptomyces cinnamoneus EF-Tu mutants conferring resistance to elfamycin http://purl.obolibrary.org/obo/ARO_3001312 elfamycin resistant EF-Tu Sequence variants of Streptomyces cinnamoneus elongation factor Tu that confer resistance to elfamycin antibiotics. http://purl.obolibrary.org/obo/ARO_3003360 Planobispora rosea EF-Tu mutants conferring resistance to elfamycin http://purl.obolibrary.org/obo/ARO_3001312 elfamycin resistant EF-Tu Sequence variants of Planobispora rosea elongation factor Tu that confer resistance to elfamycin antibiotics. http://purl.obolibrary.org/obo/ARO_3003361 Planobispora rosea EF-Tu mutants conferring resistance to inhibitor GE2270A http://purl.obolibrary.org/obo/ARO_3003360 Planobispora rosea EF-Tu mutants conferring resistance to elfamycin Sequence variants of Planobispora rosea elongation factor Tu that confer resistance to inhibitor GE2270A. http://purl.obolibrary.org/obo/ARO_3003368 Escherichia coli EF-Tu mutants conferring resistance to kirromycin http://purl.obolibrary.org/obo/ARO_3003358 Escherichia coli EF-Tu mutants conferring resistance to elfamycin Sequence variants of Escherichia coli elongation factor Tu that confer resistance to kirromycin. http://purl.obolibrary.org/obo/ARO_3003369 Escherichia coli EF-Tu mutants conferring resistance to Pulvomycin http://purl.obolibrary.org/obo/ARO_3003358 Escherichia coli EF-Tu mutants conferring resistance to elfamycin Sequence variants of Escherichia coli elongation factor Tu that confer resistance to Pulvomycin. http://purl.obolibrary.org/obo/ARO_3003370 Escherichia coli EF-Tu mutants conferring resistance to Enacyloxin IIa http://purl.obolibrary.org/obo/ARO_3003358 Escherichia coli EF-Tu mutants conferring resistance to elfamycin Sequence variants of Escherichia coli elongation factor Tu that confer resistance to Enacyloxin IIa. http://purl.obolibrary.org/obo/ARO_3003372 Escherichia coli 16S rRNA (rrsH) mutation conferring resistance to spectinomycin http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in the 3' major domain of the rrsH 16S rRNA gene of Escherichia coli can confer resistance to spectinomycin. http://purl.obolibrary.org/obo/ARO_3003373 Klebsiella pneumoniae acrR with mutation conferring multidrug antibiotic resistance http://purl.obolibrary.org/obo/ARO_3000702 acrR AcrR is a repressor of the AcrAB-TolC multidrug efflux complex. AcrR mutations result in high level antibiotic resistance. http://purl.obolibrary.org/obo/ARO_3003374 Enterobacter aerogenes acrR with mutation conferring multidrug antibiotic resistance http://purl.obolibrary.org/obo/ARO_3000702 acrR AcrR is a repressor of the AcrAB-TolC multidrug efflux complex. AcrR mutations result in high level antibiotic resistance. http://purl.obolibrary.org/obo/ARO_3003376 Escherichia coli 16S rRNA (rrsB) mutation conferring resistance to spectinomycin http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in the 3' major domain of the rrsB 16S rRNA gene of Escherichia coli can confer resistance to spectinomycin. http://purl.obolibrary.org/obo/ARO_3003377 Escherichia coli 16S rRNA (rrnB) mutation conferring resistance to spectinomycin http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in the 3' major domain of helix 35, in the rrnB gene operon for 16S rRNA of Escherichia coli can confer resistance to spectinomycin. http://purl.obolibrary.org/obo/ARO_3003378 Escherichia coli AcrAB-TolC with MarR mutations conferring resistance to ciprofloxacin and tetracycline http://purl.obolibrary.org/obo/ARO_3000718 marR MarR is a repressor of the mar operon marRAB, thus regulating the expression of marA, the activator of multidrug efflux pump AcrAB. http://purl.obolibrary.org/obo/ARO_3003379 Salmonella enterica ramR mutants http://purl.obolibrary.org/obo/ARO_3000824 ramR RamR is a repressor that regulates RamA expression. Mutations lead to the upregulation of AcrAB, which is positively regulated by RamA. http://purl.obolibrary.org/obo/ARO_3003380 Klebsiella pneumoniae ramR mutants http://purl.obolibrary.org/obo/ARO_3000824 ramR RamR is a repressor that regulates RamA expression. Mutations lead to the upregulation of AcrAB, which is positively regulated by RamA. http://purl.obolibrary.org/obo/ARO_3003381 Escherichia coli soxR with mutation conferring antibiotic resistance http://purl.obolibrary.org/obo/ARO_3000836 soxR SoxR is a sensory protein that upregulates soxS expression in the presence of redox-cycling drugs. This stress response leads to the expression many multidrug efflux pumps. http://purl.obolibrary.org/obo/ARO_3003382 Salmonella enterica soxR with mutation conferring antibiotic resistance http://purl.obolibrary.org/obo/ARO_3000836 soxR SoxR is a sensory protein that upregulates soxS expression in the presence of redox-cycling drugs. This stress response leads to the expression of many multidrug efflux pumps. http://purl.obolibrary.org/obo/ARO_3003383 Salmonella serovars soxS with mutation conferring antibiotic resistance http://purl.obolibrary.org/obo/ARO_3000837 soxS SoxS is a global regulator that up-regulates the expression of AcrAB efflux genes. It also reduces OmpF expression to decrease cell membrane permeability. http://purl.obolibrary.org/obo/ARO_3003385 Klebsiella aerogenes Omp36 http://purl.obolibrary.org/obo/ARO_3004281 General Bacterial Porin with reduced permeability to beta-lactams Mutant forms of the porin Omp36 result in reduced permeability to antibiotics. http://purl.obolibrary.org/obo/ARO_3003386 Escherichia coli folP with mutation conferring resistance to sulfonamides http://purl.obolibrary.org/obo/ARO_3003415 sulfonamide resistant dihydropteroate synthase folP Point mutations in Escherichia coli dihydropteroate synthase folP prevent sulfonamide antibiotics from inhibiting its role in folate synthesis, thus conferring sulfonamide resistance. http://purl.obolibrary.org/obo/ARO_3003387 Streptococcus pyogenes folP with mutation conferring resistance to sulfonamides http://purl.obolibrary.org/obo/ARO_3003415 sulfonamide resistant dihydropteroate synthase folP Point mutations in Streptococcus pyogenes dihydropteroate synthase folP prevent sulfonamide antibiotics from inhibiting its role in folate synthesis, thus conferring sulfonamide resistance. http://purl.obolibrary.org/obo/ARO_3003388 dapsone resistant dihydropteroate synthase folP http://purl.obolibrary.org/obo/ARO_3000226 antibiotic resistant folP Dapsone inhibits bacterial synthesis of dihydrofolic acid by competing with with para-aminobenzoate for the active site of dihydropteroate synthetase. Thus acts as a competitive inhibitor of folP. Point mutation within the folP gene results in lowered affinity of dapsone for folP. http://purl.obolibrary.org/obo/ARO_3003389 Mycobacterium leprae folP with mutation conferring resistance to dapsone http://purl.obolibrary.org/obo/ARO_3003388 dapsone resistant dihydropteroate synthase folP Dapsone inhibits bacterial synthesis of dihydrofolic acid by competing with with para-aminobenzoate for the active site of dihydropteroate synthetase. Point mutation within the Mycobacterium leprae folP gene results in lowered affinity of dapsone for folP. http://purl.obolibrary.org/obo/ARO_3003390 Escherichia coli ompF with mutation conferring resistance to beta-lactam antibiotics http://purl.obolibrary.org/obo/ARO_3000265 porin OmpF The Escherichia coli ompF (oprF) is a nonspecific porin channel involved in the membrane translocation of small hydrophilic molecules, including and especially beta-lactam antibiotics. Mutations in ompF can decrease diffusion of antibiotics across the cellular membrane, thereby decreasing overall susceptibility through absence of porin function. http://purl.obolibrary.org/obo/ARO_3003392 Mycobacterium tuberculosis katG mutations conferring resistance to isoniazid http://purl.obolibrary.org/obo/ARO_3003416 isoniazid resistant katG katG is a catalase-peroxidase that catalyzes the activation of isoniazid. Isoniazid inhibits mycolic acid synthesis, which prevents cell wall synthesis in mycobacteria. Mutations in katG results in inability to activate isoniazid. Over 280 different mutations have been documented in PubMed for katG, with mutations to Ser315 being the most prevalent. http://purl.obolibrary.org/obo/ARO_3003393 Mycobacterium tuberculosis inhA mutations conferring resistance to isoniazid http://purl.obolibrary.org/obo/ARO_3004874 isoniazid resistant inhA inhA is a enoyl-acyl carrier reductase used in lipid metabolism and farry acid biosynthesis. It is inhibited by isoniazid. mutations in the promoter region or multiple copies of the inhA shows marked resistance to isoniazid mediated inhibition of mycolic acid biosynthesis. http://purl.obolibrary.org/obo/ARO_3003394 Mycobacterium tuberculosis pncA mutations conferring resistance to pyrazinamide http://purl.obolibrary.org/obo/ARO_3003418 Pyrazinamide resistant pncA pncA is a pyrazinamidase/nicotinamidase. It catalyzes the activation of pyrazinamide. Some mutation within pncA are associated with loss of enzyme activity, resulting in pyrazinamide resistance. http://purl.obolibrary.org/obo/ARO_3003395 Mycobacterium tuberculosis rpsL mutations conferring resistance to Streptomycin http://purl.obolibrary.org/obo/ARO_3003419 antibiotic-resistant rpsL Ribosomal protein S12 stabilizes the highly conserved pseudoknot structure formed by 16S rRNA. Amino acid substitutions in RpsL affect the higher-order structure of 16S rRNA and confer streptomycin resistance by disrupting interactions between 16S rRNA and streptomycin. http://purl.obolibrary.org/obo/ARO_3003396 Escherichia coli 16S rRNA (rrsB) mutation conferring resistance to gentamicin C http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in the 3' minor domain of helix 44, in the rrsB 16S rRNA gene of Escherichia coli can confer resistance to gentamicin C. http://purl.obolibrary.org/obo/ARO_3003397 Escherichia coli 16S rRNA (rrsB) mutation conferring resistance to G418 http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in the 3' minor domain of helix 44, in the rrsB 16S rRNA gene of Escherichia coli can confer resistance to G418. http://purl.obolibrary.org/obo/ARO_3003398 undecaprenyl pyrophosphate related proteins http://purl.obolibrary.org/obo/ARO_3000012 protein(s) conferring antibiotic resistance via molecular bypass Undecaprenyl phosphate is a universal lipid carrier of glycan biosynthetic intermediates for carbohydrate polymers that are exported to the bacterial cell envelope. Antibiotics that targets this compound or proteins associated with the production of this compound leads to cell death. http://purl.obolibrary.org/obo/ARO_3003399 Escherichia coli 16S rRNA (rrsB) mutation conferring resistance to kanamycin A http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in the 3' minor domain of helix 44, in the rrsB 16S rRNA gene of Escherichia coli can confer resistance to kanamycin A. http://purl.obolibrary.org/obo/ARO_3003401 sulfone antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule A sulfone active against a wide range of bacteria but mainly employed for its actions against mycobacterium laprae. Its mechanism of action involves inhibition of folic acid synthesis in susceptible organisms. http://purl.obolibrary.org/obo/ARO_3003402 Escherichia coli 16S rRNA (rrsB) mutation conferring resistance to neomycin http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in the 3' minor domain of helix 44, in the rrsB 16S rRNA gene of Escherichia coli can confer resistance to neomycin. http://purl.obolibrary.org/obo/ARO_3003403 Escherichia coli 16S rRNA (rrsB) mutation conferring resistance to paromomycin http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in the 3' minor domain of helix 44, in the rrsB 16S rRNA gene of Escherichia coli can confer resistance to paromomycin. http://purl.obolibrary.org/obo/ARO_3003405 Escherichia coli 16S rRNA (rrsB) mutation conferring resistance to streptomycin http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in the 5' domain of helix 18, in the rrsB 16S rRNA gene of Escherichia coli can confer resistance to streptomycin. http://purl.obolibrary.org/obo/ARO_3003406 Escherichia coli 16S rRNA (rrnB) mutation conferring resistance to streptomycin http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in the 5' domain of helix 18, in the rrnB 16S rRNA gene of Escherichia coli can confer resistance to streptomycin. http://purl.obolibrary.org/obo/ARO_3003408 Escherichia coli 16S rRNA (rrsB) mutation conferring resistance to tobramycin http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in the 3' minor domain of the rrnB 16S rRNA gene of Escherichia coli can confer resistance to tobramycin. http://purl.obolibrary.org/obo/ARO_3003410 Escherichia coli 16S rRNA (rrsB) mutation conferring resistance to tetracycline http://purl.obolibrary.org/obo/ARO_3003669 16S rRNA with mutation conferring resistance to tetracycline derivatives Point mutations in the 3' major domain of the rrsB 16S rRNA gene of Escherichia coli can confer resistance to tetracycline. http://purl.obolibrary.org/obo/ARO_3003411 Escherichia coli 16S rRNA (rrnB) mutation conferring resistance to tetracycline http://purl.obolibrary.org/obo/ARO_3003669 16S rRNA with mutation conferring resistance to tetracycline derivatives Point mutations in the 3' major domain of the rrnB 16S rRNA gene of Escherichia coli can confer resistance to tetracycline. http://purl.obolibrary.org/obo/ARO_3003412 dapsone http://purl.obolibrary.org/obo/ARO_3003401 sulfone antibiotic Dapsone is a sulfone in which it inhibits folic acid synthesis, such as the dihydropteroate synthase. http://purl.obolibrary.org/obo/ARO_3003413 pyrazinamide http://purl.obolibrary.org/obo/ARO_3007155 pyrazine antibiotic Pyrazinamide is an antimycobacterial. It is highly specific and active only against Mycobacterium tuberculosis. This compound is a prodrug and needs to be activated inside the cell. It interferes with the bacterium's ability to synthesize new fatty acids, causing cell death. http://purl.obolibrary.org/obo/ARO_3003414 LFF571 http://purl.obolibrary.org/obo/ARO_3001309 cyclic thiazolyl peptide elfamycin LFF571 is a novel semi-synthetic thiopeptide antibiotic derived from GE2270. It has been shown to possess potent in vitro and in vivo activity against Gram-positive bacteria. It is hypothesized that it a translation inhibitor leading to cell death. http://purl.obolibrary.org/obo/ARO_3003415 sulfonamide resistant dihydropteroate synthase folP http://purl.obolibrary.org/obo/ARO_3000226 antibiotic resistant folP Point mutations in dihydropteroate synthase folP prevent sulfonamide antibiotics from inhibiting its role in folate synthesis, thus conferring sulfonamide resistance. http://purl.obolibrary.org/obo/ARO_3003416 isoniazid resistant katG http://purl.obolibrary.org/obo/ARO_3004266 antibiotic resistant katG Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. It is a catalase-peroxidases that catalyzes the activation of isoniazid. Mutations that arises within this protein cause changes that results in the inability for katG to activate antibiotics, conferring resistance. http://purl.obolibrary.org/obo/ARO_3003417 antibiotic resistant inhA http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant inhA is a enoyl-acyl carrier reductase used in lipid metabolism and fatty acid biosynthesis. It is inhibited by isoniazid. Mutations in the promoter region or multiple copies of the inhA shows marked resistance to isoniazid mediated inhibition of mycolic acid biosynthesis. http://purl.obolibrary.org/obo/ARO_3003418 Pyrazinamide resistant pncA http://purl.obolibrary.org/obo/ARO_3004267 antibiotic resistant pncA pncA is a pyrazinamidase/nicotinamidase. It catalyzes the activation of pyrazinamide to pyrazinoic acid. Mutations arise within the pncA gene that caused the loss of pyrazinamidase activity is the major mechanism of antibiotic resistance. http://purl.obolibrary.org/obo/ARO_3003419 antibiotic-resistant rpsL http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Ribosomal protein S12 stabilizes the highly conserved pseudoknot structure formed by 16S rRNA. Amino acid substitutions in RpsL affect the higher-order structure of 16S rRNA and confer antibiotic resistance. http://purl.obolibrary.org/obo/ARO_3003420 antibiotic resistant pgsA http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant pgsA or phosphatidylglycerophosphate synthetase is an integral membrane protein involved in phospholipid biosynthesis. It is a CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase. http://purl.obolibrary.org/obo/ARO_3003421 antibiotic resistant mprF http://purl.obolibrary.org/obo/ARO_3003580 gene altering cell wall charge Catalyzes the transfer of a lysyl group from L-lysyl-tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), a major component of the bacterial membrane with a positive net charge. LPG synthesis contributes to bacterial virulence as it is involved in the resistance mechanism against cationic antimicrobial peptides (CAMP) produces by the host's immune system (defensins, cathelicidins) and by the competing microorganisms (bacteriocins). http://purl.obolibrary.org/obo/ARO_3003422 antibiotic resistant aftA http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Arabinofuranosyltransferase is involved in the biosynthesis of the arabinogalactan region of the mAGP complex, an essential component of the mycobacterial cell wall. http://purl.obolibrary.org/obo/ARO_3003425 antibiotic resistant dihydrofolate reductase http://purl.obolibrary.org/obo/ARO_3000381 antibiotic target replacement protein Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. http://purl.obolibrary.org/obo/ARO_3003426 antibiotic sensitive inhA http://purl.obolibrary.org/obo/ARO_3000872 antibiotic sensitive enoyl-acyl carrier reductase inhA is a enoyl-acyl carrier reductase used in lipid metabolism and fatty acid biosynthesis. http://purl.obolibrary.org/obo/ARO_3003428 porin proteins permeable to antibiotics http://purl.obolibrary.org/obo/ARO_3000708 antibiotic target Porin proteins permeable to antibiotics. http://purl.obolibrary.org/obo/ARO_3003429 antibiotic sensitive beta-prime subunit of RNA polymerase (rpoC) http://purl.obolibrary.org/obo/ARO_3000712 nucleic acid synthesis machinery targeted by antibiotic RNA polymerase is a multisubunit enzyme that is necessary for transcription. The beta-prime subunit of RNA polymerase forms the active center of the enzyme and template/transcript binding sites. This enzyme can be inactivated by antibiotics leading to cell death. http://purl.obolibrary.org/obo/ARO_3003430 fluoroquinolone sensitive parE http://purl.obolibrary.org/obo/ARO_3003259 antibiotic sensitive DNA topoisomerase subunit parE ParE is a subunit of topoisomerase IV, necessary for cell survival. Point mutations in ParE prevent fluoroquinolones from inhibiting DNA synthesis, thus conferring resistance. http://purl.obolibrary.org/obo/ARO_3003431 antibiotic sensitive Ribosomal protein S12 (rpsL) http://purl.obolibrary.org/obo/ARO_3000711 protein synthesis machinery targeted by antibiotic Ribosomal protein S12 stabilizes the highly conserved pseudoknot structure formed by 16S rRNA. It is targeted and inhibited by streptomycin. http://purl.obolibrary.org/obo/ARO_3003436 Mycobacterium tuberculosis 16S rRNA mutation conferring resistance to kanamycin http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in the 3' domain of 16S rRNA of Mycobacterium tuberculosis can confer resistance to kanamycin. http://purl.obolibrary.org/obo/ARO_3003437 Mycobacterium tuberculosis 16S rRNA mutation conferring resistance to viomycin http://purl.obolibrary.org/obo/ARO_3003667 16s rRNA with mutation conferring resistance to peptide antibiotics Peptide antibiotics inhibit protein synthesis. Resistance to viomycin can be caused by an altered RNA molecule in the 16S ribosomal subunit. http://purl.obolibrary.org/obo/ARO_3003438 Enterococcus faecium EF-Tu mutants conferring resistance to GE2270A http://purl.obolibrary.org/obo/ARO_3003875 Enterococcus faecium EF-Tu mutants conferring resistance to elfamycin Sequence variants of Enterococcus faecium elongation factor Tu that confer resistance to GE2270A. http://purl.obolibrary.org/obo/ARO_3003439 antibiotic sensitive RNA polymerase switch region http://purl.obolibrary.org/obo/ARO_3000712 nucleic acid synthesis machinery targeted by antibiotic The switch region is a structural element that mediates conformational changes and contacts required for RNAP to load DNA into the RNAP active-center cleft during transcription initiation. The switch region is located at the base of the RNAP clamp and serves as the hinge that mediates opening of the RNAP clamp to load DNA into the RNAP active-center cleft and mediates closing of the RNAP clamp to retain DNA in the RNAP active-center cleft. http://purl.obolibrary.org/obo/ARO_3003440 mecB http://purl.obolibrary.org/obo/ARO_3001208 methicillin resistant PBP2 A foreign PBP2 acquired by lateral gene transfer that able to perform peptidoglycan synthesis in the presence of beta-lactams. http://purl.obolibrary.org/obo/ARO_3003441 cfrA http://purl.obolibrary.org/obo/ARO_3004607 Cfr Group CfrA is a chloramphenicol-florfenicol resistance gene and methyltransferase enzyme. Methylation of position 8 of A2503 in 23S rRNA confers resistance to chloramphenicol antibiotics first identified by Schwarz 2000 as cfr from Mammaliicoccus sciuri. Additional Oxazolidinone resistance mediated by the cfr gene in a human isolated was first reported from Colombia in linezolid- and methicillin-resistant Staphylococcus aureus. http://purl.obolibrary.org/obo/ARO_3003443 Antibiotic resistant tlyA http://purl.obolibrary.org/obo/ARO_3000857 16S ribosomal RNA methyltransferase tlyA encodes for hemolysin. It Catalyzes the 2'-O-methylation at nucleotides C1409 in 16S rRNA and C1920 in 23S rRNA. Mutation that arise within this gene reduces the binding affinity of aminoglycosides to rRNA. http://purl.obolibrary.org/obo/ARO_3003445 Mycobacterium tuberculosis tlyA mutations conferring resistance to aminoglycosides http://purl.obolibrary.org/obo/ARO_3003443 Antibiotic resistant tlyA Specific mutations that arise in Mycobacterium tuberculosis tlyA resulting in aminoglycosides resistance. http://purl.obolibrary.org/obo/ARO_3003446 antibiotic resistant iniA http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance iniA, an isoniazid-induced protein, is part of the iniBAC operon that participates in the development of tolerance to both isoniazid and ethambutol. May function through a MDR-pump like mechanism, although it does not appear to directly transport isoniazid from the cell. http://purl.obolibrary.org/obo/ARO_3003447 ethambutol resistant iniA http://purl.obolibrary.org/obo/ARO_3003446 antibiotic resistant iniA Mutations that occurs on the iniA genes resulting in the resistance to ethambutol. http://purl.obolibrary.org/obo/ARO_3003448 Mycobacterium tuberculosis iniA mutant conferring resistance to ethambutol http://purl.obolibrary.org/obo/ARO_3003447 ethambutol resistant iniA Specific mutations in Mycobacterium tuberculosis iniA resulting in resistance to ethambutol. http://purl.obolibrary.org/obo/ARO_3003449 Antibiotic resistant iniC http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance iniC, an isoniazid-induced protein, is part of the iniBAC operon that participates in the development of tolerance to both isoniazid and ethambutol. May function through a MDR-pump like mechanism, although it does not appear to directly transport isoniazid from the cell. http://purl.obolibrary.org/obo/ARO_3003450 Ethambutol resistant iniC http://purl.obolibrary.org/obo/ARO_3003449 Antibiotic resistant iniC Mutations that occurs on the iniC genes resulting in the resistance to ethambutol. http://purl.obolibrary.org/obo/ARO_3003451 Mycobacterium tuberculosis iniC mutant conferring resistance to ethambutol http://purl.obolibrary.org/obo/ARO_3003450 Ethambutol resistant iniC Specific mutations that occurs on Mycobacterium tuberculosis iniC causing it to be ethambutol resistant. http://purl.obolibrary.org/obo/ARO_3003452 ethambutol resistant embA http://purl.obolibrary.org/obo/ARO_3005005 antibiotic-resistant emb arabinosyltransferase Mutations that occurs on the embA genes resulting in the resistance to ethambutol. http://purl.obolibrary.org/obo/ARO_3003453 Mycobacterium tuberculosis embA mutant conferring resistance to ethambutol http://purl.obolibrary.org/obo/ARO_3003452 ethambutol resistant embA Specific mutations that occurs on Mycobacterium tuberculosis embA leading to the lowered affinity of ethambutol to embA. http://purl.obolibrary.org/obo/ARO_3003454 ethambutol resistant embR http://purl.obolibrary.org/obo/ARO_3005005 antibiotic-resistant emb arabinosyltransferase Mutations that occurs on the embR genes resulting in the resistance to ethambutol. http://purl.obolibrary.org/obo/ARO_3003455 Mycobacterium tuberculosis embR mutant conferring resistance to ethambutol http://purl.obolibrary.org/obo/ARO_3003454 ethambutol resistant embR Point mutation in the M.tuberculosis embR results in increased resistance to ethambutol. http://purl.obolibrary.org/obo/ARO_3003456 antibiotic resistant ethA http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Monooxygenase able to convert a wide range of ketones to the corresponding esters or lactones via a Baeyer-Villiger oxidation reaction. It is responsible for the activation of several thiocarbamide-containing pro-drugs into cytotoxic species. http://purl.obolibrary.org/obo/ARO_3003457 ethionamide resistant ethA http://purl.obolibrary.org/obo/ARO_3003456 antibiotic resistant ethA Mutations that occurs on the ethA genes resulting in the inability to catalyzes the oxidation of ethionamide (ETH) to the corresponding sulfoxide (the active drug). http://purl.obolibrary.org/obo/ARO_3003458 Mycobacterium tuberculosis ethA with mutation conferring resistance to ethionamide http://purl.obolibrary.org/obo/ARO_3003457 ethionamide resistant ethA Mycobacterium tuberculosis ethA (Rv3854c) is a mono-oxygenase enzyme which activates the antibiotic ethionamide in vivo. Mutations in ethA confer resistance to ethionamide by modulating the activation and activity of the ethionamide prodrug. http://purl.obolibrary.org/obo/ARO_3003459 Mycobacterium tuberculosis gyrB mutant conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3000864 fluoroquinolone resistant gyrB Point mutation in Mycobacterium tuberculosis gyrB resulting in fluoroquinolone resistance. http://purl.obolibrary.org/obo/ARO_3003460 antibiotic resistant ndh http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant ndh is a NADH oxidase. It participates in antibiotic resistance by diminishing NADH oxidation and consequently causes an increase in NADH concentration and depletion of NAD+. This alteration of the NADH/NAD+ ratio prevents the peroxidation reactions required for the activation of INH, as well as the displacement of the NADH-isonicotinic acyl complex from InhA enzyme binding site. http://purl.obolibrary.org/obo/ARO_3003461 Mycobacterium tuberculosis ndh with mutation conferring resistance to isoniazid http://purl.obolibrary.org/obo/ARO_3003460 antibiotic resistant ndh Point mutations in the Mycobacterium tuberculosis ndh gene shown clinically to confer resistance to isoniazid. http://purl.obolibrary.org/obo/ARO_3003462 antibiotic resistant kasA http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant kasA is a ketoacyl acyl carrier protein synthase that catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. It is involved in elongation of fatty acids intermediate in the biosynthetic pathway of mycolic acids. http://purl.obolibrary.org/obo/ARO_3003463 Mycobacterium tuberculosis kasA mutant conferring resistance to isoniazid http://purl.obolibrary.org/obo/ARO_3003462 antibiotic resistant kasA Specific mutations on the Mycobacterium tuberculosis kasA gene resulting in lowered affinity of isoniazid, resulting in resistance. http://purl.obolibrary.org/obo/ARO_3003464 rifamycin-resistant arabinosyltransferase http://purl.obolibrary.org/obo/ARO_3003422 antibiotic resistant aftA Arabinosyl transferases allow for the polymerization of arabinose to form arabinan. Arabanan is required for formation of mycobacterial cell walls and arabinosyltransferases are targets of the drug ethambutol. Mutations in these genes can confer resistance to rifampicin. http://purl.obolibrary.org/obo/ARO_3003465 Mycobacterium tuberculosis embB with mutation conferring resistance to rifampicin http://purl.obolibrary.org/obo/ARO_3003464 rifamycin-resistant arabinosyltransferase Specific mutations that occurs on Mycobacterium tuberculosis embB causing it to be rifampicin resistant. http://purl.obolibrary.org/obo/ARO_3003466 antibiotic resistant gidB http://purl.obolibrary.org/obo/ARO_3000857 16S ribosomal RNA methyltransferase GidB is a m7G methyltransferase specific for 16S rRNA. Mutations within the gidB gene causes changes in the structure or 16s rRNA, leading to resistance to aminoglycosides. http://purl.obolibrary.org/obo/ARO_3003470 Mycobacterium tuberculosis gidB mutation conferring resistance to streptomycin http://purl.obolibrary.org/obo/ARO_3003466 antibiotic resistant gidB Specific mutations that occurs on Mycobacterium tuberculosis gidB causing it to be streptomycin resistant. http://purl.obolibrary.org/obo/ARO_3003473 Antibiotic sensitive embR http://purl.obolibrary.org/obo/ARO_3000725 antibiotic sensitive aftA Wildtype embR is sensitive to antibiotics. It is an arabinosyltransferase involved in lipoarabinomannan synthesis. http://purl.obolibrary.org/obo/ARO_3003474 ethionamide http://purl.obolibrary.org/obo/ARO_3007156 thioamide antibiotic Ethionamide is a second-line antitubercular agent that inhibits mycolic acid synthesis. http://purl.obolibrary.org/obo/ARO_3003475 Antibiotic sensitive ethA http://purl.obolibrary.org/obo/ARO_3000716 mycolic acid synthesis enzyme targeted by antibiotic ethA is a monooxygenase that is able to convert a wide range of ketones to the corresponding esters or lactones via a Baeyer-Villiger oxidation reaction. Is responsible for the activation of several thiocarbamide-containing pro-drugs into cytotoxic species. http://purl.obolibrary.org/obo/ARO_3003476 antibiotic sensitive tlyA http://purl.obolibrary.org/obo/ARO_3000712 nucleic acid synthesis machinery targeted by antibiotic It Catalyzes the 2'-O-methylation at nucleotides C1409 in 16S rRNA and C1920 in 23S rRNA. http://purl.obolibrary.org/obo/ARO_3003477 antibiotic sensitive gidB http://purl.obolibrary.org/obo/ARO_3000712 nucleic acid synthesis machinery targeted by antibiotic GidB is a m7G methyltransferase specific for 16S rRNA. http://purl.obolibrary.org/obo/ARO_3003478 antibiotic sensitive kasA http://purl.obolibrary.org/obo/ARO_3000872 antibiotic sensitive enoyl-acyl carrier reductase kasA is a ketoacyl acyl carrier protein synthase that catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. It is involved in elongation of fatty acids intermediate in the biosynthetic pathway of mycolic acids. http://purl.obolibrary.org/obo/ARO_3003479 tetR http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux TetR is the repressor of the tetracycline resistance element; its N-terminal region forms a helix-turn-helix structure and binds DNA. Binding of tetracycline to TetR reduces the repressor affinity for the tetracycline resistance gene (tetA) promoter operator sites. Mutations arise within tetR results in lower affinity for tetracyclin. http://purl.obolibrary.org/obo/ARO_3003480 Mycobacterium tuberculosis 16S rRNA mutation conferring resistance to streptomycin http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations within the 530 loop of the 16S rRNA of Mycobacterium tuberculosis can result in resistance against streptomycin. These mutations do not directly inhibit the binding of streptomycin, but is hypothesized that they interfere with conformational perturbations that account for streptomycin's action on the ribosome. http://purl.obolibrary.org/obo/ARO_3003481 Mycobacterium tuberculosis 16S rRNA mutation conferring resistance to amikacin http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in the 3' domain of 16S rRNA of Mycobacterium tuberculosis can confer resistance to amikacin. http://purl.obolibrary.org/obo/ARO_3003485 Chlamydophila psittaci 16S rRNA mutation conferring resistance to spectinomycin http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutation in the 16S rRNA helix 34 region of Chlamydophila psittaci can confer resistance against spectinomycin. http://purl.obolibrary.org/obo/ARO_3003493 Pasteurella multocida 16S rRNA mutation conferring resistance to spectinomycin http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in the helix 34 region of 16S rRNA of Pasteurella multocida can confer resistance to spectinomycin. http://purl.obolibrary.org/obo/ARO_3003495 Neisseria gonorrhoeae 16S rRNA mutation conferring resistance to spectinomycin http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in the helix 34 region of 16S rRNA of Neisseria gonorrhoeae can confer resistance against spectinomycin. http://purl.obolibrary.org/obo/ARO_3003497 Neisseria meningitidis 16S rRNA mutation conferring resistance to spectinomycin http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in the 16S rRNA of Neisseria meningitidis can confer resistance to spectinomycin. http://purl.obolibrary.org/obo/ARO_3003499 Cutibacterium acnes 16S rRNA mutation conferring resistance to tetracycline http://purl.obolibrary.org/obo/ARO_3003669 16S rRNA with mutation conferring resistance to tetracycline derivatives Tetracycline binds tightly to the helix 34 domain in 16S rRNA, where it interferes sterically with the binding of aminoacyl-tRNA to the ribosome A site to block protein synthesis. Mutations in the nucleotide sequence in this domain for Cutibacterium acnes can result in resistance against tetracycline. http://purl.obolibrary.org/obo/ARO_3003502 Borreliella burgdorferi 16S rRNA mutation conferring resistance to spectinomycin http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in the 3' major domain of the 16S rRNA gene of Borreliella burgdorferi can confer resistance to spectinomycin. http://purl.obolibrary.org/obo/ARO_3003503 Borreliella burgdorferi 16S rRNA mutation conferring resistance to kanamycin http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in the 3' minor domain of the 16S rRNA gene of Borreliella burgdorferi can confer resistance to kanamycin. http://purl.obolibrary.org/obo/ARO_3003504 Borreliella burgdorferi 16S rRNA mutation conferring resistance to gentamicin http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in the 3' minor domain of the 16S rRNA gene of Borreliella burgdorferi can confer resistance to gentamicin. http://purl.obolibrary.org/obo/ARO_3003510 Helicobacter pylori 16S rRNA mutation conferring resistance to tetracycline http://purl.obolibrary.org/obo/ARO_3003669 16S rRNA with mutation conferring resistance to tetracycline derivatives Tetracycline binds tightly to the helix 34 domain in 16S rRNA, where it interferes sterically with the binding of aminoacyl-tRNA to the ribosome A site to block protein synthesis. Mutations in the nucleotide sequence in this domain of Helicobacter pylori can result in resistance against tetracycline. http://purl.obolibrary.org/obo/ARO_3003511 Escherichia coli soxS with mutation conferring antibiotic resistance http://purl.obolibrary.org/obo/ARO_3000837 soxS SoxS is a global regulator that up-regulates the expression of AcrAB efflux genes. It also reduces OmpF expression to decrease cell membrane permeability. http://purl.obolibrary.org/obo/ARO_3003512 Salmonella enterica 16S rRNA (rrsD) mutation conferring resistance to spectinomycin http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in the helix 34 region of the rrsD 16S rRNA gene of Salmonella enterica serovar Typhimurium can confer resistance to spectinomycin. http://purl.obolibrary.org/obo/ARO_3003514 Mycobacteroides chelonae 16S rRNA mutation conferring resistance to amikacin http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in the 16S rRNA of Mycobacteroides chelonae can cause resistance to amikacin. http://purl.obolibrary.org/obo/ARO_3003515 Mycobacteroides chelonae 16S rRNA mutation conferring resistance to kanamycin A http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in the 16S rRNA of Mycobacteroides chelonae can cause resistance to kanamycin A. http://purl.obolibrary.org/obo/ARO_3003516 Mycobacteroides chelonae 16S rRNA mutation conferring resistance to tobramycin http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in the 16S rRNA of Mycobacteroides chelonae can cause resistance to tobramycin. http://purl.obolibrary.org/obo/ARO_3003517 Mycobacteroides chelonae 16S rRNA mutation conferring resistance to gentamicin C http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in the 16S rRNA of Mycobacteroides chelonae can confer resistance to gentamicin C. http://purl.obolibrary.org/obo/ARO_3003518 Mycobacteroides chelonae 16S rRNA mutation conferring resistance to neomycin http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in the 16S rRNA of Mycobacteroides chelonae can cause resistance to neomycin. http://purl.obolibrary.org/obo/ARO_3003520 Antibiotic sensitive Borreliella burgdorferi 16S rRNA http://purl.obolibrary.org/obo/ARO_3000755 antibiotic sensitive 16S rRNA Sensitive form of 16s susceptable to antibiotics. http://purl.obolibrary.org/obo/ARO_3003521 Antibiotic sensitive Chlamydophila psittaci 16S rRNA http://purl.obolibrary.org/obo/ARO_3000755 antibiotic sensitive 16S rRNA Sensitive form of 16s susceptable to antibiotics. http://purl.obolibrary.org/obo/ARO_3003522 Antibiotic sensitive Helicobacter pylori 16S rRNA http://purl.obolibrary.org/obo/ARO_3000755 antibiotic sensitive 16S rRNA Sensitive form of 16s susceptable to antibiotics. http://purl.obolibrary.org/obo/ARO_3003523 Antibiotic sensitive Mycobacteroides chelonae 16S rRNA http://purl.obolibrary.org/obo/ARO_3000755 antibiotic sensitive 16S rRNA Sensitive form of 16s susceptable to antibiotics. http://purl.obolibrary.org/obo/ARO_3003524 Antibiotic sensitive Mycolicibacterium smegmatis 16S rRNA http://purl.obolibrary.org/obo/ARO_3000755 antibiotic sensitive 16S rRNA Sensitive form of 16s susceptable to antibiotics. http://purl.obolibrary.org/obo/ARO_3003525 Antibiotic sensitive Neisseria gonorrhoeae 16S rRNA http://purl.obolibrary.org/obo/ARO_3000755 antibiotic sensitive 16S rRNA Sensitive form of 16s susceptable to antibiotics. http://purl.obolibrary.org/obo/ARO_3003526 Antibiotic sensitive Neisseria meningitidis 16S rRNA http://purl.obolibrary.org/obo/ARO_3000755 antibiotic sensitive 16S rRNA Sensitive form of 16s susceptable to antibiotics. http://purl.obolibrary.org/obo/ARO_3003527 Antibiotic sensitive Pasteurella multocida 16S rRNA http://purl.obolibrary.org/obo/ARO_3000755 antibiotic sensitive 16S rRNA Sensitive form of 16s susceptable to antibiotics. http://purl.obolibrary.org/obo/ARO_3003528 Antibiotic sensitive Cutibacterium acnes 16S rRNA http://purl.obolibrary.org/obo/ARO_3000755 antibiotic sensitive 16S rRNA Sensitive form of 16s susceptable to antibiotics. http://purl.obolibrary.org/obo/ARO_3003529 Antibiotic sensitive Salmonella enterica serovar Typhimurium 16S rRNA http://purl.obolibrary.org/obo/ARO_3000755 antibiotic sensitive 16S rRNA Sensitive form of 16s susceptable to antibiotics. http://purl.obolibrary.org/obo/ARO_3003530 Antibiotic sensitive Mycobacterium tuberculosis 16S rRNA http://purl.obolibrary.org/obo/ARO_3000755 antibiotic sensitive 16S rRNA Sensitive form of 16s susceptable to antibiotics. http://purl.obolibrary.org/obo/ARO_3003539 Mycolicibacterium smegmatis 16S rRNA (rrsA) mutation conferring resistance to hygromycin B http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in the highly conserved helix 44 of the 16S rrsA rRNA gene of Mycolicibacterium smegmatis can confer resistance to hygromycin B. Resistance against hygromycin B is the result of conformational alterations that distorts a strong hydrogen bond leading to a change in the local geometry of the hygromycin B binding site. http://purl.obolibrary.org/obo/ARO_3003540 Mycolicibacterium smegmatis 16S rRNA (rrsB) mutation conferring resistance to hygromycin B http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in the highly conserved helix 44 of the 16S rrsB rRNA gene of Mycolicibacterium smegmatis can confer resistance to hygromycin B. Resistance against hygromycin B is the result of conformational alterations that distorts a strong hydrogen bond leading to a change in the local geometry of the hygromycin B binding site. http://purl.obolibrary.org/obo/ARO_3003541 Mycolicibacterium smegmatis 16S rRNA (rrsB) mutation conferring resistance to streptomycin http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in the helix 44 region of the 16S rRNA rrsB gene of Mycolicibacterium smegmatis can confer resistance to streptomycin. http://purl.obolibrary.org/obo/ARO_3003542 Mycolicibacterium smegmatis 16S rRNA (rrsB) mutation conferring resistance to kanamycin A http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in the helix 44 region of the 16S rRNA rrsB gene of Mycolicibacterium smegmatis can confer resistance to kanamycin A. http://purl.obolibrary.org/obo/ARO_3003543 Mycolicibacterium smegmatis 16S rRNA (rrsA) mutation conferring resistance to kanamycin A http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in the helix 44 region of the 16S rRNA rrsA gene of Mycolicibacterium smegmatis can confer resistance to kanamycin A. http://purl.obolibrary.org/obo/ARO_3003544 Mycolicibacterium smegmatis 16S rRNA (rrsA) mutation conferring resistance to neomycin http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in the helix 44 region of the 16S rRNA rrsA gene of Mycolicibacterium smegmatis can confer resistance to neomycin. http://purl.obolibrary.org/obo/ARO_3003545 Mycolicibacterium smegmatis 16S rRNA (rrsB) mutation conferring resistance to neomycin http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutations in the helix 44 region of the 16S rRNA rrsB gene of Mycolicibacterium smegmatis can confer resistance to neomycin. http://purl.obolibrary.org/obo/ARO_3003546 Mycolicibacterium smegmatis 16S rRNA (rrsA) mutation conferring resistance to viomycin http://purl.obolibrary.org/obo/ARO_3003667 16s rRNA with mutation conferring resistance to peptide antibiotics Point mutations in the helix 44 region of the 16S rRNA rrsA gene of Mycolicibacterium smegmatis can confer resistance to viomycin. http://purl.obolibrary.org/obo/ARO_3003547 Mycolicibacterium smegmatis 16S rRNA (rrsB) mutation conferring resistance to viomycin http://purl.obolibrary.org/obo/ARO_3003667 16s rRNA with mutation conferring resistance to peptide antibiotics Point mutations in the helix 44 region of the 16S rRNA rrsB gene of Mycolicibacterium smegmatis can confer resistance to viomycin. http://purl.obolibrary.org/obo/ARO_3003548 mdtN http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance Multidrug resistance efflux pump. Could be involved in resistance to puromycin, acriflavine and tetraphenylarsonium chloride. http://purl.obolibrary.org/obo/ARO_3003549 mdtO http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance Multidrug resistance efflux pump. Could be involved in resistance to puromycin, acriflavine and tetraphenylarsonium chloride. http://purl.obolibrary.org/obo/ARO_3003550 mdtP http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance Multidrug resistance efflux pump. Could be involved in resistance to puromycin, acriflavine and tetraphenylarsonium chloride. http://purl.obolibrary.org/obo/ARO_3003551 emeA http://purl.obolibrary.org/obo/ARO_3000112 multidrug and toxic compound extrusion (MATE) transporter A multidrug efflux pump from Enterococcus faecalis. There exist efflux activity of several antimicrobial agents such as DAPI, Hoechst 33342 and acriflavine. Efflux of DAPI via EmeA was strongly inhibited by reserpine. http://purl.obolibrary.org/obo/ARO_3003552 fusB http://purl.obolibrary.org/obo/ARO_3005086 Target protecting FusB-type protein conferring resistance to Fusidic acid FusB encodes a 2-domain zinc-binding protein that binds the ribosomal translocase EF-G, causing it to dissociate from the ribosome. This action increases the ribosomal turnover rate and confers resistance to fusidic acid. This protein is considered a FusB-type protein. http://purl.obolibrary.org/obo/ARO_3003553 CepS http://purl.obolibrary.org/obo/ARO_3004199 CepS beta-lactamase CEPS is a typical class C cephalosporinase found in Aeromonas sobria, first isolated from strain 163a. http://purl.obolibrary.org/obo/ARO_3003554 tcmA http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump Major facilitator superfamily transporter. Resistance to tetracenomycin C by an active tetracenomycin C efflux system which is probably energized by transmembrane electrochemical gradients. http://purl.obolibrary.org/obo/ARO_3003555 SHW beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase This family of sublcass B1 beta-lactamases were discovered in species of the Shewanella genus. http://purl.obolibrary.org/obo/ARO_3003556 SLB-1 http://purl.obolibrary.org/obo/ARO_3003555 SHW beta-lactamase This enzyme breaks the beta-lactam antibiotic ring open and deactivates the molecule's antibacterial properties. http://purl.obolibrary.org/obo/ARO_3003557 SFB-1 http://purl.obolibrary.org/obo/ARO_3003555 SHW beta-lactamase This enzyme breaks the beta-lactam antibiotic ring open and deactivates the molecule's antibacterial properties. http://purl.obolibrary.org/obo/ARO_3003558 y56 beta-lactamase http://purl.obolibrary.org/obo/ARO_3004190 BlaA beta-lactamase Class A beta-lactamase found in Yersinia enterocolitica biovar 1A. http://purl.obolibrary.org/obo/ARO_3003559 cepA http://purl.obolibrary.org/obo/ARO_3004192 CepA beta-lactamase A beta-lactamase found in Bacteroides fragilis producing either low or high levels of the endogenous cephalosporinase activity. http://purl.obolibrary.org/obo/ARO_3003561 SED-1 http://purl.obolibrary.org/obo/ARO_3007880 SED beta-lactamase SED-1 is a chromosomal-encoded class A beta-lactamase identified in Citrobacter sedlakii. http://purl.obolibrary.org/obo/ARO_3003562 blaF http://purl.obolibrary.org/obo/ARO_3004233 blaF family beta-lactamase Class A beta-lactamase found in Mycolicibacterium fortuitum. http://purl.obolibrary.org/obo/ARO_3003563 RCP-1 http://purl.obolibrary.org/obo/ARO_3004235 RCP beta-lactamase RCP is a class A beta-lactamase found in Rhodopseudomonas capsulata. http://purl.obolibrary.org/obo/ARO_3003564 EXO-1 http://purl.obolibrary.org/obo/ARO_3004234 EXO beta-lactamase Class A beta-lactamase found in Streptomyces albus G. http://purl.obolibrary.org/obo/ARO_3003565 R39 http://purl.obolibrary.org/obo/ARO_3004198 R39 beta-lactamase Class A beta-lactamase found in Actinomadura R39. http://purl.obolibrary.org/obo/ARO_3003567 magainin A http://purl.obolibrary.org/obo/ARO_3000694 magainin Magainins A are antimicrobial peptides produced by amphibians as part of their innate immune system. http://purl.obolibrary.org/obo/ARO_3003568 Magainin B http://purl.obolibrary.org/obo/ARO_3000694 magainin Magainin B is is a synthetic analog of magainin 1, an antimicrobial peptide. http://purl.obolibrary.org/obo/ARO_3003569 Magainin G http://purl.obolibrary.org/obo/ARO_3000694 magainin Magainin G is is a synthetic analog of magainin 1, an antimicrobial peptide. It differs from magainin B by the addition of an beta-alanine at the N terminal. http://purl.obolibrary.org/obo/ARO_3003570 Magainin H http://purl.obolibrary.org/obo/ARO_3000694 magainin Magainin H is is a synthetic analog of magainin 1, an antimicrobial peptide. It differs from magainin B with the substitution of D-alanine instead of L-alanine. http://purl.obolibrary.org/obo/ARO_3003571 magainin 1 http://purl.obolibrary.org/obo/ARO_3000694 magainin Magainin1 is an antimicrobial peptides produced by amphibians as part of their innate immune system. It is derived from the Xenopus laevis. http://purl.obolibrary.org/obo/ARO_3003572 magainin 2 http://purl.obolibrary.org/obo/ARO_3000694 magainin Magainin 2 is an antimicrobial peptides produced from Xenopus laevis skin. It induce osmotic lysis of bacteria. http://purl.obolibrary.org/obo/ARO_3003573 LpxA http://purl.obolibrary.org/obo/ARO_3003581 Acinetobacter mutant Lpx gene conferring resistance to colistin The LpxA gene is widely known to be involved in the biosynthesis of lipid A in Gram-negative bacteria and mutations to this gene may cause resistance to antimicrobial peptides that target the outer membrane. http://purl.obolibrary.org/obo/ARO_3003574 LpxC http://purl.obolibrary.org/obo/ARO_3003581 Acinetobacter mutant Lpx gene conferring resistance to colistin The LpxC gene is widely known to be involved in the biosynthesis of lipid A in Gram-negative bacteria and mutations to this gene may cause resistance to antimicrobial peptides that target the outer membrane. http://purl.obolibrary.org/obo/ARO_3003575 LpxD http://purl.obolibrary.org/obo/ARO_3003581 Acinetobacter mutant Lpx gene conferring resistance to colistin The LpxD gene is widely known to be involved in the biosynthesis of lipid A in Gram-negative bacteria and mutations to this gene may cause resistance to antimicrobial peptides that target the outer membrane. http://purl.obolibrary.org/obo/ARO_3003576 eptA http://purl.obolibrary.org/obo/ARO_3004269 pmr phosphoethanolamine transferase PmrC mediates the modification of Lipid A by the addition of 4-amino-4-deoxy-L-arabinose (L-Ara4N) and phosphoethanolamine, resulting in a less negative cell membrane and decreased binding of polymyxin B. http://purl.obolibrary.org/obo/ARO_3003577 ugd http://purl.obolibrary.org/obo/ARO_3004269 pmr phosphoethanolamine transferase PmrE is required for the synthesis and transfer of 4-amino-4-deoxy-L-arabinose (Ara4N) to Lipid A, which allows gram-negative bacteria to resist the antimicrobial activity of cationic antimicrobial peptides and antibiotics such as polymyxin. http://purl.obolibrary.org/obo/ARO_3003578 PmrF http://purl.obolibrary.org/obo/ARO_3004269 pmr phosphoethanolamine transferase PmrF is required for the synthesis and transfer of 4-amino-4-deoxy-L-arabinose (Ara4N) to Lipid A, which allows gram-negative bacteria to resist the antimicrobial activity of cationic antimicrobial peptides and antibiotics such as polymyxin. pmrF corresponds to 1 locus in Pseudomonas aeruginosa PAO1 and 1 locus in Pseudomonas aeruginosa LESB58. http://purl.obolibrary.org/obo/ARO_3003579 basRS http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux BasRS is a two-component regulatory system. BasR is phosphorylated by BasS at high[Fe3+] levels. The BasRS system regulates the expression of pmrE, pmrF and pmrC, leading to antibiotic resistance. http://purl.obolibrary.org/obo/ARO_3003580 gene altering cell wall charge http://purl.obolibrary.org/obo/ARO_3000000 determinant of antibiotic resistance Genes involved in alteration of the cell wall overall charge, leading to antimicrobial resistance due to reduced binding. http://purl.obolibrary.org/obo/ARO_3003581 Acinetobacter mutant Lpx gene conferring resistance to colistin http://purl.obolibrary.org/obo/ARO_3000012 protein(s) conferring antibiotic resistance via molecular bypass These genes are involved in the biosynthesis of lipid A in Gram-negative bacteria and mutations to this gene may cause resistance to antimicrobial peptides that target the outer membrane. Mutation by absence or insertion of ISAba11 sequence is a known cause of resistance in Acinetobacter baumannii▿. http://purl.obolibrary.org/obo/ARO_3003582 basR http://purl.obolibrary.org/obo/ARO_3000750 protein of two-component regulatory system modulating antibiotic efflux Response regulator for Lipid A modification genes; two-component system involved in polymyxin resistance that senses high extracellular Fe(2+). http://purl.obolibrary.org/obo/ARO_3003583 basS http://purl.obolibrary.org/obo/ARO_3000750 protein of two-component regulatory system modulating antibiotic efflux Histidine protein kinase sensor Lipid A modification gene; part of a two-component system involved in polymyxin resistance that senses high extracellular Fe(2+). http://purl.obolibrary.org/obo/ARO_3003585 Klebsiella mutant PhoP conferring antibiotic resistance to colistin http://purl.obolibrary.org/obo/ARO_3003580 gene altering cell wall charge A mutant phoP activates pmrHFIJKLM expression responsible for L-aminoarabinose synthesis and polymyxin resistance, by way of alteration of negative charge. http://purl.obolibrary.org/obo/ARO_3003588 charge alteration conferring antibiotic resistance http://purl.obolibrary.org/obo/ARO_0001001 antibiotic target alteration The loss or reduction of the net negative charge within the cell wall of gram negative bacteria is a mechanism of resistance for cationic antimicrobials that depend on the negative charge for binding to the surface. http://purl.obolibrary.org/obo/ARO_3003589 NmcA http://purl.obolibrary.org/obo/ARO_3000018 IMI beta-lactamase NmcA is a class A serine beta-lactamase isolated from Enterobacter cloacae. http://purl.obolibrary.org/obo/ARO_3003590 SHV-190 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-190 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003591 SHV-191 http://purl.obolibrary.org/obo/ARO_3000015 SHV beta-lactamase SHV-191 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003592 TEM-223 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-223 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003593 OXA-437 http://purl.obolibrary.org/obo/ARO_3007711 OXA-24-like beta-lactamase OXA-437 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003594 OXA-438 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-438 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003595 OXA-439 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-439 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003596 OXA-440 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-440 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003597 OXA-441 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-441 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003598 OXA-442 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-442 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003599 OXA-443 http://purl.obolibrary.org/obo/ARO_3007708 OXA-22-like beta-lactamase OXA-443 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003600 OXA-444 http://purl.obolibrary.org/obo/ARO_3007729 OXA-60-like beta-lactamase OXA-444 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003601 OXA-445 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-445 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003602 OXA-446 http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase OXA-446 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003603 OXA-447 http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase OXA-447 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003604 OXA-448 http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase OXA-448 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003605 OXA-449 http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase OXA-449 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003606 OXA-450 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-450 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003607 OXA-451 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-451 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003608 OXA-452 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-452 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003609 OXA-453 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-453 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003610 OXA-454 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase OXA-454 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003611 OXA-455 http://purl.obolibrary.org/obo/ARO_3007716 OXA-364-like beta-lactamase OXA-455 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003612 OXA-456 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-456 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003613 OXA-457 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-457 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003614 OXA-458 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-458 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003615 OXA-459 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-459 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003616 OXA-460 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-460 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003617 OXA-461 http://purl.obolibrary.org/obo/ARO_3007730 OXA-61-like beta-lactamase OXA-461 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003618 OXA-462 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-462 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003619 OXA-463 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-463 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003620 OXA-464 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-464 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003621 OXA-465 http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase OXA-465 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003622 OXA-466 http://purl.obolibrary.org/obo/ARO_3007702 OXA-184-like beta-lactamase OXA-466 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003623 OXA-467 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-467 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003624 OXA-468 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-468 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003625 OXA-469 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-469 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003626 OXA-470 http://purl.obolibrary.org/obo/ARO_3007732 OXA-63-like beta-lactamase OXA-470 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003627 OXA-471 http://purl.obolibrary.org/obo/ARO_3007732 OXA-63-like beta-lactamase OXA-471 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003628 OXA-472 http://purl.obolibrary.org/obo/ARO_3007732 OXA-63-like beta-lactamase OXA-472 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003629 OXA-473 http://purl.obolibrary.org/obo/ARO_3007732 OXA-63-like beta-lactamase OXA-473 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003631 OXA-474 http://purl.obolibrary.org/obo/ARO_3007732 OXA-63-like beta-lactamase OXA-474 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003632 OXA-475 http://purl.obolibrary.org/obo/ARO_3007732 OXA-63-like beta-lactamase OXA-475 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003633 OXA-476 http://purl.obolibrary.org/obo/ARO_3007732 OXA-63-like beta-lactamase OXA-476 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003634 OXA-477 http://purl.obolibrary.org/obo/ARO_3007732 OXA-63-like beta-lactamase OXA-477 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003635 OXA-478 http://purl.obolibrary.org/obo/ARO_3007732 OXA-63-like beta-lactamase OXA-478 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003636 OXA-479 http://purl.obolibrary.org/obo/ARO_3007732 OXA-63-like beta-lactamase OXA-479 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003637 OXA-480 http://purl.obolibrary.org/obo/ARO_3007725 OXA-51-like beta-lactamase OXA-480 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003638 OXA-481 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-481 is a carbapenem-hydrolyzing class D beta-lactamase. http://purl.obolibrary.org/obo/ARO_3003639 OXA-482 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-482 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003640 OXA-483 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-483 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003641 OXA-484 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase OXA-484 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003642 OXA-485 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-485 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003643 OXA-486 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-486 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003644 OXA-487 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase OXA-487 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003645 OXA-488 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-488 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003646 CTX-M-162 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-162 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003647 CTX-M-163 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-163 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003648 CTX-M-164 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-164 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003649 CTX-M-165 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-165 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003650 CTX-M-166 http://purl.obolibrary.org/obo/ARO_3000016 CTX-M beta-lactamase CTX-M-166 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003652 CMY-132 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-132 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003653 CMY-133 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-133 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003654 CMY-134 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-134 is a beta-lactamase found in Escherichia coli. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3003655 ACT-38 http://purl.obolibrary.org/obo/ARO_3000072 ACT beta-lactamase A class C beta-lactamase from Citrobacter freundii. http://purl.obolibrary.org/obo/ARO_3003657 IMP-49 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-49 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003658 IMP-50 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-50 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003659 IMP-51 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-51 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003660 VIM-44 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-44 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003661 VIM-45 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-45 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003662 VIM-46 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-46 is a beta-lactamase. Name originally from the historical Lahey list of beta-lactamases, some of which did not include sequence data. http://purl.obolibrary.org/obo/ARO_3003663 NDM-15 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase New Delhi metallo-beta-lactamase-15 variant of NDM-1. http://purl.obolibrary.org/obo/ARO_3003664 NDM-16a http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase New Delhi class B metallo-beta-lactamase-16a variant of NDM-1. http://purl.obolibrary.org/obo/ARO_3003665 NmcR http://purl.obolibrary.org/obo/ARO_3000100 gene modulating beta-lactam resistance NmcR is a homolog of the LysR regulator found in Enterobacter cloacae that contribute to the regulation of NmcA beta-lactamase. http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics http://purl.obolibrary.org/obo/ARO_3003211 16S rRNA with mutation conferring antibiotic resistance Point mutations in the 16S rRNA of bacteria can confer resistance to aminoglycosides. http://purl.obolibrary.org/obo/ARO_3003667 16s rRNA with mutation conferring resistance to peptide antibiotics http://purl.obolibrary.org/obo/ARO_3003211 16S rRNA with mutation conferring antibiotic resistance Point mutations in the 16S rRNA of bacteria can confer resistance to peptide antibiotics. http://purl.obolibrary.org/obo/ARO_3003668 16s rRNA with mutation conferring resistance to polyamine antibiotics http://purl.obolibrary.org/obo/ARO_3003211 16S rRNA with mutation conferring antibiotic resistance Point mutations in the 16S rRNA of bacteria can confer resistance to polyamine antibiotics. http://purl.obolibrary.org/obo/ARO_3003669 16S rRNA with mutation conferring resistance to tetracycline derivatives http://purl.obolibrary.org/obo/ARO_3003211 16S rRNA with mutation conferring antibiotic resistance Point mutations in the bacterial 16S rRNA region shown clinically to confer resistance to tetracycline and tetracycline derivatives (polyketide antibiotics). http://purl.obolibrary.org/obo/ARO_3003670 PEDO-1 http://purl.obolibrary.org/obo/ARO_3004220 subclass B3 PEDO beta-lactamase PEDO-1 is a subclass B3 metallo-beta lactamase isolated from Pedobacter roseus exhibiting resistance to carbapenems. http://purl.obolibrary.org/obo/ARO_3003675 plazomicin http://purl.obolibrary.org/obo/ARO_0000016 aminoglycoside antibiotic Plazomicin is a neoglycoside, or next-generation, aminoglycoside, that has been identified as a potentially useful agent to combat drug-resistant bacteria, such as Acinetobacter baumannii and Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3003676 AAC(6')-Ib' http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Ib' is an aminoglycoside acetyltransferase encoded by plasmids, transposons, integrons in P. aeruginosa and P. fluorescens. http://purl.obolibrary.org/obo/ARO_3003677 AAC(6')-Iaj http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Iaj is a functional acetyltransferase that modifies the amino groups at the 6' positions of aminoglycosides and contributes to aminoglycoside resistance of P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3003678 TriABC-OpmH http://purl.obolibrary.org/obo/ARO_0010004 resistance-nodulation-cell division (RND) antibiotic efflux pump TriABC-OpmH is a triclosan-specific efflux pump expressed in the Gram-negative Pseudomonas aeruginosa. TriABC is the only P. aeruginosa resistance nodulation cell division (RND) pump which contains two membrane fusion proteins, TriA and TriB, and both are required for efflux pump function. TriABC associated with OpmH assemble a functional triclosan efflux pump. http://purl.obolibrary.org/obo/ARO_3003679 TriA http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance TriA is a membrane protein that is fused to TriB and both are required for the triclosan efflux pump function of TriABC-OpmH in P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3003680 TriB http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance TriB is a membrane protein that is fused to TriA and both are required for the triclosan efflux pump function of TriABC-OpmH in P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3003681 TriC http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance TriC is a resistance nodulation cell division (RND) transporter that is a part of TriABC-OpmH, a triclosan-specific efflux protein. http://purl.obolibrary.org/obo/ARO_3003682 OpmH http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance OpmH is an outer membrane efflux protein required for triclosan-specific efflux pump function. http://purl.obolibrary.org/obo/ARO_3003684 Pseudomonas aeruginosa gyrA conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3003292 fluoroquinolone resistant gyrA Point mutation of Pseudomonas aeruginosa gyrA resulted in the lowered affinity between fluoroquinolones and gyrA. Thus, conferring resistance. http://purl.obolibrary.org/obo/ARO_3003685 Pseudomonas aeruginosa parE conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3003313 fluoroquinolone resistant parE Point mutation in Pseudomonas aeruginosa parE resulting in sensitivity to fluoroquinolones (ciprofloxacin). In combination with a gyrase mutation (gyrA or gyrB), it confers a high level of resistance to ciprofloxacin. http://purl.obolibrary.org/obo/ARO_3003686 Pseudomonas aeruginosa oprD with mutation conferring resistance to imipenem http://purl.obolibrary.org/obo/ARO_3004278 Outer Membrane Porin (Opr) oprD is an outer membrane porin which facilitates the uptake of basic amino acids and imipenem in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3003688 PvrR http://purl.obolibrary.org/obo/ARO_3004286 phenotypic variant regulator PvrR is a response regulator that controls the conversion between antibiotic-resistant and antibiotic-susceptible forms of Pseudomonas aeruginosa biofilms through porin deletion/gene absence. http://purl.obolibrary.org/obo/ARO_3003689 MCR-1.1 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase MCR-1 is a plasmid-borne phosphoethanolamine transferase that interferes with binding of colistin to the cell membrane via addition of phosphoethanolamine to lipid A, resulting reduction in negative charge of the cell membrane. http://purl.obolibrary.org/obo/ARO_3003690 sitafloxacin http://purl.obolibrary.org/obo/ARO_0000001 fluoroquinolone antibiotic Sitafloxacin is a fluoroquinolone active against multi-resistant Gram-positive and negative pathogens. Sitafloxacin shows inhibitory activity against DNA gyrase and topoisomerase IV, which blocks bacterial DNA replication, thereby causing double-stranded breaks in the bacterial chromosome. http://purl.obolibrary.org/obo/ARO_3003691 MexJK-OpmH http://purl.obolibrary.org/obo/ARO_0010004 resistance-nodulation-cell division (RND) antibiotic efflux pump MexJK-OpmH is a triclosan efflux protein expressed in the Gram-negative Pseudomonas aeruginosa. MexJ is the membrane fusion protein, MexK is the inner membrane resistance-nodulation-cell division (RND) transporter, and OpmH is the outer membrane efflux protein. MexJK is constitutively expressed in mexL mutants. http://purl.obolibrary.org/obo/ARO_3003692 MexJ http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MexJ is the membrane fusion protein of the MexJK multidrug efflux protein. http://purl.obolibrary.org/obo/ARO_3003693 MexK http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MexK is the inner membrane resistance-nodulation-cell division (RND) transporter in the MexJK multidrug efflux protein. http://purl.obolibrary.org/obo/ARO_3003694 MexJK-OprM http://purl.obolibrary.org/obo/ARO_0010004 resistance-nodulation-cell division (RND) antibiotic efflux pump MexJK-OprM is a multidrug efflux protein expressed in the Gram-negative Pseudomonas aeruginosa. MexJ is the membrane fusion protein, MexK is the inner membrane resistance-nodulation-cell division (RND) transporter, and OprM is the outer membrane factor protein. http://purl.obolibrary.org/obo/ARO_3003697 MexPQ-OpmE http://purl.obolibrary.org/obo/ARO_0010004 resistance-nodulation-cell division (RND) antibiotic efflux pump MexPQ-OpmE multidrug efflux pump expressed in Pseudomonas aeruginosa. MexP is the membrane fusion protein; MexQ is the inner membrane transporter; and OpmE is the outer membrane channel. http://purl.obolibrary.org/obo/ARO_3003698 mexP http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MexP is the membrane fusion protein of the MexPQ-OpmE multidrug efflux complex. http://purl.obolibrary.org/obo/ARO_3003699 mexQ http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MexQ is the inner membrane transporter of the multidrug efflux pump MexPQ-OpmE. http://purl.obolibrary.org/obo/ARO_3003700 opmE http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance opmE is an outer membrane factor protein that is part of the multidrug efflux pump MexPQ-OpmE. http://purl.obolibrary.org/obo/ARO_3003701 rokitamycin http://purl.obolibrary.org/obo/ARO_0000000 macrolide antibiotic Rokitamycin is a macrolide antibiotic. Synthesized from strains of Streptomyces kitasatoensis. http://purl.obolibrary.org/obo/ARO_3003702 Pseudomonas aeruginosa gyrA and parC conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3000619 fluoroquinolone resistant parC Point mutation in Pseudomonas aeruginosa parC resulting in fluoroquinolone resistance also requiring a gyrA mutation. http://purl.obolibrary.org/obo/ARO_3003703 MexMN-OprM http://purl.obolibrary.org/obo/ARO_0010004 resistance-nodulation-cell division (RND) antibiotic efflux pump MexMN-OprM is a multidrug efflux pump expressed in Pseudomonas aeruginosa. MexM is the membrane fusion protein; MexN is the inner membrane transporter; and OprM is the outer membrane channel. http://purl.obolibrary.org/obo/ARO_3003704 mexM http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance mexM is the membrane fusion protein of the MexMN-OprM multidrug efflux complex. http://purl.obolibrary.org/obo/ARO_3003705 mexN http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MexN is the inner membrane transporter of the MexMN-OprM multidrug efflux complex. http://purl.obolibrary.org/obo/ARO_3003707 faropenem http://purl.obolibrary.org/obo/ARO_3009109 other cephalosporins and penems Faropenem is an orally active beta-lactam antibiotic belonging to the penem group. http://purl.obolibrary.org/obo/ARO_3003708 panipenem http://purl.obolibrary.org/obo/ARO_0000020 carbapenem Panipenem is a carbapenem antibacterial agent with a broad spectrum of in vitro activity covering a wide range of Gram-negative and Gram-positive aerobic and anaerobic bacterial. It is used in combination with betamipron to inhibit panipenem uptake into the renal tubule and prevent nephrotoxicity. http://purl.obolibrary.org/obo/ARO_3003709 MexZ http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux MexZ is a transcriptional regulator that downregulates the mexXY multidrug transporter operon, which confers to aminoglycoside resistance on Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3003710 MexL http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux MexL is a specific repressor of mexJK transcription and autoregulates its own expression. http://purl.obolibrary.org/obo/ARO_3003712 VEB-16 http://purl.obolibrary.org/obo/ARO_3000043 VEB beta-lactamase VEB-16 (VEB-1b) is a beta-lactamase that is found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3003713 VCC-1 http://purl.obolibrary.org/obo/ARO_3004196 VCC beta-lactamase VCC-1 is a Class A carbapenemase isolated from Vibrio cholerae and exhibits resistance to penicillins, carbapenems and monobactam antibiotics. http://purl.obolibrary.org/obo/ARO_3003714 PEDO-2 http://purl.obolibrary.org/obo/ARO_3004220 subclass B3 PEDO beta-lactamase PEDO-2 is a subclass B3 metallo-beta lactamase isolated from Pedobacter borealis exhibiting carbapenem resistance. http://purl.obolibrary.org/obo/ARO_3003715 PEDO-3 http://purl.obolibrary.org/obo/ARO_3004227 subclass B1 PEDO beta-lactamase PEDO-3 is a class B1 metallo-beta lactamase isolated from Pedobacter kyungheensis exhibiting resistance to carbapenems. http://purl.obolibrary.org/obo/ARO_3003716 CPS-1 http://purl.obolibrary.org/obo/ARO_3004221 CPS beta-lactamase CPS-1 is a subclass B3 metallo-beta lactamase isolated from Chyseobacterium piscium exhibiting carbapenem resistance. http://purl.obolibrary.org/obo/ARO_3003717 ESP-1 http://purl.obolibrary.org/obo/ARO_3004222 ESP beta-lactamase ESP-1 is a subclass B3 metallo-beta lactamase isolated from Epilithonimonas tenax conferring resistance to carbapenems. http://purl.obolibrary.org/obo/ARO_3003718 MSI-1 http://purl.obolibrary.org/obo/ARO_3004223 MSI beta-lactamase MSI-1 is a subclass B3 metallo-beta lactamase isolated from Massilia oculi conferring resistance to carbapenems. http://purl.obolibrary.org/obo/ARO_3003719 MSI-OXA http://purl.obolibrary.org/obo/ARO_3004242 MSI-OXA family beta-lactamase MSI-OXA is an OXA-85-like class D beta lactamase isolated from Massilia oculi. http://purl.obolibrary.org/obo/ARO_3003720 SPG-1 http://purl.obolibrary.org/obo/ARO_3004224 SPG beta-lactamase SPG-1 is a subclass B3 metallo-beta lactamase isolated from Sphingomonas sp. http://purl.obolibrary.org/obo/ARO_3003722 glycopeptide resistance gene cluster VanI http://purl.obolibrary.org/obo/ARO_3000234 glycopeptide resistance gene cluster This inducible cluster confers high resistance to vancomycin and intermediate resistance to teicoplanin. It achieves this through peptidoglycan restructuring with its VanA ligase homologue, VanI, causing the precursurs to end in D-Ala-D-Lac. The cluster uniquely contains murF, the final enzyme in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein. The VanI gene cluster has been found in chromosomal DNA. Gene orientation: vanSRIWK-murFvanX. http://purl.obolibrary.org/obo/ARO_3003723 vanI http://purl.obolibrary.org/obo/ARO_3002978 D-Ala-D-Lac ligase VanI is a D-Ala-D-Lac ligase that reduces vancomycin binding affinity, helping to confer vancomycin resistance as part of the VanI resistance gene cluster in Desulfitobacterium spp. and Desulfosporosinus spp. http://purl.obolibrary.org/obo/ARO_3003724 vanW gene in vanI cluster http://purl.obolibrary.org/obo/ARO_3000002 vanW Also known as vanWI, is a vanW variant found in the vanI gene cluster. http://purl.obolibrary.org/obo/ARO_3003725 vanX gene in vanI cluster http://purl.obolibrary.org/obo/ARO_3000011 vanX Also known as vanXI, is a vanX variant found in the vanI glycopeptide resistance gene cluster. It is a D-Ala-D-Ala dipeptidase. http://purl.obolibrary.org/obo/ARO_3003726 vanS gene in vanI cluster http://purl.obolibrary.org/obo/ARO_3000071 vanS Also known as vanSI, is a vanS variant found in the vanI gene cluster; it is a histidine kinase. http://purl.obolibrary.org/obo/ARO_3003727 vanK gene in vanI cluster http://purl.obolibrary.org/obo/ARO_3002915 vanK Also known as vanKI, is a peptidoglycan bridge formation protein also known as FemAB that is part of the vanI glycopeptide resistance gene cluster. http://purl.obolibrary.org/obo/ARO_3003728 vanR gene in vanI cluster http://purl.obolibrary.org/obo/ARO_3000574 vanR Also known as vanRI, is the regulatory transcriptional activator in the vanSR regulator within the vanI glycopeptide resistance gene cluster. http://purl.obolibrary.org/obo/ARO_3003729 Staphylococcus aureus ileS with mutation conferring resistance to mupirocin http://purl.obolibrary.org/obo/ARO_3000446 antibiotic-resistant isoleucyl-tRNA synthetase (ileS) Point mutations to the isoleucyl-tRNA synthetase (ileS) in Staphylococcus aureus that confer resistance to mupirocin. http://purl.obolibrary.org/obo/ARO_3003730 Bifidobacterium bifidum ileS conferring resistance to mupirocin http://purl.obolibrary.org/obo/ARO_3000446 antibiotic-resistant isoleucyl-tRNA synthetase (ileS) Bifidobacteria have an intrinsically resistant form of ileS (isoleucyl-tRNA synthetase) that confers resistance to mupirocin. http://purl.obolibrary.org/obo/ARO_3003731 fusD http://purl.obolibrary.org/obo/ARO_3005086 Target protecting FusB-type protein conferring resistance to Fusidic acid A specific fusidic acid resistance gene conferring intrinsic resistance in the bacteria Staphylococcus saprophyticus. FusD behaves by causing dissociation of EF-G from the ribosome thus counteracting the action of Fusidic acid. It is considered a FusB-type protein. http://purl.obolibrary.org/obo/ARO_3003733 fusC http://purl.obolibrary.org/obo/ARO_3005086 Target protecting FusB-type protein conferring resistance to Fusidic acid FusC is a fusidic acid resistance gene enabling ribosomal translocase EF-G dissociation from the ribosome that has been detected in Staphylococcus aureus and Staphylococcus intermedius. Its mechanism is believed to be similar to fusB due to its high level of sequence homology. It is considered a FusB-type protein. http://purl.obolibrary.org/obo/ARO_3003734 antibiotic resistant fusA http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Antibiotic resistant fusA is caused by mutations to the elongation factor G (EF-G) and confers resistance to fusidic acid. http://purl.obolibrary.org/obo/ARO_3003735 Staphylococcus aureus fusA with mutation conferring resistance to fusidic acid http://purl.obolibrary.org/obo/ARO_3003734 antibiotic resistant fusA The mutations to this gene are involved in altering the translation elongation factor G (EF-G) in association with the ribosome to prevent fusidic acid from binding EF-G and preventing translation. http://purl.obolibrary.org/obo/ARO_3003736 antibiotic resistant fusE http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Antibiotic resistant fusE is caused by mutations in a region of the rplF gene encoding riboprotein L6, and confers resistance to fusidic acid. http://purl.obolibrary.org/obo/ARO_3003737 Staphylococcus aureus fusE with mutation conferring resistance to fusidic acid http://purl.obolibrary.org/obo/ARO_3003736 antibiotic resistant fusE The mutations to the rplF gene encoding riboprotein L6 have been shown to cause fusidic acid resistance, demonstrating a potential secondary site of action of the antibiotic that is blocked through these mutations. Several types of mutations have been identified that cause resistance, including SNPs, frameshift mutations and early stop codons. http://purl.obolibrary.org/obo/ARO_3003741 mphE http://purl.obolibrary.org/obo/ARO_3000333 macrolide phosphotransferase (MPH) mphE is a macrolide phosphotransferase and resistance gene identified on a plasmid, pRSB105. http://purl.obolibrary.org/obo/ARO_3003742 mphG http://purl.obolibrary.org/obo/ARO_3000333 macrolide phosphotransferase (MPH) The mphG gene encodes a macrolide 2'-phosphotransferase found in Photobacterium damselae sharing sequence similarity to mphA in E. coli. http://purl.obolibrary.org/obo/ARO_3003744 vatF http://purl.obolibrary.org/obo/ARO_3000453 streptogramin vat acetyltransferase vatF is a streptogramin A acetyl transferase gene isolated from the chromosome of Yersinia enterocolitica. http://purl.obolibrary.org/obo/ARO_3003745 mef(C) http://purl.obolibrary.org/obo/ARO_3000747 mef mef(C) is a macrolide efflux gene isolated from a plasmid in Photobacterium damselae. http://purl.obolibrary.org/obo/ARO_3003746 optrA http://purl.obolibrary.org/obo/ARO_3007068 Miscellaneous ABC-F subfamily ATP-binding cassette ribosomal protection proteins OptrA is a member of the ABC-F protein subfamily that confers resistance to oxazolidinones. The gene encoding the protein was originally isolated from a plasmid in Enterococcus faecalis and Enterococcus faecium. http://purl.obolibrary.org/obo/ARO_3003748 oleC http://purl.obolibrary.org/obo/ARO_0010001 ATP-binding cassette (ABC) antibiotic efflux pump oleC is an ABC transporter isolated from Streptomyces antibioticus and is involved in oleandomycin secretion. http://purl.obolibrary.org/obo/ARO_3003749 salA http://purl.obolibrary.org/obo/ARO_3007030 sal-type ABC-F protein salA is an ABC-F subfamily protein gene isolated from the chromosome of Mammaliicoccus sciuri conferring resistance to lincosamides and streptogramins. http://purl.obolibrary.org/obo/ARO_3003751 Escherichia coli nfsA mutations conferring resistance to nitrofurantoin http://purl.obolibrary.org/obo/ARO_3003754 antibiotic resistant nfsA nfsA encodes the major oxygen-insesitive nitroreductase in E. coli. The first step of resistance to nitrofurazone is mutation of nfsA. http://purl.obolibrary.org/obo/ARO_3003754 antibiotic resistant nfsA http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant The nfsA-encoded nitroreductase is the major oxygen-insensitive nitroreductase present in E. coli. NfsA uses only NADPH and has broad electron acceptor specificity. Mutations in nfsA cause resistance to nitrofurazone and furazolidone. Resistance to nitrofurantoin via mutation of nfsA reduces the fitness of clinical isolates of E. coli. http://purl.obolibrary.org/obo/ARO_3003755 Antibiotic resistant nfsB http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant The nsfB gene encodes a minor oxygen-insensitive nitroreductase. NfsB reduces a broad range of nitroaromatic compounds including the antibiotics nitrofurazone and nitrofurantoin. NfsB is a flavin mononucleotide (FMN)-containing protein and uses both NADH and NADPH as a source of reducing equivalents. Mutations in nfsB lead to increased resistance to nitrofurazone and furazolidone in an nfsA mutant background. http://purl.obolibrary.org/obo/ARO_3003756 Escherichia coli nfsB with mutation conferring resistance to nitrofurantoin http://purl.obolibrary.org/obo/ARO_3003755 Antibiotic resistant nfsB nfsB encodes the minor oxygen-insesitive nitroreductase in E. coli. The first step of resistance to nitrofurazone is mutation of nfsA, while the increased resistance associated with second step mutants is a consequence of nfsB mutation. http://purl.obolibrary.org/obo/ARO_3003760 Enterococcus faecalis cls with mutation conferring resistance to daptomycin http://purl.obolibrary.org/obo/ARO_3003272 daptomycin resistant cls Cardiolipin synthase (cls) is an inner membrane protein involved in membrane synthesis and phosopholipid metabolism, with mutations to the gene being capable of conferring daptomycin resistance. http://purl.obolibrary.org/obo/ARO_3003761 eatAv http://purl.obolibrary.org/obo/ARO_3007068 Miscellaneous ABC-F subfamily ATP-binding cassette ribosomal protection proteins eatAv is a mutated form of the wildtype eatA ABC-F subfamily protein isolated from Enterococcus faecium conferring resistance to lincosamides, streptogramin A's and pleuromutilins (LSaP phenotype). http://purl.obolibrary.org/obo/ARO_3003762 lnuE http://purl.obolibrary.org/obo/ARO_3000221 lincosamide nucleotidyltransferase (LNU) lnuE encodes a lincosamide resistance gene isolated from Streptococcus suis that was truncated by an ISEnfa5-cfr-ISEnfa5 segment insertion. It shares the closest sequence similarity to lnuA. http://purl.obolibrary.org/obo/ARO_3003764 resistance by absence http://purl.obolibrary.org/obo/ARO_1000002 mechanism of antibiotic resistance Mechanism of antibiotic resistance conferred by deletion of gene (usually a porin). http://purl.obolibrary.org/obo/ARO_3003767 mphM http://purl.obolibrary.org/obo/ARO_3000333 macrolide phosphotransferase (MPH) mphM is a chromosomally-encoded macrolide phosphotransferases that inactivate 14-, 15- and 16-membered macrolides. http://purl.obolibrary.org/obo/ARO_3003768 gene conferring resistance via absence http://purl.obolibrary.org/obo/ARO_3000000 determinant of antibiotic resistance Deletion of gene or gene product results in resistance. For example, deletion of a porin gene blocks drug from entering the cell. http://purl.obolibrary.org/obo/ARO_3003769 Staphylococcus aureus mprF http://purl.obolibrary.org/obo/ARO_3000863 defensin resistant mprF MprF is a integral membrane protein that modifies the negatively-charged phosphatidylglycerol on the membrane surface. A point mutation in the putative mprF synthase domain is associated with enhanced expression, increased synthesis and reduced daptomycin surface binding. This confers resistance to cationic peptides that disrupt the cell membrane, including defensins. http://purl.obolibrary.org/obo/ARO_3003770 Listeria monocytogenes mprF http://purl.obolibrary.org/obo/ARO_3000863 defensin resistant mprF MprF is a integral membrane protein that modifies the negatively-charged phosphatidylglycerol on the membrane surface. This confers resistance to cationic peptides that disrupt the cell membrane, including defensins. http://purl.obolibrary.org/obo/ARO_3003772 Brucella suis mprF http://purl.obolibrary.org/obo/ARO_3000863 defensin resistant mprF MprF is a integral membrane protein that modifies the negatively-charged phosphatidylglycerol on the membrane surface. This confers resistance to cationic peptides that disrupt the cell membrane, including defensins. http://purl.obolibrary.org/obo/ARO_3003773 Clostridium perfringens mprF http://purl.obolibrary.org/obo/ARO_3000863 defensin resistant mprF MprF is a integral membrane protein that modifies the negatively-charged phosphatidylglycerol on the membrane surface. This confers resistance to cationic peptides that disrupt the cell membrane, including defensins. http://purl.obolibrary.org/obo/ARO_3003774 Streptococcus agalactiae mprF http://purl.obolibrary.org/obo/ARO_3000863 defensin resistant mprF MprF is a integral membrane protein that modifies the negatively-charged phosphatidylglycerol on the membrane surface. This confers resistance to cationic peptides that disrupt the cell membrane, including defensins. http://purl.obolibrary.org/obo/ARO_3003775 Escherichia coli murA with mutation conferring resistance to fosfomycin http://purl.obolibrary.org/obo/ARO_3002811 antibiotic-resistant murA transferase murA or UDP-N-acetylglucosamine enolpyruvyl transferase catalyses the initial step in peptidoglycan biosynthesis and is inhibited by fosfomycin. Overexpression of murA through mutations such as Asp369Asn and Leu370Ile confers fosfomycin resistance. Extensive evidence has shown the significance of C115 mutations in conferring fosfomycin resistance since this residue represents a primary binding site for the antibiotic across many species. http://purl.obolibrary.org/obo/ARO_3003776 Staphylococcus aureus murA with mutation conferring resistance to fosfomycin http://purl.obolibrary.org/obo/ARO_3002811 antibiotic-resistant murA transferase murA or UDP-N-acetylglucosamine enolpyruvyl transferase catalyses the initial step in peptidoglycan biosynthesis and is inhibited by fosfomycin. Overexpression of murA through mutations confers fosfomycin resistance. http://purl.obolibrary.org/obo/ARO_3003777 Borreliella burgdorferi murA with mutation conferring resistance to fosfomycin http://purl.obolibrary.org/obo/ARO_3002811 antibiotic-resistant murA transferase murA or UDP-N-acetylglucosamine enolpyruvyl transferase catalyses the initial step in peptidoglycan biosynthesis and is inhibited by fosfomycin. Mutations to the murA enzyme confers resistance to the antibiotic. http://purl.obolibrary.org/obo/ARO_3003778 Mycolicibacterium smegmatis ndh with mutation conferring resistance to isoniazid http://purl.obolibrary.org/obo/ARO_3003460 antibiotic resistant ndh Mutations in the Mycolicibacterium smegmatis ndh gene that results in increased resistance to isoniazid. http://purl.obolibrary.org/obo/ARO_3003779 Mycobacterium tuberculosis variant bovis ndh with mutation conferring resistance to isoniazid http://purl.obolibrary.org/obo/ARO_3003460 antibiotic resistant ndh Mutations in the Mycobacterium tuberculosis variant bovis ndh gene that results in increased resistance to isoniazid. http://purl.obolibrary.org/obo/ARO_3003780 nybomycin http://purl.obolibrary.org/obo/ARO_3007157 nybomycin-like antibiotic A heterocyclic antibiotic that targets mutant gyrA (type II topoisomerase) containing an S84L substitution, counteracting acquired quinolone resistance. It is effective against quinolone-resistant Gram-positive bacteria including S. aureus and E. faecalis. Due to its ability to counteract quinolone resistance by targeting the mutant form of the gyrA protein, it is classified as a reverse antibiotic (RA). http://purl.obolibrary.org/obo/ARO_3003784 Mycobacterium tuberculosis intrinsic murA conferring resistance to fosfomycin http://purl.obolibrary.org/obo/ARO_3002811 antibiotic-resistant murA transferase Mycobacterium tuberculosis murA confers intrinsic resistance to fosfomycin. The presence of an aspartic acid residue in place of the critical cysteine at position 117 that enables fosfomycin binding is believed to be responsible for this intrinsic resistance. http://purl.obolibrary.org/obo/ARO_3003785 Chlamydia trachomatis intrinsic murA conferring resistance to fosfomycin http://purl.obolibrary.org/obo/ARO_3002811 antibiotic-resistant murA transferase Chlamydia murA confers intrinsic resistance to fosfomycin. The presence of an aspartic acid residue in place of the critical cysteine at position 119 that enables fosfomycin binding is believed to be responsible for this intrinsic resistance. http://purl.obolibrary.org/obo/ARO_3003786 fluoroquinolone self resistant parC http://purl.obolibrary.org/obo/ARO_3000492 gene involved in self-resistance to antibiotic Inherent parC resistance to fluoroquinolone from an antibiotic producer. The presence of these genes confers self-resistance to the antibiotic it produces. http://purl.obolibrary.org/obo/ARO_3003787 aminocoumarin self resistant parY http://purl.obolibrary.org/obo/ARO_3000492 gene involved in self-resistance to antibiotic Inherent ParY resistant to aminocoumarin from an antibiotic producer. The presence of these genes confers self resistance to the antibiotic it produces. http://purl.obolibrary.org/obo/ARO_3003788 Bacillus subtilis pgsA with mutation conferring resistance to daptomycin http://purl.obolibrary.org/obo/ARO_3003080 daptomycin resistant pgsA Point mutations that occur within the Bacillus subtilis pgsA gene resulting in resistance to daptomycin. http://purl.obolibrary.org/obo/ARO_3003789 Campylobacter jejuni gyrA conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3003292 fluoroquinolone resistant gyrA Campylobacter jejuni is a major bacterial infectious agent associated with gastroenteritis. Quinolone resistance is reportedly conferred by a single C-257-T nucleotide substitution in the gyrA gene. http://purl.obolibrary.org/obo/ARO_3003790 Enterococcus faecium liaF mutant conferring daptomycin resistance http://purl.obolibrary.org/obo/ARO_3004262 daptomycin resistant liaF liaF is an accessory protein that acts as a negative regulator of liaRS signal transduction pathway. Mutations confer daptomycin resistance. http://purl.obolibrary.org/obo/ARO_3003791 Enterococcus faecalis liaS mutant conferring daptomycin resistance http://purl.obolibrary.org/obo/ARO_3004264 daptomycin resistant liaS liaS is a histidine kinase found in the liaFSR signal transduction pathway. Mutations confer daptomycin resistance. http://purl.obolibrary.org/obo/ARO_3003792 Enterococcus faecalis liaR mutant conferring daptomycin resistance http://purl.obolibrary.org/obo/ARO_3004263 daptomycin resistant liaR liaR is a response regulator found in the liaFSR signal transduction pathway. Mutations confer daptomycin resistance. http://purl.obolibrary.org/obo/ARO_3003793 SPM-1 http://purl.obolibrary.org/obo/ARO_3000580 SPM beta-lactamase Plasmid-mediated SPM metallo-beta-lactamase conferring resistance to carbapenem. Originally isolated from Pseudomonas aeruginosa. Responsible for carbapenem-resistant Pseudomonas aeruginosa (CRPA) outbreaks in Brazil. http://purl.obolibrary.org/obo/ARO_3003794 Staphylococcus aureus walK with mutation conferring resistance to daptomycin http://purl.obolibrary.org/obo/ARO_3003795 daptomycin resistant walK walK is the histidine kinase sensor of a two-component regulatory system controlling peptidoglycan metabolism through regulation of the expression of most of the peptidoglycan hydrolase genes. Mutations in the gene have been found that confer daptomycin resistance. http://purl.obolibrary.org/obo/ARO_3003795 daptomycin resistant walK http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations to the walK gene, part of a cell wall metabolism 2-component regulatory system, confers resistance to antibiotics, specifically daptomycin. http://purl.obolibrary.org/obo/ARO_3003796 Acinetobacter baumannii ampC beta-lactamase http://purl.obolibrary.org/obo/ARO_3004232 ampC-type beta-lactamase A class C beta-lactamase found in Acinetobacter baumannii that confers resistance to piperacillin and cefepime. http://purl.obolibrary.org/obo/ARO_3003797 Enterococcus faecalis YybT with mutation conferring daptomycin resistance http://purl.obolibrary.org/obo/ARO_3003798 daptomycin resistant YybT YybT has phosphodiesterase activity towards cyclic dinucleotides using a c-di-GMP hydrolyzing phosphodiesterase domain. Mutations to the gene confer resistance to daptomycin. http://purl.obolibrary.org/obo/ARO_3003798 daptomycin resistant YybT http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations to the YybT gene confers daptomycin resistance. http://purl.obolibrary.org/obo/ARO_3003800 Enterococcus faecalis gdpD with mutation conferring daptomycin resistance http://purl.obolibrary.org/obo/ARO_3003802 daptomycin resistant gdpD gdpD is a glycerolphosphodiesterase whose mutations confer resistance to daptomycin. http://purl.obolibrary.org/obo/ARO_3003801 bcr-1 http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump Transmembrane protein which expels bicyclomycin from the cell, leading to bicyclomycin resistance. Identified in Pseudomonas aeruginosa strains responsible for outbreaks in Brazil, often appearing with blaSPM-1, another bicyclomycin resistance gene. http://purl.obolibrary.org/obo/ARO_3003802 daptomycin resistant gdpD http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations to the gdpD glycerolphosphodiesterase confer resistance to daptomycin. http://purl.obolibrary.org/obo/ARO_3003803 Staphylococcus aureus agrA with mutation conferring resistance to daptomycin http://purl.obolibrary.org/obo/ARO_3003804 daptomycin resistant agrA agrA is an autoinducer in a peptide-quorum two-component regulatory system whose mutations confer daptomycin resistance. http://purl.obolibrary.org/obo/ARO_3003804 daptomycin resistant agrA http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations to the regulatory gene agrA confer daptomycin resistance. http://purl.obolibrary.org/obo/ARO_3003805 Enterococcus faecalis gshF with mutation conferring daptomycin resistance http://purl.obolibrary.org/obo/ARO_3003806 daptomycin resistant gshF gshF is a bifunctional glutamate-cysteine ligase/ glutathione synthetase that when mutated, confers daptomycin resistance. http://purl.obolibrary.org/obo/ARO_3003806 daptomycin resistant gshF http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations to the glutathione synthetase gshF confers daptomycin resistance. http://purl.obolibrary.org/obo/ARO_3003807 Escherichia coli AcrAB-TolC with AcrR mutation conferring resistance to ciprofloxacin, tetracycline, and ceftazidime http://purl.obolibrary.org/obo/ARO_3000702 acrR AcrR is a repressor of the AcrAB-TolC multidrug efflux complex. AcrR mutations result in high level antibiotic resistance. The mutations associated with this model are specific to E. coli. http://purl.obolibrary.org/obo/ARO_3003808 carO http://purl.obolibrary.org/obo/ARO_3003768 gene conferring resistance via absence carO is a transmembrane beta-barrel involved in the influx of carbapenem antibiotics in Acinetobacter baumannii. Disruption of the carO gene by distinct insertion elements results in a loss of carO expression causing resistance to carbapenem antibiotics. Homologs of carO have been identified in genera Acinetobacter, Moraxella and Psychrobacter. http://purl.obolibrary.org/obo/ARO_3003809 Acinetobacter baumannii OprD conferring resistance to imipenem http://purl.obolibrary.org/obo/ARO_3003768 gene conferring resistance via absence An outer member protein (OMP) found in Acinetobacter baumannii involved in the uptake of imipenem and basic amino acids. This porin is homologous to Pseudomonas aeruginosa OprD, which performs an identical function. http://purl.obolibrary.org/obo/ARO_3003810 kirromycin self resistant EF-Tu http://purl.obolibrary.org/obo/ARO_3000492 gene involved in self-resistance to antibiotic Natural producers of kirromycin and kirromycin-like antibiotics (i.e., kirrothrycin) possess self-resistance, which is classified here. http://purl.obolibrary.org/obo/ARO_3003811 adeC http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance AdeC is the outer membrane factor of the AdeABC multidrug efflux complex. It can be replaced by other outer membrane channels, and is not essential for antibiotic resistance. http://purl.obolibrary.org/obo/ARO_3003813 Enterococcus faecalis drmA with mutation conferring daptomycin resistance http://purl.obolibrary.org/obo/ARO_3003814 daptomycin resistant drmA drmA is an uncharacterized 6-pass membrane protein, with mutations to the protein causing modest resistance to daptomycin. http://purl.obolibrary.org/obo/ARO_3003814 daptomycin resistant drmA http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations to drmA confer daptomycin resistance. http://purl.obolibrary.org/obo/ARO_3003815 Enterococcus faecalis YvlB with mutation conferring daptomycin resistance http://purl.obolibrary.org/obo/ARO_3003816 daptomycin resistant YvlB YvlB is a putative target of the liaFSR signalling pathway, whose mutations confer daptomycin resistance. http://purl.obolibrary.org/obo/ARO_3003816 daptomycin resistant YvlB http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations to the putative liaFSR target YvlB confer daptomycin resistance. http://purl.obolibrary.org/obo/ARO_3003817 Acinetobacter baumannii gyrA conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3003292 fluoroquinolone resistant gyrA Mutations in the A subunit of DNA gyrase reduce its affinity for fluoroquinolones, thereby conferring resistance. http://purl.obolibrary.org/obo/ARO_3003818 Acinetobacter baumannii parC conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3000619 fluoroquinolone resistant parC Mutations in Acinetobacter baumannii parC that result in resistance to fluoroquinolones. http://purl.obolibrary.org/obo/ARO_3003820 mgrB http://purl.obolibrary.org/obo/ARO_3007684 transmembrane protein conferring colistin resistance mgrB is a small transmembrane protein produced in the PhoPQ signalling system. It acts as a negative regulator in this system. Inactivation or down-regulation of mgrB confers colistin resistance by absence as shown in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3003821 BAL30072 http://purl.obolibrary.org/obo/ARO_0000004 monobactam BAL30072 is a monocyclic beta-lactam antibiotic belonging to the sulfactams. BAL30072 was found to trigger the spheroplasting and lysis of Escherichia coli rather than the formation of extensive filaments. http://purl.obolibrary.org/obo/ARO_3003822 battacin http://purl.obolibrary.org/obo/ARO_3000035 lipopeptide antibiotic Battacin is a cationic lipopeptide antibiotic produced from a Paenibacillus tianmuensis soil isolate. Battacin kills bacteria in vitro and has potent activity against Gram-negative bacteria, including multidrug-resistant and extremely drug-resistant clinical isolates. The bactericidal kinetics of battacin correlate with the depolarization of the cell membrane, suggesting that battacin kills bacteria by disrupting the cytoplasmic membrane. http://purl.obolibrary.org/obo/ARO_3003823 benzalkonium chloride http://purl.obolibrary.org/obo/ARO_3005386 disinfecting agents and antiseptics Benzalkonium chloride is a type of cationic surfactant. It is an organic salt called a quaternary ammonium compound. It has three main categories of use: as a biocide, a cationic surfactant, and as a phase transfer agent. http://purl.obolibrary.org/obo/ARO_3003830 Aminocoumarin resistant alaS http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant An alanyl-tRNA synthetase conferring resistance to novobiocin in Escherichia coli. Sequence data unavailable. http://purl.obolibrary.org/obo/ARO_3003831 temocillin http://purl.obolibrary.org/obo/ARO_3009123 penicillin with extended spectrum Temocillin is a beta-lactamase resistant carboxypenicillin. It is primarily used for the treatment of multiple drug resistant, Gram-negative bacteria, specifically Enterobacteriaceae. http://purl.obolibrary.org/obo/ARO_3003832 ticarcillin http://purl.obolibrary.org/obo/ARO_3009123 penicillin with extended spectrum Ticarcillin is a carboxypenicillin used for the treatment of Gram-negative bacteria, particularly P. aeruginosa. Ticarcillin's antibiotic properties arise from its ability to prevent cross-linking of peptidoglycan during cell wall synthesis, when the bacteria try to divide, causing cell death. http://purl.obolibrary.org/obo/ARO_3003835 cdeA http://purl.obolibrary.org/obo/ARO_3000112 multidrug and toxic compound extrusion (MATE) transporter Clostridioides difficile and Escherichia coli multidrug efflux transporter with antiporter function. Confers resistance to fluoroquinolones in E. coli and acriflavin in Clostridioides difficile. http://purl.obolibrary.org/obo/ARO_3003836 qacH http://purl.obolibrary.org/obo/ARO_0010003 small multidrug resistance (SMR) antibiotic efflux pump qacH is a subunit of the qac multidrug efflux pump in Staphylococcus saprophyticus. http://purl.obolibrary.org/obo/ARO_3003838 gadW http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux GadW is an AraC-family regulator that promotes mdtEF expression to confer multidrug resistance. GadW inhibits GadX-dependent activation. GadW clearly represses gadX and, in situations where GadX is missing, activates gadA and gadBC. http://purl.obolibrary.org/obo/ARO_3003839 Mrx http://purl.obolibrary.org/obo/ARO_3000333 macrolide phosphotransferase (MPH) Mrx is part of the macrolide inactivation gene cluster in Aeromonas hydrophila. http://purl.obolibrary.org/obo/ARO_3003840 aminocoumarin resistant cysB http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Positive regulator of gene expression in the cysteine regulon. cysB mutants confer resistance to novobiocin, an aminocoumarin antibiotic, in Escherichia coli. Sequence data unavailable. http://purl.obolibrary.org/obo/ARO_3003841 kdpE http://purl.obolibrary.org/obo/ARO_3000750 protein of two-component regulatory system modulating antibiotic efflux kdpE is a transcriptional activator that is part of the two-component system KdpD/KdpE that is studied for its regulatory role in potassium transport and has been identified as an adaptive regulator involved in the virulence and intracellular survival of pathogenic bacteria. kdpE regulates a range of virulence loci through direct promoter binding. http://purl.obolibrary.org/obo/ARO_3003842 MUS-2 http://purl.obolibrary.org/obo/ARO_3004067 MUS beta-lactamase MUS-2 is a chromosome-encoded beta-lactamase from Myroides odoratimimus. http://purl.obolibrary.org/obo/ARO_3003843 leuO http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux leuO, a LysR family transcription factor, exists in a wide variety of bacteria of the family Enterobacteriaceae and is involved in the regulation of as yet unidentified genes affecting the stress response and pathogenesis expression. LeuO is also an activator of the MdtNOP efflux pump. http://purl.obolibrary.org/obo/ARO_3003844 mfd http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) mfd dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. The Mfd (mutation frequency decline) protein, also known as transcription-repair coupling factor, is responsible for ATP-dependent removal of stalled RNA polymerase from DNA lesions by inducing forward movement of the RNA polymerase and subsequent recruitment of nucleotide excision repair machinery to the sites of the lesions. http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity http://purl.obolibrary.org/obo/ARO_3005459 ADC beta-lactamase ADC beta-lactamases, also known as AmpC beta-lactamases, are cephalosporinases with extended-spectrum resistance to cephalosporins but not to carbapenems. ADC beta-lactamases are found in Acinetobacter sp. and Oligella urethralis. http://purl.obolibrary.org/obo/ARO_3003847 ADC-1 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-1 is a beta-lactamase found in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3003848 ADC-2 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-2 is a beta-lactamase found in Oligella urethralis. http://purl.obolibrary.org/obo/ARO_3003849 ADC-3 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-3 is a beta-lactamase found in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3003850 ADC-4 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-4 is a beta-lactamase found in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3003851 ADC-5 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-5 is a beta-lactamase found in Acinetobacter pittii. http://purl.obolibrary.org/obo/ARO_3003852 ADC-6 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-6 is a beta-lactamase found in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3003853 ADC-7 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-7 is a beta-lactamase that is found in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3003854 ADC-8 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-8 is a beta-lactamase found in Acinetobacter sp. http://purl.obolibrary.org/obo/ARO_3003856 ADC-12 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-12 is a beta-lactamase found in Acinetobacter pittii. http://purl.obolibrary.org/obo/ARO_3003857 ADC-13 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-13 is a beta-lactamase found in Acinetobacter pittii. http://purl.obolibrary.org/obo/ARO_3003858 ADC-14 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-14 is a beta-lactamase found in Acinetobacter pittii. http://purl.obolibrary.org/obo/ARO_3003859 ADC-15 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-15 is a beta-lactamase found in Acinetobacter pittii. http://purl.obolibrary.org/obo/ARO_3003860 ADC-16 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-16 is a beta-lactamase found in Acinetobacter pittii. http://purl.obolibrary.org/obo/ARO_3003861 ADC-17 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-17 is a beta-lactamase found in Acinetobacter pittii. http://purl.obolibrary.org/obo/ARO_3003862 ADC-18 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-18 is a beta-lactamase found in Acinetobacter pittii. http://purl.obolibrary.org/obo/ARO_3003863 ADC-19 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-19 is a beta-lactamase found in Acinetobacter pittii. http://purl.obolibrary.org/obo/ARO_3003864 ADC-20 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-20 is a beta-lactamase found in Acinetobacter pittii. http://purl.obolibrary.org/obo/ARO_3003865 ADC-21 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-21 is a beta-lactamase found in Acinetobacter pittii. http://purl.obolibrary.org/obo/ARO_3003866 ADC-22 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-22 is a beta-lactamase found in Acinetobacter pittii. http://purl.obolibrary.org/obo/ARO_3003867 ADC-23 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-23 is a beta-lactamase found in Acinetobacter pittii. http://purl.obolibrary.org/obo/ARO_3003868 ADC-25 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-25 is a beta-lactamase found in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3003870 ADC-31 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-31 is a beta-lactamase found in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3003871 ADC-39 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-39 is a beta-lactamase found in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3003872 ADC-41 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-41 is a beta-lactamase found in Acinetobacter pittii. http://purl.obolibrary.org/obo/ARO_3003873 ADC-42 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-42 is a beta-lactamase found in Acinetobacter pittii. http://purl.obolibrary.org/obo/ARO_3003874 ADC-43 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-43 is a beta-lactamase found in Acinetobacter pittii. http://purl.obolibrary.org/obo/ARO_3003875 Enterococcus faecium EF-Tu mutants conferring resistance to elfamycin http://purl.obolibrary.org/obo/ARO_3001312 elfamycin resistant EF-Tu Sequence variants of Enterococcus faecium elongation factor Tu that confer resistance to elfamycin antibiotics. http://purl.obolibrary.org/obo/ARO_3003876 ADC-44 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-44 is a beta-lactamase found in Acinetobacter pittii. http://purl.obolibrary.org/obo/ARO_3003878 ADC-56 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-56 is a beta-lactamase found in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3003879 ADC-61 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-61 is a beta-lactamase found in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3003880 ADC-74 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-74 is a beta-lactamase found in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3003881 ADC-75 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-75 is a beta-lactamase found in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3003882 ADC-76 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-76 is a beta-lactamase found in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3003883 ADC-77 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-77 is a beta-lactamase found in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3003884 ADC-78 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-78 is a beta-lactamase found in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3003885 ADC-79 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-79 is a beta-lactamase found in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3003886 ADC-80 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-80 is a beta-lactamase found in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3003887 ADC-81 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-81 is a beta-lactamase found in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3003888 ADC-82 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-82 is a beta-lactamase found in Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3003889 Escherichia coli GlpT with mutation conferring resistance to fosfomycin http://purl.obolibrary.org/obo/ARO_3004247 antibiotic-resistant GlpT Point mutations to the active importer GlpT, which is involved with the uptake of many phosphorylated sugars, confer resistance to fosfomycin by reducing import of the drug into the bacteria. http://purl.obolibrary.org/obo/ARO_3003890 Escherichia coli UhpT with mutation conferring resistance to fosfomycin http://purl.obolibrary.org/obo/ARO_3004248 antibiotic-resistant UhpT Mutations to the active importer UhpT, which is involved with the uptake of many phosphorylated sugars, confer resistance to fosfomycin by reducing import of the drug into the bacteria. http://purl.obolibrary.org/obo/ARO_3003893 Escherichia coli uhpA with mutation conferring resistance to fosfomycin http://purl.obolibrary.org/obo/ARO_3004249 UhpA uhpA is a positive activator of the fosfomycin importer uhpT, thus mutations to uhpA confer fosfomycin resistance by reducing uhpT expression. Both knockout and amino acid substitution mutations have been found that confer resistance, with the Protein Knockout model describing the large, knockout mutations causing loss of function of the gene, and the Protein Variant model describing the amino acid substitutions. http://purl.obolibrary.org/obo/ARO_3003894 Rm3 http://purl.obolibrary.org/obo/ARO_3004225 Rm3 family beta-lactamase Rm3 is a class B3 metallo-beta-lactamase isolated from a metagenomic soil sample in Yorkshire, United Kingdom, shown to confer resistance to clinically used penicillins, cephalosporins, and carbapenems. http://purl.obolibrary.org/obo/ARO_3003895 Pseudomonas mutant PhoP conferring resistance to colistin http://purl.obolibrary.org/obo/ARO_3000834 phoP Mutations in Pseudomonas aeruginosa PhoP of the two-component PhoPQ regulatory system. Presence of mutation confers resistance to colistin. http://purl.obolibrary.org/obo/ARO_3003896 Pseudomonas mutant PhoQ conferring resistance to colistin http://purl.obolibrary.org/obo/ARO_3000835 phoQ Mutations in Pseudomonas aeruginosa PhoQ of the two-component PhoPQ regulatory system. Presence of mutation confers resistance to colistin. http://purl.obolibrary.org/obo/ARO_3003897 tedizolid http://purl.obolibrary.org/obo/ARO_3000079 oxazolidinone antibiotic Tedizolid is a synthetic oxazolidinone antibiotic that is administered to the patient as a prodrug that is activated in vivo. It acts as an inhibitor of protein synthesis by binding the 50S subunit of the ribosome and preventing formation of the 70S initiation complex. It is active against Gram-positive pathogens. http://purl.obolibrary.org/obo/ARO_3003898 lugdunin http://purl.obolibrary.org/obo/ARO_3000053 peptide antibiotic Lugdunin is a thiazolidine-containing cyclic peptide antibiotic isolated from nasal Staphylococcus lugnunensis that prohibits Staphylococcus aureus colony formation. It is a human commensal bacteria, indicating the potential for further antibiotic discoveries from human microbiota. http://purl.obolibrary.org/obo/ARO_3003899 Escherichia coli PtsI with mutation conferring resistance to fosfomycin http://purl.obolibrary.org/obo/ARO_3004250 antibiotic-resistant ptsI phosphotransferase PtsI (phosphoenolpyruvate-protein phosphotransferase) is involved in cyclic AMP synthesis, which regulates glpT expression. As a result, mutations to ptsI confer resistance to fosfomycin by affecting the regulation of fosfomycin import. http://purl.obolibrary.org/obo/ARO_3003900 Escherichia coli cyaA with mutation conferring resistance to fosfomycin http://purl.obolibrary.org/obo/ARO_3004251 antibiotic-resistant cya adenylate cyclase CyaA (adenylate cyclase) is involved with the synthesis of cyclic AMP which regulates the fosfomycin transporter glpT. As a result, mutations to cyaA confer resistance to fosfomycin. http://purl.obolibrary.org/obo/ARO_3003901 Staphylococcus aureus GlpT with mutation conferring resistance to fosfomycin http://purl.obolibrary.org/obo/ARO_3004247 antibiotic-resistant GlpT Mutations to the active importer GlpT, which is involved with the uptake of many phosphorylated sugars, confer resistance to fosfomycin by reducing import of the drug into the bacteria. http://purl.obolibrary.org/obo/ARO_3003902 Staphylococcus aureus UhpT with mutation conferring resistance to fosfomycin http://purl.obolibrary.org/obo/ARO_3004248 antibiotic-resistant UhpT Mutations to the active importer UhpT, which is involved with the uptake of many phosphorylated sugars, confer resistance to fosfomycin by reducing import of the drug into the bacteria. http://purl.obolibrary.org/obo/ARO_3003903 thusin http://purl.obolibrary.org/obo/ARO_3000053 peptide antibiotic Thusin is a two-component lantibiotic isolated from B. thuringiensis strain BGSC 4BT1, exhibiting antimicrobial activity against several Gram-positive pathogens. Bacillus cereus, Listeria monocytogenes, Staphylococcus aureus (MRSA), Mammaliicoccus sciuri, Enterococcus faecalis, and Streptococcus pneumoniae have all shown susceptibility to Thusin, with inhibition activities greater than Vancomycin or other lantibiotics. http://purl.obolibrary.org/obo/ARO_3003904 formicin http://purl.obolibrary.org/obo/ARO_3000053 peptide antibiotic Formicin is a two-component broad-spectrum lantibiotic produced by Bacillus paralicheniformis APC 1576, exhibiting antimicrobial activity against several Gram-positive species, including Staphylococcus aureus, Clostridioides difficile and Listeria monocytogenes. http://purl.obolibrary.org/obo/ARO_3003905 ANT(4')-Ib http://purl.obolibrary.org/obo/ARO_3007403 ANT(4')-I Aminoglycoside nucleotidyltransferase sequence from Staphylococcus aureus plasmid. http://purl.obolibrary.org/obo/ARO_3003907 cipA http://purl.obolibrary.org/obo/ARO_3004609 cfr(B) Group Cfr-like methyltransferase enzyme conferring resistance to multiple clinically relevant antibiotic classes. http://purl.obolibrary.org/obo/ARO_3003908 Erm(47) http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase Chromosome-encoded gene conferring MLSB resistance. Identified from Helcococcus kunzii. http://purl.obolibrary.org/obo/ARO_3003915 Lysocin E http://purl.obolibrary.org/obo/ARO_3003919 lysocin A drug which binds to menaquinone in the bacterial cell membrane. Binding of Lysocin to menaquinone facilitates lysis of the cell. http://purl.obolibrary.org/obo/ARO_3003916 menaquinone http://purl.obolibrary.org/obo/ARO_3000710 cell membrane component targeted by antibiotic A molecule involved in electron transport in bacterial cell membrane. http://purl.obolibrary.org/obo/ARO_3003917 Staphylococcus aureus menA with mutation conferring resistance to lysocin http://purl.obolibrary.org/obo/ARO_3004265 lysocin resistant menA menA encodes a 1,4-dihydroxy-2-naphthoate octaprenyltransferase, with mutations to the protein conferring resistance to lysocin E. http://purl.obolibrary.org/obo/ARO_3003918 apmA http://purl.obolibrary.org/obo/ARO_3000341 AAC(2') Plasmid-borne apramycin-resistant aminocyclitol acetyltransferase gene identified from bovine MRSA. http://purl.obolibrary.org/obo/ARO_3003919 lysocin http://purl.obolibrary.org/obo/ARO_3000053 peptide antibiotic Lysocin family of peptide antibiotics isolated from Lysobacter spp. http://purl.obolibrary.org/obo/ARO_3003920 pgpB http://purl.obolibrary.org/obo/ARO_3004287 lipid A phosphatase A gene that produces the protein lipid A 4'-phosphatase. http://purl.obolibrary.org/obo/ARO_3003921 oqxAB http://purl.obolibrary.org/obo/ARO_0010004 resistance-nodulation-cell division (RND) antibiotic efflux pump oqxAB encodes for OqxAB, a plasmid-encoded efflux pump, which confer resistance to multiple agents including fluoroquinolones. http://purl.obolibrary.org/obo/ARO_3003922 oqxA http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance RND efflux pump conferring resistance to fluoroquinolone. http://purl.obolibrary.org/obo/ARO_3003923 oqxB http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance RND efflux pump conferring resistance to fluoroquinolone. http://purl.obolibrary.org/obo/ARO_3003924 Haemophilus parainfluenzae gyrA conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3003292 fluoroquinolone resistant gyrA Point mutation of Haemophilus parainfluenzae gyrA resulted in the lowered affinity between fluoroquinolones and GyrA. Thus, conferring resistance. Both Ser and Tyr are hydrophilic amino acids, however Tyr has an additional bulky hydrophobic group which could affect the interaction between the DNA gyrase with quinolones. http://purl.obolibrary.org/obo/ARO_3003925 Haemophilus parainfluenzae parC conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3000619 fluoroquinolone resistant parC Point mutation of Haemophilus parainfluenzae parC resulted in the lowered affinity between fluoroquinolones and ParC. Thus, conferring resistance. http://purl.obolibrary.org/obo/ARO_3003926 Salmonella enterica gyrA conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3003292 fluoroquinolone resistant gyrA Point mutations in Salmonella gyrA that confer resistance to Nalidixic acid, a fluoroquinolone antibiotic. These mutations have also been shown to reduce susceptibility to ciprofloxacin. http://purl.obolibrary.org/obo/ARO_3003927 ceftolozane http://purl.obolibrary.org/obo/ARO_3009109 other cephalosporins and penems Ceftolozane is a fifth-generation cephalosporin antibiotic developed for the treatment of infections with gram-negative bacteria that have become resistant to conventional antibiotics. http://purl.obolibrary.org/obo/ARO_3003928 Neisseria gonorrhoeae gyrA with mutations conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3003292 fluoroquinolone resistant gyrA Point mutation in Neisseria gonorrhoeae DNA gyrase subunit A. Decreases affinity between fluoroquinolone antibiotic molecule and gyrA, thereby conferring resistance to fluoroquinolone. http://purl.obolibrary.org/obo/ARO_3003929 Neisseria gonorrhoeae parC conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3000619 fluoroquinolone resistant parC Point mutations in Neisseria gonorrhoeae parC protein that confer resistance to fluoroquinolone by reducing affinity to antibiotic binding site. http://purl.obolibrary.org/obo/ARO_3003930 rpsJ http://purl.obolibrary.org/obo/ARO_0000002 tetracycline-resistant ribosomal protection protein rpsJ is a tetracycline resistance protein identified in Neisseria gonorrhoeae. Tetracycline resistance is conferred by binding to the ribosome as a 30S ribosomal protection protein. http://purl.obolibrary.org/obo/ARO_3003931 Capnocytophaga gingivalis gyrA conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3003292 fluoroquinolone resistant gyrA Point mutation in Capnocytophaga gingivalis that decreases binding affinity of fluoroquinolone antibiotics to gyrA, thereby conferring resistance. http://purl.obolibrary.org/obo/ARO_3003932 antibiotic efflux inhibitor http://purl.obolibrary.org/obo/ARO_3007224 adjuvants inhibiting antibiotic removal Compounds and molecules that inhibit the action of antibiotic efflux proteins, thereby decreasing resistance caused by efflux pumps. http://purl.obolibrary.org/obo/ARO_3003933 Berberine http://purl.obolibrary.org/obo/ARO_3003932 antibiotic efflux inhibitor Berberine is a benzylisoquinoline alkaloid shown to reduce MexXY-dependent antibiotic resistance of cephalosporins, macrolides, lincosamides and aminoglycosides in Pseudomonas, Burkholderia and Achromobacter. http://purl.obolibrary.org/obo/ARO_3003936 Omadacycline http://purl.obolibrary.org/obo/ARO_3000050 tetracycline antibiotic An aminomethylcycline antibiotic that targets 16s rRNA in gram positive and gram negative bacteria. http://purl.obolibrary.org/obo/ARO_3003937 Neisseria meningititis PBP2 conferring resistance to beta-lactam http://purl.obolibrary.org/obo/ARO_3003938 Penicillin-binding protein mutations conferring resistance to beta-lactam antibiotics Point mutation in Neisseria meningititis PBP2 (penA) decreases affinity between beta-lactam antibiotic molecule and PBP2, thereby conferring resistance to beta-lactam. http://purl.obolibrary.org/obo/ARO_3003938 Penicillin-binding protein mutations conferring resistance to beta-lactam antibiotics http://purl.obolibrary.org/obo/ARO_3003040 beta-lactam resistant penicillin-binding proteins Mutations in PBP transpeptidases that change the affinity for penicillin thereby conferring resistance to penicillin antibiotics. http://purl.obolibrary.org/obo/ARO_3003939 Salmonella enterica parC conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3000619 fluoroquinolone resistant parC Point mutations in Salmonella parC gene implicated in decreased susceptibility to fluoroquinolone antibiotics, primarily ciprofloxacin and nalidixic acid. http://purl.obolibrary.org/obo/ARO_3003940 Shigella flexneri gyrA conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3003292 fluoroquinolone resistant gyrA Point mutations in Shigella flexneri gyrA observed to confer resistance to fluoroquinolone antibiotics. http://purl.obolibrary.org/obo/ARO_3003941 Shigella flexneri parC conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3000619 fluoroquinolone resistant parC Point mutation in parC conferring resistance to fluoroquinolone antibiotics in Shigella flexneri,. http://purl.obolibrary.org/obo/ARO_3003942 abcA http://purl.obolibrary.org/obo/ARO_0010001 ATP-binding cassette (ABC) antibiotic efflux pump AbcA is a multidrug resistant ABC transporter that confers resistance to methicillin, daptomycin, cefotaxime, and moenomycin. http://purl.obolibrary.org/obo/ARO_3003947 EfrAB http://purl.obolibrary.org/obo/ARO_0010001 ATP-binding cassette (ABC) antibiotic efflux pump EfrAB is a heterodimeric ABC transporter efflux pump found in Enterococcus faecalis and Enterococcus faecium that confers resistance to ciprofloxacin, erythromycin, rifampicin, quinupristine. http://purl.obolibrary.org/obo/ARO_3003948 efrA http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance efrA is a part of the EfrAB efflux pump, and both efrA and efrB are necessary to confer drug resistance. http://purl.obolibrary.org/obo/ARO_3003949 efrB http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance efrB is a part of the EfrAB efflux pump, and both efrA and efrB are necessary to confer multidrug resistance. http://purl.obolibrary.org/obo/ARO_3003950 msbA http://purl.obolibrary.org/obo/ARO_0010001 ATP-binding cassette (ABC) antibiotic efflux pump MsbA is a multidrug resistance transporter homolog from E. coli and belongs to a superfamily of transporters that contain an adenosine triphosphate (ATP) binding cassette (ABC) which is also called a nucleotide-binding domain (NBD). MsbA is a member of the MDR-ABC transporter group by sequence homology. MsbA transports lipid A, a major component of the bacterial outer cell membrane, and is the only bacterial ABC transporter that is essential for cell viability. http://purl.obolibrary.org/obo/ARO_3003951 microcin J25 http://purl.obolibrary.org/obo/ARO_3000053 peptide antibiotic Microcin J25 is a peptide antibiotic that inhibits transcription by bacterial RNA polymerase. MccJ25 is produced by Escherichia coli strains that harbor a plasmid-borne antibiotic-synthesis and antibiotic-export cassette, consisting of a gene for MccJ25 precursor (a 58 residue linear peptide), two genes for factors that process MccJ25 precursor into MccJ25, and one gene for export of MccJ25. http://purl.obolibrary.org/obo/ARO_3003952 YojI http://purl.obolibrary.org/obo/ARO_0010001 ATP-binding cassette (ABC) antibiotic efflux pump YojI mediates resistance to the peptide antibiotic microcin J25 when it is expressed from a multicopy vector. YojI is capable of pumping out microcin molecules. The outer membrane protein TolC in addition to YojI is required for export of microcin J25 out of the cell. Microcin J25 is thus the first known substrate for YojI. http://purl.obolibrary.org/obo/ARO_3003953 hmrM http://purl.obolibrary.org/obo/ARO_3000112 multidrug and toxic compound extrusion (MATE) transporter hmrM is a multidrug efflux pump belonging to the MATE family and functions as a Na+/drug antiporter. http://purl.obolibrary.org/obo/ARO_3003954 efmA http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump efmA is an MFS transporter permease in E. faecium. http://purl.obolibrary.org/obo/ARO_3003955 efpA http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump efpA is an MFS transporter found in Mycobacterium tuberculosis. http://purl.obolibrary.org/obo/ARO_3003956 antibacterial free fatty acids http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule Amongst the diverse and potent biological activities of free fatty acids (FFAs) is the ability to kill or inhibit the growth of bacteria. The antibacterial properties of FFAs are used by many organisms to defend against parasitic or pathogenic bacteria. The prime target of FFA action is the cell membrane, where FFAs disrupt the electron transport chain and oxidative phosphorylation. Besides interfering with cellular energy production, FFA action may also result from the inhibition of enzyme activity, impairment of nutrient uptake, generation of peroxidation and auto-oxidation degradation products or direct lysis of bacterial cells. http://purl.obolibrary.org/obo/ARO_3003957 palmitic acid http://purl.obolibrary.org/obo/ARO_3003956 antibacterial free fatty acids Palmitic acid is the most common saturated fatty acid found in animals, plants, and microorganisms. Palmitic acid is found to have antibacterial properties. http://purl.obolibrary.org/obo/ARO_3003958 oleic acid http://purl.obolibrary.org/obo/ARO_3003956 antibacterial free fatty acids Oleic acid is a fatty acid that occurs naturally in various animal and vegetable fats and oils. Oleic acid is found to have antibacterial activity, particularly in inhibiting the growth of several Gram-positive bacterial species. http://purl.obolibrary.org/obo/ARO_3003959 linoleic acid http://purl.obolibrary.org/obo/ARO_3003956 antibacterial free fatty acids Linoleic acid is a polyunsaturated omega-6 fatty acid. Linoleic acid has been found to have antibacterial activity, particularly in inhibiting the growth of Gram-positive bacterial species. http://purl.obolibrary.org/obo/ARO_3003960 farAB http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump farAB is an MFS efflux pump found in gonococci that is involved in antibacterial fatty acid resistance. Moreover, expression of the tandemly linked farA and farB genes was positively associated with the presence of the MtrR transcriptional regulatory protein that normally downregulates the expression of mtrCDE. http://purl.obolibrary.org/obo/ARO_3003961 farA http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance farA is the membrane fusion protein that is part of the farAB efflux pump. http://purl.obolibrary.org/obo/ARO_3003962 farB http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance farB is the cytoplasmic transporter protein that is part of the farAB efflux pump. farB corresponds to 3 loci in Pseudomonas aeruginosa PAO1 and 3 loci in Pseudomonas aeruginosa LESB58. http://purl.obolibrary.org/obo/ARO_3003963 flo http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump The Flo transporters can be plasmid- or chromosome-encoded. flo is an important determinant of florfenicol resistance in animal isolates of E. coli but is also found in human pathogens (e.g. Salmonella enterica and V. cholerae). http://purl.obolibrary.org/obo/ARO_3003964 hp1181 http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump hp1181 is a translocase that is part of the MFS efflux pump family. It is found in H. pylori and has role in the active efflux of antibiotics. http://purl.obolibrary.org/obo/ARO_3003965 hp1184 http://purl.obolibrary.org/obo/ARO_3000112 multidrug and toxic compound extrusion (MATE) transporter hp1184 is a translocase that belongs to the MATE efflux pump family. It is found in H. pylori and is involved in the active efflux of antibiotics. http://purl.obolibrary.org/obo/ARO_3003966 Klebsiella pneumoniae OmpK35 http://purl.obolibrary.org/obo/ARO_3003768 gene conferring resistance via absence Klebsiella pneumoniae outer membrane porin protein. In beta-lactam-resistant Klebsiella, this porin is often deleted, limiting diffusion of the antibiotic into the cell. Klebsiella strains expressing OmpK35 are often beta-lactam sensitive even in the presence of beta-lactamases because of an inefficient mechanism. http://purl.obolibrary.org/obo/ARO_3003967 lfrA http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump lfrA is involved in the active efflux of quinolones and is found in Mycobacteroides abscessus. http://purl.obolibrary.org/obo/ARO_3003968 Klebsiella pneumoniae OmpK36 http://purl.obolibrary.org/obo/ARO_3003768 gene conferring resistance via absence Klebsiella pneumoniae outer membrane porin protein. In beta-lactam-resistant Klebsiella, this porin is often deleted, limiting diffusion of the antibiotic into the cell. Klebsiella strains expressing OmpK36 are often beta-lactam sensitive even in the presence of beta-lactamases because of an inefficient mechanism. http://purl.obolibrary.org/obo/ARO_3003969 lmrP http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump lmrP is a proton motive force-dependent drug transporter that is part of the MFS efflux pump family. http://purl.obolibrary.org/obo/ARO_3003970 D-Ala-D-Ala ligase http://purl.obolibrary.org/obo/ARO_3002906 Van ligase Non-van ligases that synthesize D-Ala-D-Ala, the default cell wall precursor that makes a cell vulnerable to glycopeptide antibiotics. Mutations in the ddl gene can cause the production of nonfunctional/inactivated D-Ala-D-Ala ligases, which can render bacteria glycopeptide dependent depending on the presence of vancomycin resistance clusters. http://purl.obolibrary.org/obo/ARO_3003971 Erm(44)v http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase Variant of Erm(44)v isolated from Staphylococcus saprophyticus, confers resistance to lincosamide and macrolide antibiotics but not streptogramins. http://purl.obolibrary.org/obo/ARO_3003972 Solithromycin http://purl.obolibrary.org/obo/ARO_0000000 macrolide antibiotic A clinically developed Macrolide antibiotic targeting gram positive and gram negative bacteria. http://purl.obolibrary.org/obo/ARO_3003974 Cutibacterium acnes gyrA conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3003292 fluoroquinolone resistant gyrA Point mutations in Cutibacterium acnes gyrA protein known to confer resistance to fluoroquinolone antibiotics. http://purl.obolibrary.org/obo/ARO_3003975 pactamycin http://purl.obolibrary.org/obo/ARO_3007158 pactamycin-like antibiotic Antibiotic produced by Streptomyces pactum, considered a universal translation inhibitor. http://purl.obolibrary.org/obo/ARO_3003976 16S rRNA with mutation conferring resistance to pactamycin http://purl.obolibrary.org/obo/ARO_3003211 16S rRNA with mutation conferring antibiotic resistance Point mutations in bacterial 16S rRNA that confer resistance to antibiotic pactamycin. http://purl.obolibrary.org/obo/ARO_3003977 Halobacterium salinarum 16S rRNA mutation conferring resistance to pactamycin http://purl.obolibrary.org/obo/ARO_3003976 16S rRNA with mutation conferring resistance to pactamycin Point mutations in Halobacterium 16S rRNA that confer resistance to pactamycin antibiotic. http://purl.obolibrary.org/obo/ARO_3003978 Chlamydomonas reinhardtii 16S rRNA (rrnS) mutation conferring resistance to streptomycin http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutation in C. reinhardtii rrnS conferring resistance to streptomycin antibiotic. http://purl.obolibrary.org/obo/ARO_3003979 Eravacycline http://purl.obolibrary.org/obo/ARO_3000050 tetracycline antibiotic A fluorocycline that acts to inhibit the bacterial ribosome. http://purl.obolibrary.org/obo/ARO_3003980 tetA(58) http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump TetA(58) is a Tetracycline efflux pump described in Paenibacillus sp. LC231, a strain of Paenibacillus isolated from Lechuguilla Cave, NM, USA. Described by Pawlowski et al. 2016. http://purl.obolibrary.org/obo/ARO_3003981 tetB(58) http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump Tetracycline resistant TetB(58) efflux pump found in Paenibacillus sp. LC231, a strain of Paenibacillus isolated from Lechuguilla Cave, NM, USA. Described by Pawlowski et al. 2016. http://purl.obolibrary.org/obo/ARO_3003982 LlmA 23S ribosomal RNA methyltransferase http://purl.obolibrary.org/obo/ARO_3004273 Llm 23S ribosomal RNA methyltransferase Lincosamide (Clindamycin) resistant (putative) ribosomal methyltransferase related to the RlmK 23S rRNA methyltransferase COG family. Detected in Paenibacillus sp. LC231, an isolated strain of Paenibacillus found in Lechuguilla Cave, NM, USA. Described by Pawlowski et al. 2016. http://purl.obolibrary.org/obo/ARO_3003983 CatU http://purl.obolibrary.org/obo/ARO_3000122 chloramphenicol acetyltransferase (CAT) Chloramphenicol acetyltransferase conferring resistance to phenicol antibiotics detected in Paenibacillus sp. LC231, an isolated strain of Paenibacillus from Lechuguilla Cave, NM, USA. Described by Pawlowski et al. 2016. http://purl.obolibrary.org/obo/ARO_3003984 BahA http://purl.obolibrary.org/obo/ARO_3004260 Bah amidohydrolase Bacitracin amidohydrolase found in Paenibacillus sp. LC231, an isolated strain of Paenibacillus from Lechuguilla Cave, NM, USA. Confers resistance by bacitracin inactivation through amidohydrolysis. Described by Pawlowski et al. 2016. http://purl.obolibrary.org/obo/ARO_3003985 amidohydrolysis of bacitracin undecaprenyl pyrophosphate http://purl.obolibrary.org/obo/ARO_3000040 hydrolysis of antibiotic conferring resistance Hydrolysis of amido side-chain of asparagine-12 forming hydrogen bond with undecaprenyl pyrophosphate in bacitracin leading to antibiotic inactivation. http://purl.obolibrary.org/obo/ARO_3003986 TaeA http://purl.obolibrary.org/obo/ARO_0010001 ATP-binding cassette (ABC) antibiotic efflux pump Pleuromutilin (Tiamulin) ABC efflux pump found in Paenibacillus sp. LC231, a strain of Paenibacillus isolated from Lechuguilla Cave, NM, USA. Confers resistance to pleuromutilin antibiotics. Described by Pawlowski et al. 2016. http://purl.obolibrary.org/obo/ARO_3003987 VatI http://purl.obolibrary.org/obo/ARO_3000453 streptogramin vat acetyltransferase Streptogramin A acetyltransferase found in Paenibacillus sp. LC231, isolated from Lechuguilla Cave, NM, USA. Confers resistance to streptogramin A antibiotics. Described by Pawlowski et al. 2016. http://purl.obolibrary.org/obo/ARO_3003988 AAC(2')-IIb http://purl.obolibrary.org/obo/ARO_3007394 AAC(2')-II AAC(2')-IIb is an intrinsic Kasugamycin 2' acetyltransferase protein found in Paenibacillus sp. LC231, a strain of Paenibacillus isolated from Lechuguilla Cave, NM, USA. Confers resistance to aminoglycoside antibiotics, including kasugamycin. Described by Pawlowski et al. 2016. http://purl.obolibrary.org/obo/ARO_3003989 AAC(6')-34 http://purl.obolibrary.org/obo/ARO_3000345 AAC(6') AAC(6')-34 is an aminoglycoside 6'-phosphotransferase found in Paenibacillus sp. LC231, a strain of Paenibacillus from Lechuguilla Cave, NM, USA. Confers resistance to aminoglycoside antibiotics. Described by Pawlowski et al. 2016. http://purl.obolibrary.org/obo/ARO_3003990 vgbC http://purl.obolibrary.org/obo/ARO_3000376 streptogramin vgb lyase VgbC is a streptogramin B-type lyase found in Paenibacillus sp. LC231, a strain of Paenibacillus isolated from Lechuguilla Cave, NM, USA. Confers resistance to streptogramin B-type antibiotics by linearization of the lactone ring on an ester bond, resulting in antibiotic inactivation. Described by Pawlowski et al. 2016. http://purl.obolibrary.org/obo/ARO_3003991 mphI http://purl.obolibrary.org/obo/ARO_3000333 macrolide phosphotransferase (MPH) mphI is a macrolide phosphotransferase protein found in Paenibacillus sp. LC231, a strain of Paenibacillus isolated from Lechuguilla Cave, NM, USA. Confers resistance to macrolide antibiotics. Described by Pawlowski et al. 2016. http://purl.obolibrary.org/obo/ARO_3003992 rphB http://purl.obolibrary.org/obo/ARO_3004040 rifampin phosphotransferase rphB is a rifampin phosphotransferase protein found in Paenibacillus sp. LC231, a strain of Paenibacillus isolated from Lechuguilla Cave, NM, USA. Confers resistance to rifamycin antibiotics, specifically rifampin, through rifampin inactivation. Described by Pawlowski et al. 2016. http://purl.obolibrary.org/obo/ARO_3003993 capreomycin http://purl.obolibrary.org/obo/ARO_0000016 aminoglycoside antibiotic Capreomycin is an aminoglycoside antibiotic, capable of treating a large number of infections but in particular used for killing bacteria causing tuberculosis. http://purl.obolibrary.org/obo/ARO_3003994 cpaA http://purl.obolibrary.org/obo/ARO_3004257 cpa acetyltransferase cpaA is a capreomycin acetyltransferase protein found in Paenibacillus sp. LC231, an isolated strain of Paenibacillus in Lechuguilla Cave, NM, USA. Confers resistance to capreomycin, an aminoglycoside antibiotic. Described by Pawlowski et al. 2016. http://purl.obolibrary.org/obo/ARO_3003995 Clostridioides difficile gyrA conferring resistance to fluoroquinolones http://purl.obolibrary.org/obo/ARO_3003292 fluoroquinolone resistant gyrA Amino acid substitutions in Clostridioides difficile gyrase subunit A which when present confer functional resistance to fluoroquinolone antibiotics. http://purl.obolibrary.org/obo/ARO_3003997 amoxicillin-clavulanic acid http://purl.obolibrary.org/obo/ARO_3000707 antibiotic mixture An antibiotic cocktail containing the beta-lactam antibiotic Amoxicillin and the beta-lactamase inhibitor Clavulanic Acid (potassium clavulanate). http://purl.obolibrary.org/obo/ARO_3003998 ampicillin-sulbactam http://purl.obolibrary.org/obo/ARO_3000707 antibiotic mixture An antibiotic mixture containing the penicillin-derived beta-lactam antibiotic Ampicillin and the beta-lactamase inhibitor Sulbactam. Also known as Unasyn and/or Ampictam. http://purl.obolibrary.org/obo/ARO_3003999 cefamandole http://purl.obolibrary.org/obo/ARO_3009106 second-generation cephalosporin Cefamandole is a second-generation cephalosporin-class beta-lactam antibiotic. http://purl.obolibrary.org/obo/ARO_3004000 cefetamet http://purl.obolibrary.org/obo/ARO_3009107 third-generation cephalosporin Cefetamet is a third-generation semi-synthetic beta-lactam antibiotic that inactivates inner cell wall PBPs through targeting binding, resulting in cell lysis. http://purl.obolibrary.org/obo/ARO_3004001 cefmetazole http://purl.obolibrary.org/obo/ARO_3009106 second-generation cephalosporin Cefmetazole is a semi-synthetic cephamycin antibiotic with broad spectrum antibiotic activity against both gram-positive and gram-negative bacteria, that disrupt cell wall synthesis through binding to PBPs causing cell lysis. http://purl.obolibrary.org/obo/ARO_3004002 cefonicid http://purl.obolibrary.org/obo/ARO_3009106 second-generation cephalosporin Cefonicid is a second-generation cephalosporin-class beta-lactam antibiotic with broad spectrum activity. Particularly used against urinary tract infections and lower respiratory infections. Causes cell lysis by inactivation of PBPs through binding, inhibiting peptidoglycan synthesis. http://purl.obolibrary.org/obo/ARO_3004003 cefoperazone http://purl.obolibrary.org/obo/ARO_3009107 third-generation cephalosporin Cefoperazone is a semi-synthetic cephalosporin containing a tetrazolyl moiety that is resistant to beta-lactamases. Particularly used for treatment of Pseudomonas spp. infections. http://purl.obolibrary.org/obo/ARO_3004004 cefotetan http://purl.obolibrary.org/obo/ARO_3009106 second-generation cephalosporin Cefotetan is a cephamycin-class beta-lactam antibiotic that is highly resistant to beta-lactamases and effective against a wide range of gram-negative and gram-positive bacteria. http://purl.obolibrary.org/obo/ARO_3004005 cefprozil http://purl.obolibrary.org/obo/ARO_3009106 second-generation cephalosporin Cefprozil is a cephalosporin and beta-lactam antibiotic with bactericidal activity. It selectively binds to PBPs and inhibits peptidoglycan synthesis, a major cell wall component, resulting in cell lysis. http://purl.obolibrary.org/obo/ARO_3004006 ceftiofur http://purl.obolibrary.org/obo/ARO_3009107 third-generation cephalosporin Ceftiofur is a third-generation broad spectrum cephalosporin and beta-lactam antibiotic predominantly used in veterinary medicine. It causes cell lysis by disrupting peptidoglycan cross-linkage and cell wall formation by binding to PBPs. http://purl.obolibrary.org/obo/ARO_3004007 ceftizoxime http://purl.obolibrary.org/obo/ARO_3009107 third-generation cephalosporin Ceftizoxime is a third-generation cephalosporin and broad spectrum beta-lactam antibiotic. Ceftizoxime causes bacterial cell lysis through peptidoglycan cross-linking inhibition by binding to PBPs. http://purl.obolibrary.org/obo/ARO_3004008 cephapirin http://purl.obolibrary.org/obo/ARO_3009105 first-generation cephalosporin Cephapirin is a first-generation cephalosporin and broad spectrum beta-lactam antibiotic. Inactivation of penicillin-binding proteins through cephapirin binding disrupts peptidoglycan cross-linking, resulting in cell lysis. http://purl.obolibrary.org/obo/ARO_3004009 cefradine http://purl.obolibrary.org/obo/ARO_3009105 first-generation cephalosporin Cefradine is a first-generation cephalosporin and broad spectrum beta-lactam antibiotic. Cefradine binding to penicillin-binding proteins disrupts cell wall peptidoglycan cross-linkage, resulting in cell lysis. http://purl.obolibrary.org/obo/ARO_3004010 cinoxacin http://purl.obolibrary.org/obo/ARO_0000001 fluoroquinolone antibiotic Cinoxacin is a fluoroquinolone antibiotic primarily used for the treatment of urinary tract infections in adults. Cinoxacin binds to DNA gyrase, resulting in double-stranded DNA breaks and cell death. http://purl.obolibrary.org/obo/ARO_3004011 clinafloxacin http://purl.obolibrary.org/obo/ARO_0000001 fluoroquinolone antibiotic Clinafloxacin is a fluoroquinolone antibiotic and gyrase (DNA topoisomerase II) inhibitor. It binds to DNA gyrase and disrupts replication by causing double-stranded DNA breaks, resulting in cell death. http://purl.obolibrary.org/obo/ARO_3004012 clofazimine http://purl.obolibrary.org/obo/ARO_0000001 fluoroquinolone antibiotic Clofazimine is a fluoroquinolone-class phenazine dye used for the treatment of leprosy. Clofazimine binds to DNA and disrupts bacterial DNA gyrase, thereby causing double-stranded DNA breaks, and subsequent cell death. http://purl.obolibrary.org/obo/ARO_3004013 fleroxacin http://purl.obolibrary.org/obo/ARO_0000001 fluoroquinolone antibiotic Fleroxacin is a broad spectrum fluoroquinolone antibiotic that inhibits the DNA supercoiling activity of bacterial DNA gyrase, resulting in double-stranded DNA breaks and subsequent cell death. http://purl.obolibrary.org/obo/ARO_3004014 flomoxef http://purl.obolibrary.org/obo/ARO_3009106 second-generation cephalosporin Flomoxef is an oxacephem antibiotic which was effective in preventing the growth of all ESBL-producing strains and is widely active against Gram-positive, Gram-negative, and anaerobic bacteria. It is sometimes classified as a second-generation or fourth-generation cephalosporin. http://purl.obolibrary.org/obo/ARO_3004015 gentamicin A http://purl.obolibrary.org/obo/ARO_3007382 gentamicin Gentamicin A is part of a complex of broad spectrum aminoglycoside antibiotics. Gentamicin inhibits protein synthesis, resulting in bacterial cell death. http://purl.obolibrary.org/obo/ARO_3004016 loracarbef http://purl.obolibrary.org/obo/ARO_3009106 second-generation cephalosporin Loracarbef is a second-generation cephalosporin (carbacephem) and broad spectrum beta-lactam antibiotic. Loracarbef inhibits PBPs through binding, disrupting peptidoglycan cell wall cross-linkage and resulting in cell death. http://purl.obolibrary.org/obo/ARO_3004017 moxalactam http://purl.obolibrary.org/obo/ARO_3009107 third-generation cephalosporin Moxalactam (Latamoxef) is a broad spectrum cephalosporin (oxacephem) and beta-lactam antibiotic. Moxalactam binding to PBPs inhibits peptidoglycan cross-linkage in the cell wall, resulting in cell death. Moxalactam is proposed to be effective against meningitides as it passes the blood-brain barrier. http://purl.obolibrary.org/obo/ARO_3004018 nafcillin http://purl.obolibrary.org/obo/ARO_3009125 beta-lactamase resistant penicillin Nafcillin is a penicillin-class narrow-spectrum beta-lactam antibiotic. It inhibits cell wall synthesis and peptidoglycan cross-linkage through binding to PBPs, similarly to other penicillin-like antibiotics. http://purl.obolibrary.org/obo/ARO_3004019 para-aminosalicylic acid http://purl.obolibrary.org/obo/ARO_3007159 salicylic acid antibiotic Para-aminosalicylic acid (PAS) is an anti-tubercular antibiotic agent, often used in conjunction with Isoniazid for treatment of M. tuberculosis infections. PAS diminishes bacterial cell growth by limiting folic acid production. http://purl.obolibrary.org/obo/ARO_3004020 piperacillin-sulbactam http://purl.obolibrary.org/obo/ARO_3000707 antibiotic mixture An antibiotic cocktail containing the beta-lactam penam antibiotic Piperacillin and the beta-lactamase inhibitor sulbactam. http://purl.obolibrary.org/obo/ARO_3004021 piperacillin-tazobactam http://purl.obolibrary.org/obo/ARO_3000707 antibiotic mixture An antibiotic cocktail containing the penam beta-lactam antibiotic Piperacillin and the beta-lactamase inhibitor Tazobactam. http://purl.obolibrary.org/obo/ARO_3004022 quinupristin-dalfopristin http://purl.obolibrary.org/obo/ARO_3000707 antibiotic mixture An antibiotic cocktail of the streptogramin A dalfopristin and the streptogramin B quinupristin antibiotics. Used particularly to treat MRSA and vancomycin-resistant Enterococcus. http://purl.obolibrary.org/obo/ARO_3004023 ticarcillin-clavulanic acid http://purl.obolibrary.org/obo/ARO_3000707 antibiotic mixture An antibiotic cocktail containing the beta-lactam antibiotic ticarcillin and the beta-lactamase inhibitor clavulanic acid (clavulanate). http://purl.obolibrary.org/obo/ARO_3004024 trimethoprim-sulfamethoxazole http://purl.obolibrary.org/obo/ARO_3000707 antibiotic mixture An antibiotic cocktail containing the diaminopyrimidine antibiotic Trimethoprim and the sulfonamide antibiotic sulfamethoxazole (1 TMP:5 SMX). http://purl.obolibrary.org/obo/ARO_3004025 prothionamide http://purl.obolibrary.org/obo/ARO_3007156 thioamide antibiotic Prothionamide is a thioamide derivative with antibacterial properties. It increases cell wall permeability and decreases cell wall damage resistance by inhibition of mycolic acid synthesis, resulting in cell death. It is particularly used to treat M. tuberculosis and M. leprae infections. http://purl.obolibrary.org/obo/ARO_3004026 tinidazole http://purl.obolibrary.org/obo/ARO_3004115 nitroimidazole antibiotic Tinidazole is a nitroimidazole anti-parasitic drug. It is used in the treatment of protozoan infections. http://purl.obolibrary.org/obo/ARO_3004030 RosAB http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump An efflux pump/potassium antiporter system (RosAB) formed by the RosA and RosB proteins found in Yersinia. http://purl.obolibrary.org/obo/ARO_3004031 tetAB(46) http://purl.obolibrary.org/obo/ARO_0010001 ATP-binding cassette (ABC) antibiotic efflux pump tetAB(46) is a heterodimeric ABC transporter conferring tetracycline resistance in Streptococcus australis isolated from the oral cavity. Both tetA(46) and tetB(46) genes are required for resistance. http://purl.obolibrary.org/obo/ARO_3004032 tetA(46) http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance tetA(46) is a subunit of tetAB(46), a heterodimeric ABC transporter, that is required for conferring tetracycline resistance in Streptococcus australis isolated from the oral cavity. http://purl.obolibrary.org/obo/ARO_3004033 tetB(46) http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance tetB(46) is a subunit of tetAB(46), a heterodimeric ABC transporter, that is required for conferring tetracycline resistance in Streptococcus australis isolated from the oral cavity. http://purl.obolibrary.org/obo/ARO_3004034 tetAB(60) http://purl.obolibrary.org/obo/ARO_0010001 ATP-binding cassette (ABC) antibiotic efflux pump tetAB(60) is an ABC transporter that confers resistance to tetracycline and tigercycline identified by screening a human saliva metagenomic library in Escherichia coli. Both tetA(60) and tetB(60) are required for resistance. http://purl.obolibrary.org/obo/ARO_3004035 tetA(60) http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance tetA(60) is a subunit of tetAB(60), an ABC transporter that confers resistance to tetracycline and tigercycline identified by screening a human saliva metagenomic library in Escherichia coli, which is required for resistance. http://purl.obolibrary.org/obo/ARO_3004036 tetB(60) http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance tetB(60) is a subunit of tetAB(60), an ABC transporter that confers resistance to tetracycline and tigercycline identified by screening a human saliva metagenomic library in Escherichia coli, which is required for resistance. http://purl.obolibrary.org/obo/ARO_3004038 Pseudomonas aeruginosa emrE http://purl.obolibrary.org/obo/ARO_3000264 emrE EmrE is a small multidrug transporter that functions as a homodimer and that couples the efflux of small polyaromatic cations from the cell with the import of protons down an electrochemical gradient. Confers resistance to tetraphenylphosphonium, methyl viologen, gentamicin, kanamycin, and neomycin. http://purl.obolibrary.org/obo/ARO_3004039 Escherichia coli emrE http://purl.obolibrary.org/obo/ARO_3000264 emrE Member of the small MDR (multidrug resistance) family of transporters; in Escherichia coli this protein provides resistance against a number of positively charged compounds including ethidium bromide and erythromycin; proton-dependent secondary transporter which exchanges protons for compound translocation. http://purl.obolibrary.org/obo/ARO_3004040 rifampin phosphotransferase http://purl.obolibrary.org/obo/ARO_3000576 rifampin inactivation enzyme Enzymes, protein or other gene products that inactivate rifampin (rifamycin) antibiotics through phosphorylation of the antibiotic at the 21-OH position. http://purl.obolibrary.org/obo/ARO_3004041 Klebsiella pneumoniae acrA http://purl.obolibrary.org/obo/ARO_3000207 acrA AcrA is a subunit of the AcrAB multidrug efflux system that is found in K. pneumoniae, which is encoded by the acrRAB operon. http://purl.obolibrary.org/obo/ARO_3004042 Enterobacter cloacae acrA http://purl.obolibrary.org/obo/ARO_3000207 acrA AcrA is a subunit of the AcrAB-TolC multidrug efflux system in E. cloacae. http://purl.obolibrary.org/obo/ARO_3004043 Escherichia coli acrA http://purl.obolibrary.org/obo/ARO_3000207 acrA AcrA is a subunit of the AcrAB-TolC multidrug efflux system found in E. coli. http://purl.obolibrary.org/obo/ARO_3004044 antibiotic sensitive fabI http://purl.obolibrary.org/obo/ARO_3000872 antibiotic sensitive enoyl-acyl carrier reductase fabI is a bacterial enoyl-acyl carrier reductase (ENR) isozyme. As with other ENRs, mutations in fabI can confer resistance to the biocide triclosan. http://purl.obolibrary.org/obo/ARO_3004045 Escherichia coli fabI mutations conferring resistance to isoniazid and triclosan http://purl.obolibrary.org/obo/ARO_3004270 antibiotic resistant fabI fabI is a enoyl-acyl carrier reductase used in lipid metabolism and fatty acid biosynthesis. The bacterial biocide Triclosan blocks the final reduction step in fatty acid elongation, inhibiting biosynthesis. Point mutations in fabI can confer resistance to Triclosan and Isoniazid. http://purl.obolibrary.org/obo/ARO_3004046 kdpDE http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux kdpDE is a two-component regulatory system in Escherichia coli, well studied for its role in potassium transport and homeostasis. kdpE is also implicated in virulence loci regulation and overexpression of kdpE is shown to confer resistance to aminoglycoside antibiotics. http://purl.obolibrary.org/obo/ARO_3004047 kdpD http://purl.obolibrary.org/obo/ARO_3000750 protein of two-component regulatory system modulating antibiotic efflux kdpD is a component of the two-component regulatory system, kdpDE. This system is involved in potassium transport and homeostasis, and has been implicated in virulence factor regulation along with kdpE. http://purl.obolibrary.org/obo/ARO_3004049 Escherichia coli fabG mutations conferring resistance to triclosan http://purl.obolibrary.org/obo/ARO_3004284 antibiotic resistant fabG fabG is a 3-oxoacyl-acyl carrier protein reductase involved in lipid metabolism and fatty acid biosynthesis.The bacterial biocide Triclosan blocks the final reduction step in fatty acid elongation, inhibiting biosynthesis. Point mutations in fabG can confer resistance to Triclosan. http://purl.obolibrary.org/obo/ARO_3004050 antibiotic sensitive fabG http://purl.obolibrary.org/obo/ARO_3000872 antibiotic sensitive enoyl-acyl carrier reductase fabG is a bacterial 3-oxoacyl enoyl-acyl carrier reductase (ENR) isozyme. As with other ENRs, mutations in fabG are shown to confer resistance to the biocide triclosan. http://purl.obolibrary.org/obo/ARO_3004054 Pseudomonas aeruginosa CpxR http://purl.obolibrary.org/obo/ARO_3000831 CpxR CpxR is directly involved in activation of expression of RND efflux pump MexAB-OprM in P. aeruginosa. CpxR is required to enhance mexAB-oprM expression and drug resistance, in the absence of repressor MexR. http://purl.obolibrary.org/obo/ARO_3004055 Escherichia coli CpxR http://purl.obolibrary.org/obo/ARO_3000831 CpxR The Escherichia coli CpxR/CpxA system responds to general periplasmic stress and has been used as a model two-component system for transcription regulation in bacteria. CpxR/CpxA system facilitates Salmonella and E. coli resistance to cationic antimicrobial peptides.The CpxR/CpxA system can activate transcription of marRAB operon, thus facilitating multidrug-resistant regulator to enhance expression of TolC-dependent tripartite multidrug transporters. http://purl.obolibrary.org/obo/ARO_3004056 ArmR http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux ArmR, a 53-amino-acid antirepressor, allosterically inhibits MexR dimer-DNA binding by occupying a hydrophobic binding cavity within the center of the MexR dimer. ArmR up-regulation and MexR-ArmR complex formation have previously been shown to upregulate MexAB-OprM. http://purl.obolibrary.org/obo/ARO_3004057 23S rRNA with mutation conferring resistance to linezolid antibiotics http://purl.obolibrary.org/obo/ARO_3000336 23S rRNA with mutation conferring antibiotic resistance Point mutations in the 23S rRNA subunit may confer resistance to linezolid and other oxazolidinone antibiotics. http://purl.obolibrary.org/obo/ARO_3004058 Staphylococcus aureus 23S rRNA with mutation conferring resistance to linezolid http://purl.obolibrary.org/obo/ARO_3004057 23S rRNA with mutation conferring resistance to linezolid antibiotics Point mutations in the 23S rRNA subunit of the large ribosomal bacterial subunit in Staphylococcus aureus, which confer resistance to linezolid by disrupting antibiotic target binding. http://purl.obolibrary.org/obo/ARO_3004059 Type A NfxB http://purl.obolibrary.org/obo/ARO_3000820 NfxB Type A NfxB mutants are four to eight times more resistant to ofloxacin, erythromycin, and new zwitterionic cephems, i.e., cefpirome, cefclidin, cefozopran, and cefoselis, than the parent strain, PAO1. nfxB corresponds to 2 loci in Pseudomonas aeruginosa PAO1 (gene name: esrC/nfxB) and 2 loci in Pseudomonas aeruginosa LESB58 (gene name: nfxB). http://purl.obolibrary.org/obo/ARO_3004060 Type B NfxB http://purl.obolibrary.org/obo/ARO_3000820 NfxB Type B NfxB mutants are more resistant to tetracycline and chloramphenicol, as well as ofloxacin, erythromycin, and the new zwitterionic cephems, than was PAO1, and they are four to eight times more susceptible to carbenicillin, sulbenicillin, imipenem, panipenem, biapenem, moxalactam, aztreonam, gentamicin, and kanamycin than PAO1. The mutation at the 46th amino acid position is sufficient for overproduction of OprJ and the multidrug resistance. nfxB corresponds to 2 loci in Pseudomonas aeruginosa PAO1 (gene name: esrC/nfxB) and 2 loci in Pseudomonas aeruginosa LESB58 (gene name: nfxB). http://purl.obolibrary.org/obo/ARO_3004061 MexCD-OprJ with type A NfxB mutation http://purl.obolibrary.org/obo/ARO_3000797 MexCD-OprJ MexCD–OprJ with type A NfxB phenotype are four to eight times more resistant to ofloxacin, erythromycin, and new zwitterionic cephems, i.e., cefpirome, cefclidin, cefozopran, and cefoselis, than the parent strain, PAO1. http://purl.obolibrary.org/obo/ARO_3004062 MexCD-OprJ with type B NfxB mutation http://purl.obolibrary.org/obo/ARO_3000797 MexCD-OprJ MexCD-OprJ with Type B NfxB mutions are more resistant to tetracycline and chloramphenicol, as well as ofloxacin, erythromycin, and the new zwitterionic cephems, than was PAO1, and they are four to eight times more susceptible to carbenicillin, sulbenicillin, imipenem, panipenem, biapenem, moxalactam, aztreonam, gentamicin, and kanamycin than PAO1. http://purl.obolibrary.org/obo/ARO_3004063 EdeQ http://purl.obolibrary.org/obo/ARO_3004064 Edeine acetyltransferase EdeQ is an N-acetyltransferase enzyme that confers high-level self-resistance to edeine in Brevibacillus brevis, a natural edeine producer. EdeQ converts active edeine to N-acetyledeine, which is ineffective in vivo. http://purl.obolibrary.org/obo/ARO_3004064 Edeine acetyltransferase http://purl.obolibrary.org/obo/ARO_3000557 antibiotic inactivation enzyme Edeine acetyltransferase enzymes catalyze the transfer of an acetyl group to active edeine, converting it to an inactive form in vivo. This mechanism is used for high-level self-resistance in edeine-producing Brevibacillus spp. http://purl.obolibrary.org/obo/ARO_3004066 MexEF-OprN with MexT mutation conferring resistance to chloramphenicol, ciprofloxacin, and trimethoprim http://purl.obolibrary.org/obo/ARO_3000798 MexEF-OprN The MexEF–OprN efflux pump in P. aeruginosa is overexpressed with MexT mutation conferring resistance to chloramphenicol and ciprofloxacin. http://purl.obolibrary.org/obo/ARO_3004067 MUS beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase Subclass B1 (metallo-) beta-lactamases found in Myroides spp., which confer resistance to carbapenam class beta-lactamase antibiotics. http://purl.obolibrary.org/obo/ARO_3004068 MexEF-OprN with MexS mutations conferring resistance to chloramphenicol, ciprofloxacin, and trimethoprim http://purl.obolibrary.org/obo/ARO_3000798 MexEF-OprN The MexEF–OprN efflux pump with MexS mutations conferring resistance to chloramphenicol and ciprofloxacin. The model includes the MexT regulator, as MexS is suggested to inactivate MexT. http://purl.obolibrary.org/obo/ARO_3004069 MvaT http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux MvaT, a global regulator of virulence genes in P. aeruginosa, has also shown to be able to repress the expression of the MexEF-OprN pump. http://purl.obolibrary.org/obo/ARO_3004070 MexEF-OprN with MvaT deletion conferring resistance to chloramphenicol and norfloxacin http://purl.obolibrary.org/obo/ARO_3000798 MexEF-OprN A deletion of MvaT results in the overexpression of MexEF-OprN conferring resistance to chloramphenicol and norfloxacin. http://purl.obolibrary.org/obo/ARO_3004072 OpmB http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance OpmB is an outer membrane efflux protein in Pseudomonas aeruginosa that shows functional cooperation with MuxABC, to form the efflux pump system MuxABC-OpmB. http://purl.obolibrary.org/obo/ARO_3004073 MuxA http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MuxA is a membrane fusion protein component of the efflux pump system MuxABC-OpmB in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3004074 MuxB http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MuxB is one of the two necessary RND components in the Pseudomonas aeruginosa efflux pump system MuxABC-OpmB. http://purl.obolibrary.org/obo/ARO_3004075 MuxC http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance MuxC is one of the two necessary RND components of the MuxABC-OpmB efflux pumps system in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3004076 MuxABC-OpmB http://purl.obolibrary.org/obo/ARO_0010004 resistance-nodulation-cell division (RND) antibiotic efflux pump MuxABC-OpmB is an RND-type multidrug efflux pump in Pseudomonas aeruginosa. This efflux pump confers resistance to aztreonam, novobiocin, tetracycline, erythromycin, kitasamycin and rokitamycin. http://purl.obolibrary.org/obo/ARO_3004077 PmpM http://purl.obolibrary.org/obo/ARO_3000112 multidrug and toxic compound extrusion (MATE) transporter PmpM is a multidrug efflux pump belonging to the MATE family of Pseudomonas aeruginosa. PmpM is an H+ drug antiporter and is the first reported case of an H+ coupled efflux pump in the MATE family. PmpM confers resistance to fluoroquinolones, fradiomycin, benzalkonium chloride, chlorhexidine gluconate, ethidium bromide, tetraphenylphosphonium chloride (TPPCl), and rhodamine 6G. http://purl.obolibrary.org/obo/ARO_3004082 AcrAD-TolC http://purl.obolibrary.org/obo/ARO_0010004 resistance-nodulation-cell division (RND) antibiotic efflux pump AcrAD-TolC efflux pump system in E. coli from the resistance-nodulation-division family, was shown to participate in the efflux of aminoglycosides. http://purl.obolibrary.org/obo/ARO_3004083 AcrEF-TolC confers resistance to ciprofloxacin http://purl.obolibrary.org/obo/ARO_3000503 AcrEF-TolC AcrEF-TolC efflux pump system of E. coli confers resistance to fluoroquinolones (ciprofloxacin). http://purl.obolibrary.org/obo/ARO_3004085 lnuG http://purl.obolibrary.org/obo/ARO_3000221 lincosamide nucleotidyltransferase (LNU) lnuG is a transposon-mediated lincosamide nucleotidyltransferase found in Enterococcus faecalis on Tn6260. http://purl.obolibrary.org/obo/ARO_3004086 APH(3')-VIIIb http://purl.obolibrary.org/obo/ARO_3000126 APH(3') APH(3')-VIIIb is an aminoglycoside phosphoryltransferase that acts on the 3-OH target of aminoglycosides found in Acinetobacter rudis. http://purl.obolibrary.org/obo/ARO_3004087 APH(3')-IXa http://purl.obolibrary.org/obo/ARO_3000126 APH(3') APH(3')-IXa is an aminoglycoside phosphoryltransferase that acts on the 3-OH target of aminoglycosides. http://purl.obolibrary.org/obo/ARO_3004088 lefamulin http://purl.obolibrary.org/obo/ARO_3000670 pleuromutilin antibiotic Lefamulin is a semi-synthetic pleuromutilin compound highly active against multi-resistant pathogens. http://purl.obolibrary.org/obo/ARO_3004089 ANT(3'')-IIa http://purl.obolibrary.org/obo/ARO_3004275 ANT(3'') ANT(3'')-IIa is a aminoglycoside nucleotidyltransferase identified in Acinetobacter spp. via horizontal gene transfer mechanisms. http://purl.obolibrary.org/obo/ARO_3004090 ANT(3'')-IIb http://purl.obolibrary.org/obo/ARO_3004275 ANT(3'') ANT(3'')-IIb is a aminoglycoside nucleotidyltransferase identified in Acinetobacter spp. via horizontal gene transfer mechanisms. http://purl.obolibrary.org/obo/ARO_3004091 ANT(3'')-IIc http://purl.obolibrary.org/obo/ARO_3004275 ANT(3'') ANT(3'')-IIc is a aminoglycoside nucleotidyltransferase identified in Acinetobacter spp. via horizontal gene transfer mechanisms. http://purl.obolibrary.org/obo/ARO_3004092 HMB-1 http://purl.obolibrary.org/obo/ARO_3004209 HMB beta-lactamase Shotgun cloning of beta-lactam resistant P. aeruginosa NRZ-03096 yielded a clone producing a novel subclass B1 enzyme with only 74.3% identity to the next nearest relative, KHM-1. The novel MBL was named HMB-1 (for Hamburg MBL). HMB-1 gene was chromosomally located as part of a Tn 3 family transposon that was named Tn 6345, where expression of bla HMB-1 in E. coli TOP10 led to increased resistance to beta-lactams. http://purl.obolibrary.org/obo/ARO_3004093 NDM-17 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase NDM-17 is a metallo-beta-lactamase isolated from Escherichia coli with enhanced carbapenemase activity compared to NDM-1. http://purl.obolibrary.org/obo/ARO_3004096 daptomycin resistant CdsA http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations to the CdsA phosphatidate cytidylyltransferase conferring resistance to daptomycin. http://purl.obolibrary.org/obo/ARO_3004097 Streptococcus mitis CdsA with mutation conferring daptomycin resistance http://purl.obolibrary.org/obo/ARO_3004096 daptomycin resistant CdsA CdsA is a phosphatidate cytidylyltransferase which plays a role in the production of membrane phosphatidylglycerol and cardiolipin. http://purl.obolibrary.org/obo/ARO_3004098 LpeAB http://purl.obolibrary.org/obo/ARO_0010004 resistance-nodulation-cell division (RND) antibiotic efflux pump LpeAB are components of an efflux pump, which is a macrolide resistance determinant in L. pneumophila Paris strain. Mutations observed in the upstream sequence of lpeAB operon in resistant lineages led to an overexpression of this efflux pump. Sub-inhibitory concentrations of macrolides themselves participated in upregulating this efflux and could constitute a first step in the acquisition of a high macrolide resistance level. As Lpp2879–Lpp2880 is homologous to Escherichia coli AcrAB, lpp2879–lpp2880 was renamed to lpeAB. http://purl.obolibrary.org/obo/ARO_3004099 LpeA http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance LpeA is a subunit of the LpeAB efflux pump in Legionella pneumophila, which is homologous to AcrA in E. coli. http://purl.obolibrary.org/obo/ARO_3004100 LpeB http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance LpeB is a subunit of the LpeAB efflux pump in Legionella pneumophila, which is homologous to AcrB in E. coli. http://purl.obolibrary.org/obo/ARO_3004101 MdtNOP http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump MdtNOP is a MFS efflux pump protein found in E. coli. The deletion of mdtP from strain W3110 resulted in increased susceptibility to acriflavin, puromycin, and tetraphenylarsonium chloride. An E. coli mdtN null mutant is more sensitive to sulfur drugs than wild type. http://purl.obolibrary.org/obo/ARO_3004102 kamB http://purl.obolibrary.org/obo/ARO_3004272 16S rRNA methyltransferase (A1408) Methyltransferase enzyme first described in Streptoalloteichus tenebrarius. Confers resistance to aminoglycoside antibiotics (esp. apramycin) through methylation of the 16S rRNA at A1408, thereby modifying the antibiotic target. http://purl.obolibrary.org/obo/ARO_3004103 QepA2 http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump QepA2 is a plasmid-mediated quinolone resistance pump found in an Escherichia coli isolate from France. http://purl.obolibrary.org/obo/ARO_3004104 TMB beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase TMB-1, the first known member of the Tripoli metallo-beta-lactamase family (TMB) was isolated from Achromobacter xylosoxidans in a Tripoli central hospital. TMB-1 was located on a class 1 integron and is a chromosomally-encoded beta-lactamase capable of hydrolyzing multiple antibiotics. http://purl.obolibrary.org/obo/ARO_3004105 TMB-1 http://purl.obolibrary.org/obo/ARO_3004104 TMB beta-lactamase TMB-1 is a TMB metallo-beta-lactamase found in Achromobacter sp. http://purl.obolibrary.org/obo/ARO_3004106 TMB-2 http://purl.obolibrary.org/obo/ARO_3004104 TMB beta-lactamase TMB-2 is a TMB metallo-beta-lactamase found in Acinetobacter sp. http://purl.obolibrary.org/obo/ARO_3004107 Pseudomonas aeruginosa soxR http://purl.obolibrary.org/obo/ARO_3000836 soxR SoxR is a redox-sensitive transcriptional activator that induces expression of a small regulon that includes the RND efflux pump-encoding operon mexGHI-opmD. SoxR was shown to be activated by pyocyanin. http://purl.obolibrary.org/obo/ARO_3004108 Enterobacter cloacae rob http://purl.obolibrary.org/obo/ARO_3000825 rob rob is a positive regulator for the acrAB efflux genes, and is structurally similar to SoxS and MarA. http://purl.obolibrary.org/obo/ARO_3004109 Escherichia coli rob http://purl.obolibrary.org/obo/ARO_3000825 rob rob is a positive regulator for the acrAB efflux genes, and is structurally similar to SoxS and MarA. http://purl.obolibrary.org/obo/ARO_3004110 MCR-2.1 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase MCR-2 is a plasmid-borne phosphoethanolamine transferase that interferes with binding of colistin to the cell membrane via addition of phosphoethanolamine to lipid A, resulting in reduction of the negative charge of the cell membrane. Originally identified in a Belgian sample of Escherichia coli by Xavier et al, (2016). http://purl.obolibrary.org/obo/ARO_3004111 FosA6 http://purl.obolibrary.org/obo/ARO_3000133 fosfomycin thiol transferase FosA6 is a plasmid-encoded enzyme that confers resistance to fosfomycin in Escherichia coli by breaking the epoxide ring of the molecule. http://purl.obolibrary.org/obo/ARO_3004112 phosphoethanolamine transferase conferring colistin resistance http://purl.obolibrary.org/obo/ARO_3003580 gene altering cell wall charge This group of enzymes catalyzes the addition of a phosphoethanolamine group to another molecule. The addition of this moiety to lipid A in bacterial species is often associated with polymyxin (otherwise known as colistin) resistance. http://purl.obolibrary.org/obo/ARO_3004113 FosA7 http://purl.obolibrary.org/obo/ARO_3000133 fosfomycin thiol transferase FosA7 is an enzyme that confers resistance to fosfomycin in Escherichia coli by breaking the epoxide ring of the molecule. http://purl.obolibrary.org/obo/ARO_3004114 porin OmpC http://purl.obolibrary.org/obo/ARO_3004281 General Bacterial Porin with reduced permeability to beta-lactams In the presence of antibiotic stress, there is a coupled down-regulation of the porin OmpC with the OmpF. Mutants both lacking both OmpC and OmpF proteins are resistant to cephaloridine and cefazolin. Analyses of genes involved in the increased resistance to tetracycline suggest that the up-regulation of efflux pump genes is accompanied by a decrease of OmpF and OmpC synthesis. Homologs of OmpC have been identified in Escherichia coli, Salmonella enterica, Klebsiella aerogenes and Serratia marcescens. http://purl.obolibrary.org/obo/ARO_3004115 nitroimidazole antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule Nitroimidazoles are a group of drugs that have both antiprotozoal and antibacterial activity, classified with respect to the location of the nitro functional group. http://purl.obolibrary.org/obo/ARO_3004116 nitrofuran antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule Nitrofurans are chemotherapeutic agents with antibacterial and antiprotozoal activity. http://purl.obolibrary.org/obo/ARO_3004117 Vibrio cholerae OmpU http://purl.obolibrary.org/obo/ARO_3004282 General Bacterial Porin with reduced permeability to peptide antibiotics A ToxR-Regulated outer membrane porin. In Vibrio cholerae, ToxR controls resistance to P2 (a BPI-derived antimicrobial peptide) by regulating the production of OmpU. OmpU also confers resistance to polymyxin B sulfate. http://purl.obolibrary.org/obo/ARO_3004118 Vibrio cholerae OmpT http://purl.obolibrary.org/obo/ARO_3004282 General Bacterial Porin with reduced permeability to peptide antibiotics A ToxR negatively regulated outer membrane porin. In Vibrio cholerae, ToxR controls resistance to P2 (a BPI-derived antimicrobial peptide) by regulating the production of OmpT, especially in the absence of OmpU. http://purl.obolibrary.org/obo/ARO_3004120 CBP C1-aminomethylene vancomycin http://purl.obolibrary.org/obo/ARO_3000081 glycopeptide antibiotic CBP C1-aminomethylene vancomycin is a synthetic vancomycin derivative which exhibits multiple synergistic mechanisms of action, allowing it to effectively inhibit otherwise-glycopeptide resistant Gram-positive bacteria (notably those with functioning VanA clusters). http://purl.obolibrary.org/obo/ARO_3004121 BPI http://purl.obolibrary.org/obo/ARO_3000053 peptide antibiotic Bactericidal/permeability-increasing (BPI) protein is a member of a new generation of proteins known as super-antibiotics that are implicated as endotoxin neutralising agents. The potent (nM) cytotoxicity of BPI is limited to gram-negative bacteria (GNB), reflecting the high affinity (<10 nM) of BPI for bacterial lipopolysaccharides (LPS). Binding of BPI to live bacteria via LPS causes immediate growth arrest, actual killing coincides with later damage to the inner membrane. http://purl.obolibrary.org/obo/ARO_3004122 Klebsiella pneumoniae OmpK37 http://purl.obolibrary.org/obo/ARO_3004281 General Bacterial Porin with reduced permeability to beta-lactams Klebsiella pneumoniae outer membrane porin protein. Is preferentially detected in porin-deficient strains. Functional characterization of this new porin revealed a narrower pore than those of porins OmpK35 and OmpK36, which did not allow penetration by certain beta-lactams. Also, when a resistant strain expresses porin OmpK37 is less susceptible to cefotaxime and cefoxitin than when it is expressing either OmpK36 or OmpK35. http://purl.obolibrary.org/obo/ARO_3004123 Burkholderia pseudomallei Omp38 http://purl.obolibrary.org/obo/ARO_3004281 General Bacterial Porin with reduced permeability to beta-lactams Heterologous expression of Burkholderia pseudomallei Omp38 (BpsOmp38) in Omp-deficient E. coli host cells lowers their permeability and in consequence, their antimicrobial susceptibility to penicillin G, cefoxitin, ceftazidime and imipenem. http://purl.obolibrary.org/obo/ARO_3004124 Moraxella catarrhalis M35 http://purl.obolibrary.org/obo/ARO_3003768 gene conferring resistance via absence The outer membrane protein M35 of Moraxella catarrhalis is an antigenically conserved porin. Down-regulation of M35 significantly increases the MICs of aminopenicillins, specifically amoxicillin. http://purl.obolibrary.org/obo/ARO_3004125 23S rRNA with mutation conferring resistance to macrolide antibiotics http://purl.obolibrary.org/obo/ARO_3000336 23S rRNA with mutation conferring antibiotic resistance Nucleotide point mutations in the 23S rRNA subunit may confer resistance to macrolide antibiotics. http://purl.obolibrary.org/obo/ARO_3004126 Escherichia coli LamB http://purl.obolibrary.org/obo/ARO_3003768 gene conferring resistance via absence LamB is a negative regulator for antibiotic resistance, it serves as a porin to influx antibiotic. When down-regulated, it increases resistance to chlortetracycline, ciprofloxacin, balofloxacin and nalidixic acid. It also interacts with Odp1, an energy metabolic enzyme, creating a complex that decreases in antibiotic-resistant strains. http://purl.obolibrary.org/obo/ARO_3004127 Escherichia coli mipA http://purl.obolibrary.org/obo/ARO_3003768 gene conferring resistance via absence MltA-interacting protein (mipA), is an antibiotic resistance-related outer membrane protein. Deletion of mipA increases kanamycin, nalidixic acid and streptomycin resistance. http://purl.obolibrary.org/obo/ARO_3004128 Serratia marcescens Omp1 http://purl.obolibrary.org/obo/ARO_3003768 gene conferring resistance via absence Omp1 is an outer membrane porin that confers resistance by absence in S. marcescens. Knockout, deletion or other inhibition of the omp1 gene confers resistance to certain beta-lactamase antibiotics - including Cefoxitin, Ceftriaxone, Cefotaxime, and Moxalactam - as well as Ciprofloxacin, Tetracycline, and Chloramphenicol, by preventing passage of the antibiotic into the cell. http://purl.obolibrary.org/obo/ARO_3004129 cephaloridine http://purl.obolibrary.org/obo/ARO_3009105 first-generation cephalosporin Cephaloridine is a semisynthetic, broad-spectrum, first-generation cephalosporin with antibacterial activity. Cephaloridine binds to and inactivates penicillin-binding proteins (PBPs) located on the inner membrane of the bacterial cell wall. PBPs are enzymes involved in the terminal stages of assembling the bacterial cell wall and in reshaping the cell wall during growth and division. Inactivation of PBPs interferes with the cross-linkage of peptidoglycan chains necessary for bacterial cell wall strength and rigidity. This results in the weakening of the bacterial cell wall and causes cell lysis. http://purl.obolibrary.org/obo/ARO_3004130 balofloxacin http://purl.obolibrary.org/obo/ARO_0000001 fluoroquinolone antibiotic Balofloxacin is an 8-methoxy fluoroquinolone antibiotic. It shows potent bactericidal activity and inhibits the supercoiling activity of DNA gyrase of S. aureus, E. coli, and P. aeruginosa. http://purl.obolibrary.org/obo/ARO_3004131 Escherichia coli 23S rRNA with mutation conferring resistance to erythromycin and telithromycin http://purl.obolibrary.org/obo/ARO_3004125 23S rRNA with mutation conferring resistance to macrolide antibiotics Point mutation in the 23S rRNA of Escherichia coli shown clinically to confer resistance to the macrolide-class antibiotics erythromycin and telithromycin. http://purl.obolibrary.org/obo/ARO_3004132 Chlamydomonas reinhardtii 23S rRNA with mutation conferring resistance to erythromycin http://purl.obolibrary.org/obo/ARO_3004125 23S rRNA with mutation conferring resistance to macrolide antibiotics Point mutation in 23S rRNA of C. reinhardtii chloroplast shown clinically to confer resistance to Erythromycin, a macrolide antibiotic. http://purl.obolibrary.org/obo/ARO_3004133 Brachyspira hyodysenteriae 23S rRNA with mutation conferring resistance to tylosin http://purl.obolibrary.org/obo/ARO_3004125 23S rRNA with mutation conferring resistance to macrolide antibiotics Point mutation in B. hyodysenteriae 23S rRNA shown to confer resistance to tylosin and erythromycin. http://purl.obolibrary.org/obo/ARO_3004134 Helicobacter pylori 23S rRNA with mutation conferring resistance to clarithromycin http://purl.obolibrary.org/obo/ARO_3004125 23S rRNA with mutation conferring resistance to macrolide antibiotics Point mutations in Helicobacter pylori shown to confer resistance to clarithromycin, a macrolide antibiotic. http://purl.obolibrary.org/obo/ARO_3004135 Mycobacterium tuberculosis iniB with mutation conferring resistance to ethambutol http://purl.obolibrary.org/obo/ARO_3004136 Ethambutol resistant iniB Point mutations in M. tuberculosis iniB shown to confer resistance to ethambutol. http://purl.obolibrary.org/obo/ARO_3004136 Ethambutol resistant iniB http://purl.obolibrary.org/obo/ARO_3004137 Antibiotic resistant iniB Point mutations occurring in the iniB region of the iniBAC operon shown to confer resistance to ethambutol. http://purl.obolibrary.org/obo/ARO_3004137 Antibiotic resistant iniB http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance iniB, an isoniazid-induced protein, is part of the iniBAC operon that participates in the development of tolerance to both isoniazid and ethambutol. May function through a MDR-pump like mechanism, although it does not appear to directly transport isoniazid from the cell. http://purl.obolibrary.org/obo/ARO_3004138 Moraxella catarrhalis 23S rRNA with mutation conferring resistance to macrolide antibiotics http://purl.obolibrary.org/obo/ARO_3004125 23S rRNA with mutation conferring resistance to macrolide antibiotics Point mutations in the 23S ribosomal RNA subunit of M. catarrhalis shown clinically to confer resistance to macrolide class antibiotics. http://purl.obolibrary.org/obo/ARO_3004139 MCR-3.1 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase MCR-3 is a plasmid-borne phosphoethanolamine transferase that interferes with binding of colistin to the cell membrane via addition of phosphoethanolamine to lipid A, resulting reduction in negative charge of the cell membrane. Originally described by Yin et al. 2017, from a porcine Escherichia coli plasmid pWJ1. http://purl.obolibrary.org/obo/ARO_3004140 hydrolysis of fusidic acid to inactive lactone derivative http://purl.obolibrary.org/obo/ARO_3000040 hydrolysis of antibiotic conferring resistance Enzymes shown to inactivate fusidic acid by hydrolytic cleavage from the 16 beta-position of fusidic acid and its derivatives. This converts fusidic acid to an inactivate lactone derivative, thus conferring resistance to fusidic acid. http://purl.obolibrary.org/obo/ARO_3004141 AxyXY-OprZ http://purl.obolibrary.org/obo/ARO_0010004 resistance-nodulation-cell division (RND) antibiotic efflux pump An RND-type efflux system that confers innate aminoglycoside resistance to Achromobacter spp. It has a transcriptional regulator encoded by the axyZ gene located upstream of axyXY-oprZ. In-frame axyZ gene deletion assay led to increased MICs of antibiotic substrates of the efflux system: aminoglycosides, cefepime, fluoroquinolones, tetracyclines and erythromycin, indicating that the product of axyZ negatively regulates expression of axyXY-oprZ. Moreover a 45 amino-acid substitution at position 29 of AxyZ (V29G) was identified in a clinical Achromobacter strain that occurred during the course of chronic respiratory tract colonization in a cystic fibrosis (CF) patient. This substitution, also detected in 3 other strains exposed in vitro to tobramycin, led to the increase in axyY transcription level (5 to 17-fold) together with the increase in antibiotic resistance level. http://purl.obolibrary.org/obo/ARO_3004142 OprZ http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance OprZ is the outer membrane component of the AxyXY-OprZ efflux pump system in Achromobacter spp. http://purl.obolibrary.org/obo/ARO_3004143 AxyX http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance AxyX is the inner membrane transporter of the AxyXY-OprZ efflux pump system in Achromobacter spp. http://purl.obolibrary.org/obo/ARO_3004144 AxyY http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance AxyY is the periplasmic adaptor protein of the AxyXY-OprZ efflux pump system in Achromobacter spp. http://purl.obolibrary.org/obo/ARO_3004145 AxyZ http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux AxyZ is a transcriptional regulator of the AxyXY-OprZ efflux pump system. http://purl.obolibrary.org/obo/ARO_3004146 cfrC http://purl.obolibrary.org/obo/ARO_3004610 cfr(C) Group A cfr-like 23S rRNA methyltransferase shown to confer resistance to linezolid and phenicol antibiotics, including florfenicol and chloramphenicol, in Clostridium. http://purl.obolibrary.org/obo/ARO_3004149 Escherichia coli 23S rRNA with mutation conferring resistance to clindamycin http://purl.obolibrary.org/obo/ARO_3004187 23S rRNA with mutation conferring resistance to lincosamide antibiotics Point mutation in the 23S rRNA of Escherichia coli shown clinically to confer resistance to clindamycin, a lincosamide antibiotic. http://purl.obolibrary.org/obo/ARO_3004150 Escherichia coli 23S rRNA with mutation conferring resistance to chloramphenicol http://purl.obolibrary.org/obo/ARO_3004188 23S rRNA with mutation conferring resistance to phenicol antibiotics Point mutation in the 23S rRNA of Escherichia coli shown clinically to confer resistance to chloramphenicol. http://purl.obolibrary.org/obo/ARO_3004152 aminosalicylate resistant thymidylate synthase http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Antibiotic resistant form of thymidylate synthase (synthetase), an enzyme that catalyzes the conversion of dUMP to dTMP in nucleotide biosynthesis. Loss-of-function mutations in thymidylate synthase confer resistance to p-aminosalicylic acid by disrupting the substrate-binding affinity and catalytic activity. http://purl.obolibrary.org/obo/ARO_3004153 Mycobacterium tuberculosis thyA with mutation conferring resistance to para-aminosalicylic acid http://purl.obolibrary.org/obo/ARO_3004152 aminosalicylate resistant thymidylate synthase Point mutations in the thymidylate synthetase thyA gene shown clinically to confer resistance to para-aminosalicylic acid. Loss-of-function mutations in thyA disrupt the catalytic activity and substrate-binding affinity, thus conferring resistance. http://purl.obolibrary.org/obo/ARO_3004154 antibiotic sensitive thymidylate synthase http://purl.obolibrary.org/obo/ARO_3000712 nucleic acid synthesis machinery targeted by antibiotic Thymidylate synthase (synthetase) catalyzes the conversion of dUMP to dTMP in the nucleic acid biosynthesis pathway. Inhibition of thyA imbalances the cellular concentration of dUMP causing DNA damage. http://purl.obolibrary.org/obo/ARO_3004155 aminosalicylate resistant dihydrofolate synthase http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Dihydrofolate synthase (synthetase) enzymes resistant to aminosalicylates (inc. para-aminosalicylic acid) caused by mutation. Dihydrofolate synthase is required for bioactivation of p-aminosalicylic acid, and mutation in dihydrofolate synthase inhibits production of the dihydrofolate analog hydroxyl-dihydrofolate, thus preventing activation and conferring resistance. http://purl.obolibrary.org/obo/ARO_3004156 antibiotic sensitive dihydrofolate synthase http://purl.obolibrary.org/obo/ARO_3000714 folate synthesis enzyme targeted by antibiotic Wild-type form of dihydrofolate synthase (synthetase) enzymes. Bioactivation of p-aminosalicylic acid occurs during the folate pathway when dihydrofolate and its analog hydroxyl-dihydrofolate are produced by dihydrofolate synthase. Disruption of this pathway by PAS results in cell damage and death. http://purl.obolibrary.org/obo/ARO_3004157 Mycobacterium tuberculosis folC with mutation conferring resistance to para-aminosalicylic acid http://purl.obolibrary.org/obo/ARO_3004155 aminosalicylate resistant dihydrofolate synthase Point mutations in the dihydrofolate synthetase folC gene shown clinically to confer resistance to p-aminosalicylic acid or other aminosalicylates. Mutations in folC inhibit bioactivation of PAS and thus confer resistance. http://purl.obolibrary.org/obo/ARO_3004159 Mycoplasma gallisepticum 23S rRNA mutation conferring resistance to pleuromutilin antibiotics http://purl.obolibrary.org/obo/ARO_3004178 23S rRNA with mutation conferring resistance to pleuromutilin antibiotics Point mutations in the 23S rRNA (domain V) of Mycoplasma gallisepticum can confer resistance to pleuromutilin antibiotics (tiamulin and valnemulin). The mutants also show cross-resistance to lincomycin, chloramphenicol and florfenicol. http://purl.obolibrary.org/obo/ARO_3004160 Escherichia coli 23S rRNA with mutation conferring resistance to clarithromycin http://purl.obolibrary.org/obo/ARO_3004125 23S rRNA with mutation conferring resistance to macrolide antibiotics Point mutation in the 23S rRNA of Escherichia coli shown clinically to confer resistance to clarithromycin, a macrolide antibiotic. http://purl.obolibrary.org/obo/ARO_3004161 Propionibacteria 23S rRNA with mutation conferring resistance to macrolide antibiotics http://purl.obolibrary.org/obo/ARO_3004125 23S rRNA with mutation conferring resistance to macrolide antibiotics Point mutation in the 23S rRNA of Propionibacteria shown clinically to confer resistance to macrolides. http://purl.obolibrary.org/obo/ARO_3004163 Mycobacteroides abscessus 23S rRNA with mutation conferring resistance to clarithromycin http://purl.obolibrary.org/obo/ARO_3004125 23S rRNA with mutation conferring resistance to macrolide antibiotics Point mutation in the 23S rRNA of Mycobacteroides abscessus shown to confer resistance to clarithromycin, a macrolide type antibiotic. http://purl.obolibrary.org/obo/ARO_3004164 Mycobacterium avium 23S rRNA with mutation conferring resistance to clarithromycin http://purl.obolibrary.org/obo/ARO_3004125 23S rRNA with mutation conferring resistance to macrolide antibiotics Point mutation in the 23S rRNA of Mycobacterium avium shown to confer resistance to clarithromycin, a macrolide type antibiotic. http://purl.obolibrary.org/obo/ARO_3004165 Mycobacteroides chelonae 23S rRNA with mutation conferring resistance to clarithromycin http://purl.obolibrary.org/obo/ARO_3004125 23S rRNA with mutation conferring resistance to macrolide antibiotics Point mutation in the 23S rRNA of Mycobacteroides chelonae shown to confer resistance to clarithromycin, a macrolide type antibiotic. http://purl.obolibrary.org/obo/ARO_3004166 Mycobacterium intracellulare 23S rRNA with mutation conferring resistance to clarithromycin http://purl.obolibrary.org/obo/ARO_3004125 23S rRNA with mutation conferring resistance to macrolide antibiotics Point mutation in the 23S rRNA of Mycobacterium intracellulare shown to confer resistance to clarithromycin, a macrolide type antibiotic. http://purl.obolibrary.org/obo/ARO_3004167 Mycobacterium intracellulare 23S rRNA with mutation conferring resistance to azithromycin http://purl.obolibrary.org/obo/ARO_3004125 23S rRNA with mutation conferring resistance to macrolide antibiotics Point mutation in the 23S rRNA of Mycobaccterium avium shown to confer resistance to azithromycin, a macrolide type antibiotic. http://purl.obolibrary.org/obo/ARO_3004168 Mycobacterium kansasii 23S rRNA with mutation conferring resistance to clarithromycin http://purl.obolibrary.org/obo/ARO_3004125 23S rRNA with mutation conferring resistance to macrolide antibiotics Point mutation in the 23S rRNA of Mycobacterium kansasii shown to confer resistance to clarithromycin, a macrolide type antibiotic. http://purl.obolibrary.org/obo/ARO_3004169 Mycolicibacterium smegmatis 23S rRNA with mutation conferring resistance to clarithromycin http://purl.obolibrary.org/obo/ARO_3004125 23S rRNA with mutation conferring resistance to macrolide antibiotics Point mutation in the 23S rRNA of Mycolicibacterium smegmatis shown to confer resistance to clarithromycin, a macrolide type antibiotic. http://purl.obolibrary.org/obo/ARO_3004170 Streptococcus pneumoniae 23S rRNA with mutation conferring resistance to macrolide antibiotics http://purl.obolibrary.org/obo/ARO_3004125 23S rRNA with mutation conferring resistance to macrolide antibiotics Point mutation in the 23S rRNA of Streptococcus pneumoniae shown to confer resistance to macrolide type antibiotics. http://purl.obolibrary.org/obo/ARO_3004171 Streptomyces ambofaciens 23S rRNA with mutation conferring resistance to macrolide antibiotics http://purl.obolibrary.org/obo/ARO_3004125 23S rRNA with mutation conferring resistance to macrolide antibiotics Point mutation in the 23S rRNA of Streptomyces ambofaciens shown to confer resistance to macrolide type antibiotics. http://purl.obolibrary.org/obo/ARO_3004172 23S rRNA with mutation conferring resistance to oxazolidinone antibiotics http://purl.obolibrary.org/obo/ARO_3000336 23S rRNA with mutation conferring antibiotic resistance Point mutations in the 23S rRNA subunit may confer resistance to oxazolidinone antibiotics. http://purl.obolibrary.org/obo/ARO_3004173 Escherichia coli 23S rRNA with mutation conferring resistance to oxazolidinone antibiotics http://purl.obolibrary.org/obo/ARO_3004172 23S rRNA with mutation conferring resistance to oxazolidinone antibiotics Point mutation in the 23S rRNA of Escherichia coli shown to confer resistance to oxazolidinone type antibiotics. http://purl.obolibrary.org/obo/ARO_3004174 Chlamydia trachomatis 23S rRNA with mutation conferring resistance to macrolide antibiotics http://purl.obolibrary.org/obo/ARO_3004125 23S rRNA with mutation conferring resistance to macrolide antibiotics Point mutation in the 23S rRNA of Chlamydia trachomatis shown to confer resistance to macrolide type antibiotics. http://purl.obolibrary.org/obo/ARO_3004176 Mycoplasma hominis 23S rRNA with mutation conferring resistance to macrolide antibiotics http://purl.obolibrary.org/obo/ARO_3004125 23S rRNA with mutation conferring resistance to macrolide antibiotics Point mutation in the 23S rRNA of Mycoplasma hominis shown to confer resistance to macrolide type antibiotics. http://purl.obolibrary.org/obo/ARO_3004177 Mycoplasmopsis fermentans 23S rRNA with mutation conferring resistance to macrolide antibiotics http://purl.obolibrary.org/obo/ARO_3004125 23S rRNA with mutation conferring resistance to macrolide antibiotics Point mutation in the 23S rRNA of Mycoplasmopsis fermentans shown to confer resistance to macrolide type antibiotics. http://purl.obolibrary.org/obo/ARO_3004178 23S rRNA with mutation conferring resistance to pleuromutilin antibiotics http://purl.obolibrary.org/obo/ARO_3000336 23S rRNA with mutation conferring antibiotic resistance Point mutations in the 23S rRNA subunit may confer resistance to pleuromutilin antibiotics. http://purl.obolibrary.org/obo/ARO_3004179 Mycoplasma pneumoniae 23S rRNA mutation conferring resistance to erythromycin http://purl.obolibrary.org/obo/ARO_3004125 23S rRNA with mutation conferring resistance to macrolide antibiotics Point mutation in the 23S rRNA of Mycoplasma pneumoniae shown to confer resistance to erythromycin. http://purl.obolibrary.org/obo/ARO_3004180 Halobacterium halobium 23S rRNA mutation conferring resistance to chloramphenicol http://purl.obolibrary.org/obo/ARO_3004188 23S rRNA with mutation conferring resistance to phenicol antibiotics Point mutation in the 23S rRNA of Halobacterium halobium shown to confer resistance to chloramphenicol. http://purl.obolibrary.org/obo/ARO_3004181 Streptococcus pneumoniae 23S rRNA mutation conferring resistance to macrolides and streptogramins antibiotics http://purl.obolibrary.org/obo/ARO_3004182 23S rRNA with mutation conferring resistance to streptogramins antibiotics Point mutation in the 23S rRNA of Streptococcus pneumoniae shown to confer resistance to macrolides and streptogramins types of antibiotics. http://purl.obolibrary.org/obo/ARO_3004182 23S rRNA with mutation conferring resistance to streptogramins antibiotics http://purl.obolibrary.org/obo/ARO_3000336 23S rRNA with mutation conferring antibiotic resistance Nucleotide point mutations in the 23S rRNA subunit may confer resistance to streptogramins antibiotics. http://purl.obolibrary.org/obo/ARO_3004183 aminosalicylate resistant dihydrofolate reductase http://purl.obolibrary.org/obo/ARO_3003425 antibiotic resistant dihydrofolate reductase Antibiotic target replacement dihydrofolate reductase enzymes or domains with catalytic activity that confer resistance to aminosalicylates, esp. p-aminosalicylic acid. http://purl.obolibrary.org/obo/ARO_3004184 Mycobacterium tuberculosis ribD with mutation conferring resistance to para-aminosalicylic acid http://purl.obolibrary.org/obo/ARO_3004183 aminosalicylate resistant dihydrofolate reductase ribD is a Mycobacterium tuberculosis riboflavin biosynthesis enzyme. Point mutations in ribD cause enzyme overexpression, which allows the C-terminal reductase domain to act as an alternative dihydrofolate reductase. Thus, mutations in ribD confer resistance to DHFR inhibitors such as para-aminosalicylic acid. http://purl.obolibrary.org/obo/ARO_3004185 mecD http://purl.obolibrary.org/obo/ARO_3001208 methicillin resistant PBP2 mecD is a PBP2a variant identified on a genomic resistance island in Macrococcus caseolyticus. MecD confers resistance to methicillin and other beta-lactam antibiotics through the production of an alternative low-affinity PBP. First described by Schwendener et al. 2017 and identified from canine and bovine sources. http://purl.obolibrary.org/obo/ARO_3004187 23S rRNA with mutation conferring resistance to lincosamide antibiotics http://purl.obolibrary.org/obo/ARO_3000336 23S rRNA with mutation conferring antibiotic resistance Point mutations in the 23S rRNA subunit may confer resistance to lincosamide antibiotics by reducing antibiotic binding-site affinity. http://purl.obolibrary.org/obo/ARO_3004188 23S rRNA with mutation conferring resistance to phenicol antibiotics http://purl.obolibrary.org/obo/ARO_3000336 23S rRNA with mutation conferring antibiotic resistance Point mutations in the 23S rRNA subunit shown clinically to confer resistance to phenicol class antibiotics, including chloramphenicol and florfenicol, by disrupting antibiotic binding-site affinity. http://purl.obolibrary.org/obo/ARO_3004189 Bla2 http://purl.obolibrary.org/obo/ARO_3004230 subclass B1 Bacillus anthracis Bla beta-lactamase Bla2 is a chromosomal-encoded beta-lactamase, found in Bacillus anthracis, which has penicillin, cephalosporin, and carbapenem-hydrolizing abilities. http://purl.obolibrary.org/obo/ARO_3004190 BlaA beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase BlaA beta-lactamases are Class A beta-lactamases first identified in Yersinia enterocolitica and have the ability to hydrolize penicilins and cephalosporins. http://purl.obolibrary.org/obo/ARO_3004191 APH(2'')-If http://purl.obolibrary.org/obo/ARO_3000128 APH(2'') Aminoglycoside 2''-phosphotransferase identified from the gram-negative pathogen Campylobacter jejuni. APH(2'')-If was shown to confer resistance to 4,6-disubstituted antibiotics kanamycin, tobramycin, dibekacin, gentamicin and sisomicin through antibiotic phosphorylation. Described by Toth et al. 2013. http://purl.obolibrary.org/obo/ARO_3004192 CepA beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase CepA beta-lactamases are Class A beta-lactamases found in Bateroides fragilis and have the ability to hydrolyze cephalosporin. http://purl.obolibrary.org/obo/ARO_3004194 MCR-1.2 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase A plasmid-borne novel MCR-1 functional variant detected in a Klebsiella pneumoniae isolate collected from a rectal swab in Italy. MCR-1.2 differs from MCR-1 by a single amino acid substitution from Glutamine to Leucine at position 3 in the N-terminal region. Described by DiPilato et al. 2016. http://purl.obolibrary.org/obo/ARO_3004196 VCC beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase VCC beta-lactamases are Class A beta-lactamases. http://purl.obolibrary.org/obo/ARO_3004197 BlaZ beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase BlaZ beta-lactamases are Class A beta-lactamases. These beta-lactamases are responsible for penicillin resistance in Staphylococcus aureus. http://purl.obolibrary.org/obo/ARO_3004198 R39 beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase R39 beta-lactamases are Class A beta-lactamases encoded in Actinomadura R39 with the ability to hydrolyze penicillins. http://purl.obolibrary.org/obo/ARO_3004199 CepS beta-lactamase http://purl.obolibrary.org/obo/ARO_3000076 class C beta-lactamase CepS beta-lactamases are Class C beta-lactamases capable of hydrolyzing cephalosporin. http://purl.obolibrary.org/obo/ARO_3004200 CfiA beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase CfiA beta-lactamases are chromosomal-encoded carbapenemase commonly found in Bacteroides fragilis isolates. http://purl.obolibrary.org/obo/ARO_3004201 BlaB beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase BlaB beta-lactamases are class B beta-lactamases that are found in a variety of species and have the ability to hydrolyze penams and carbapenems. http://purl.obolibrary.org/obo/ARO_3004202 JOHN beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase JOHN beta-lactamases hydrolyse penicillins, narrow- and expanded-spectrum cephalosporins, and carbapenems. http://purl.obolibrary.org/obo/ARO_3004203 CGB beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase CGB beta-lactamases are Class B beta-lactamases found in Chryseobacterium gleu that can hydrolyze penicillins; narrow- and expanded-spectrum cephalosporins; and carbapenems. http://purl.obolibrary.org/obo/ARO_3004204 EBR beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase EBR beta-lactamases are Class B beta-lactamases first isolated from Empedobacter brevis and are able to hydrolyze penicillins, cephalosporins, and carbapenems. http://purl.obolibrary.org/obo/ARO_3004205 TUS beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase TUS beta-lactamases are Class B beta-lactamases that can hydrolyze a variety of beta-lactams, such as cephems and carbapenems. http://purl.obolibrary.org/obo/ARO_3004206 SIM beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase SIM beta-lactamases are Class B beta-lactamases that are capable of hydrolyzing a wide variety of beta-lactams, including penicillins, narrow- to expanded-spectrum cephalosporins, and carbapenem. The SIM family of beta-lactamases appear to be transferable through integrons. http://purl.obolibrary.org/obo/ARO_3004207 KHM beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase KHM beta-lactamases are Class B beta-lactamases that can confer resistance to all classes of beta-lactams, except the monobactams. http://purl.obolibrary.org/obo/ARO_3004208 DIM beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase DIM type beta-lactamases were first identified from a carbapenem-resistant Pseudomonas stutzeri strain isolated from a Dutch patient. Encoded in mobile elements, these MBLs significantly hydrolyze broad-spectrum cephalosporins and carbapenems. http://purl.obolibrary.org/obo/ARO_3004209 HMB beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase First identified from a multi-drug resistant Pseudomonas aeruginosa clinical isolate in 2012, HMB type beta-lactamases can be encoded in transposons and hydrolyze carbapenems. http://purl.obolibrary.org/obo/ARO_3004210 SFH beta-lactamase http://purl.obolibrary.org/obo/ARO_3000570 subclass B2 (metallo-) beta-lactamase This type of Subclass B2 beta-lactamases was first identified from a Serratia fonticola environmental isolate. http://purl.obolibrary.org/obo/ARO_3004211 FEZ beta-lactamase http://purl.obolibrary.org/obo/ARO_3000571 subclass B3 (metallo-) beta-lactamase The FEZ family of beta-lactamases are subclass B3 beta-lactamases that hydrolyze penicillins, cephalosporins, and carbapenems. http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase http://purl.obolibrary.org/obo/ARO_3000571 subclass B3 (metallo-) beta-lactamase The GOB family of beta-lactamases have been discovered in the Elizabethkingia meningoseptica and are classified as subclass B3 beta-lactamase. They confer resistance to cephalosporins, penicillins, and carbapenems. http://purl.obolibrary.org/obo/ARO_3004213 GOB-18 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-18 is a member of subclass B3 GOB family of beta-lactamases isolated from Elizabethkingia meningoseptica. GOB-18 is unlike other subclass B3 beta-lactamases as it is fully active against a broad range of beta-lactam substrates using a single Zn(II) ion in its active site. http://purl.obolibrary.org/obo/ARO_3004214 THIN-B beta-lactamase http://purl.obolibrary.org/obo/ARO_3000571 subclass B3 (metallo-) beta-lactamase Beta-lactamases that are part of the THIN-B family, which is a subclass B3 beta-lactamase family and hydrolyze a broad spectrum of beta-lactams including penicillins, cephalosporins, and carbapenems. http://purl.obolibrary.org/obo/ARO_3004215 L1 family beta-lactamase http://purl.obolibrary.org/obo/ARO_3000571 subclass B3 (metallo-) beta-lactamase This subclass B3 of beta-lactamses have the ability to hydrolyze cephalosporins. http://purl.obolibrary.org/obo/ARO_3004216 AIM beta-lactamase http://purl.obolibrary.org/obo/ARO_3000571 subclass B3 (metallo-) beta-lactamase A subclass B3 family of beta-lactamases that confer resistance to a range of beta-lactam antibiotics including penams, cephamycins, and cephalosporins. http://purl.obolibrary.org/obo/ARO_3004217 SMB beta-lactamase http://purl.obolibrary.org/obo/ARO_3000571 subclass B3 (metallo-) beta-lactamase SMB beta-lactamases are a subclass B3 beta-lactamases that hydrolyze a variety of beta-lactams, including penicillins, cephalosporins, and carbapenems. http://purl.obolibrary.org/obo/ARO_3004218 CAU beta-lactamase http://purl.obolibrary.org/obo/ARO_3000571 subclass B3 (metallo-) beta-lactamase CAU beta-lactamases are a subclass B3 family. http://purl.obolibrary.org/obo/ARO_3004219 BJP beta-lactamase http://purl.obolibrary.org/obo/ARO_3000571 subclass B3 (metallo-) beta-lactamase BJP beta-lactamases are a subclass B3 family. http://purl.obolibrary.org/obo/ARO_3004220 subclass B3 PEDO beta-lactamase http://purl.obolibrary.org/obo/ARO_3000571 subclass B3 (metallo-) beta-lactamase PEDO family enzymes that are classified under subclass B3 (metallo-) beta-lactamases. http://purl.obolibrary.org/obo/ARO_3004221 CPS beta-lactamase http://purl.obolibrary.org/obo/ARO_3000571 subclass B3 (metallo-) beta-lactamase CPS beta-lactamases are a subclass B3 family. http://purl.obolibrary.org/obo/ARO_3004222 ESP beta-lactamase http://purl.obolibrary.org/obo/ARO_3000571 subclass B3 (metallo-) beta-lactamase ESP family beta-lactamases are subclass B3 (metallo-) beta-lactamases. http://purl.obolibrary.org/obo/ARO_3004223 MSI beta-lactamase http://purl.obolibrary.org/obo/ARO_3000571 subclass B3 (metallo-) beta-lactamase MSI beta-lactamases are a family of subclass B3 (metallo-) beta-lactamases. http://purl.obolibrary.org/obo/ARO_3004224 SPG beta-lactamase http://purl.obolibrary.org/obo/ARO_3000571 subclass B3 (metallo-) beta-lactamase SPG beta-lactamases are a family of subclass B3 (metallo-) beta-lactamases. http://purl.obolibrary.org/obo/ARO_3004225 Rm3 family beta-lactamase http://purl.obolibrary.org/obo/ARO_3000571 subclass B3 (metallo-) beta-lactamase A family encompassing subclass B3 Rm3-like beta-lactamases. http://purl.obolibrary.org/obo/ARO_3004226 subclass B3 LRA beta-lactamase http://purl.obolibrary.org/obo/ARO_3000571 subclass B3 (metallo-) beta-lactamase Beta-lactamases that are part of the LRA gene family and are classified as B3 (metallo-) beta-lactamases. http://purl.obolibrary.org/obo/ARO_3004227 subclass B1 PEDO beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase Beta-lactamases that are part of the PEDO gene family and are classified as subclass B1 (metallo-) beta-lactamases. http://purl.obolibrary.org/obo/ARO_3004228 class A LRA beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase Beta-lactamases that are part of the LRA gene family and are classified as Class A beta-lactamases. http://purl.obolibrary.org/obo/ARO_3004229 class A Bacillus anthracis Bla beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase Beta-lactamases belonging to the Bla genes from Bacillus anthracis that are classified as class A beta-lactamases. http://purl.obolibrary.org/obo/ARO_3004230 subclass B1 Bacillus anthracis Bla beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase Beta-lactamases belonging to the Bla genes from Bacillus anthracis that are classified as subclass B1 beta-lactamases. http://purl.obolibrary.org/obo/ARO_3004231 class C LRA beta-lactamase http://purl.obolibrary.org/obo/ARO_3000076 class C beta-lactamase Beta-lactamases that are part of the LRA gene family and are classified as Class C beta-lactamases. http://purl.obolibrary.org/obo/ARO_3004232 ampC-type beta-lactamase http://purl.obolibrary.org/obo/ARO_3000076 class C beta-lactamase AmpC beta-lactamases are clinically important class C beta-lactamase enzymes which confer resistance to cephalosporins and penicillin-like antibiotics. AmpC beta-lactamases are typically found in Enterobacteriaceae, and were described in Escherichia coli in 1940 as the first reported enzymatic deactivation of penicillin. The name AmpC connects these enzymes functionally across many species, however these enzymes are generally unnamed and not phylogenetically related. http://purl.obolibrary.org/obo/ARO_3004233 blaF family beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase Class A Beta-lactamases first isolated from Mycolicibacterium fortuitum. http://purl.obolibrary.org/obo/ARO_3004234 EXO beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase Beta-lactamases part of this family discovered in Streptomyces albus G. http://purl.obolibrary.org/obo/ARO_3004235 RCP beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase A family of class A beta-lactamases that have been discovered in the Rhodobacter genus. http://purl.obolibrary.org/obo/ARO_3004236 gimA family macrolide glycosyltransferase http://purl.obolibrary.org/obo/ARO_3000458 macrolide glycosyltransferase This family of macrolide glycosyltransferases derive from gimA, which was discovered in Streptomyces ambofaciens. http://purl.obolibrary.org/obo/ARO_3004237 mgt macrolide glycotransferase http://purl.obolibrary.org/obo/ARO_3000458 macrolide glycosyltransferase The mgt family encompasses macrolide glycotransferases of the Streptomyces genus. http://purl.obolibrary.org/obo/ARO_3004238 sulfonamide resistant sul http://purl.obolibrary.org/obo/ARO_3000381 antibiotic target replacement protein The sul genes encode forms of dihydropteroate synthase that confer resistance to sulfonamide. http://purl.obolibrary.org/obo/ARO_3004239 NPS-1 http://purl.obolibrary.org/obo/ARO_3004240 NPS beta-lactamase NPS-1 is a plasmid-encoded class D beta-lactamases identified from two Pseudomonas aeruginosa isolates in 1986. http://purl.obolibrary.org/obo/ARO_3004240 NPS beta-lactamase http://purl.obolibrary.org/obo/ARO_3000075 class D beta-lactamase NPS beta-lactamases are class D beta-lactamases that have partial hydrolyzing abilities against penicillins and cephalosporin. http://purl.obolibrary.org/obo/ARO_3004241 class D LRA beta-lactamase http://purl.obolibrary.org/obo/ARO_3000075 class D beta-lactamase Beta-lactamases that are part of the LRA gene family and are classified as Class D beta-lactamases. http://purl.obolibrary.org/obo/ARO_3004242 MSI-OXA family beta-lactamase http://purl.obolibrary.org/obo/ARO_3000075 class D beta-lactamase Members of the MSI-OXA family are class D beta-lactamases that encompass hybrids of MSI-1 and putative OXA homologues. http://purl.obolibrary.org/obo/ARO_3004243 RbpA bacterial RNA polymerase-binding protein http://purl.obolibrary.org/obo/ARO_3000507 rifampin-resistant RNA polymerase-binding protein RbpA is a family of bacterial RNA polymerase-binding proteins, which acts as a transcription factor and binds to the sigma subunit of RNA polymerase. http://purl.obolibrary.org/obo/ARO_3004244 DnaA chromosomal replication initiation protein http://purl.obolibrary.org/obo/ARO_3000507 rifampin-resistant RNA polymerase-binding protein The DnaA family of replication initiation proteins interact with RNA polymerase to confer resistance against rifampicin anitibiotics. http://purl.obolibrary.org/obo/ARO_3004245 fosC phosphotransferase family http://purl.obolibrary.org/obo/ARO_3000359 fosfomycin phosphotransferase The fosC family of phosphotransferases phosphorylate fosfomycin to confer resistance and have been found in various bacterial isolates. http://purl.obolibrary.org/obo/ARO_3004246 Fom phosphotransferase family http://purl.obolibrary.org/obo/ARO_3000359 fosfomycin phosphotransferase Two members of the Fom family have been identified, FomA and FomB. FomB must interact with FomA confer resistance to fosfomycin, however FomA is capable of conferring resistance alone. http://purl.obolibrary.org/obo/ARO_3004247 antibiotic-resistant GlpT http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Fosfomycin is transported bacterial cells through transporters, one of them being glycerol-3-phosphate, which is encoded by the GlpT gene. Mutations in the GlpT gene can confer resistance to fosfomycin. http://purl.obolibrary.org/obo/ARO_3004248 antibiotic-resistant UhpT http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant UhpT encodes a transporter that can import fosfomycin-type drugs into bacterial cells. Mutations to UhpT confer resistance. http://purl.obolibrary.org/obo/ARO_3004249 UhpA http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant UhpA acts as a positive regulator of UhpT, which is a transporter to bring fosfomycin drugs into bacterial cells. Mutations in UhpA that negatively impact the expression of UhpT can confer resistance. http://purl.obolibrary.org/obo/ARO_3004250 antibiotic-resistant ptsI phosphotransferase http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant PtsI family phosphotransferases are involved in cyclic AMP synthesis, which regulates glpT expression. Mutations in PtsI family genes can negatively affect expression of UhpT, which is needed for fosfomycin import. http://purl.obolibrary.org/obo/ARO_3004251 antibiotic-resistant cya adenylate cyclase http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Adenylate cyclases encoded by cya genes, which are involved in the synthesis cyclic AMP which regulates the fosfomycin transporter glpT. Mutations in cya genes can confer resistance to fosfomycin. http://purl.obolibrary.org/obo/ARO_3004253 vanU gene in vanG cluster http://purl.obolibrary.org/obo/ARO_3000575 vanU Also known as vanUG, is a vanG variant found in the vanG gene cluster. http://purl.obolibrary.org/obo/ARO_3004254 vanV gene in vanB cluster http://purl.obolibrary.org/obo/ARO_3002916 vanV Also known as vanVB, is a vanV variant found in the vanB gene cluster. It is found in some but not all vanB operons in E. faecalis, suggesting the existence of varied gene compositions in vanB operons. http://purl.obolibrary.org/obo/ARO_3004255 vanJ membrane protein http://purl.obolibrary.org/obo/ARO_3002976 gene(s) or protein(s) associated with a glycopeptide resistance cluster vanJ and vanJ homologue proteins confer resistance to teicoplanin. http://purl.obolibrary.org/obo/ARO_3004256 Bleomycin resistant protein http://purl.obolibrary.org/obo/ARO_3001207 gene involved in antibiotic sequestration Bleomycin resistant proteins (BRP) confer resistance to bleomycin and to bleomycin-like molecules. http://purl.obolibrary.org/obo/ARO_3004257 cpa acetyltransferase http://purl.obolibrary.org/obo/ARO_3000121 aminoglycoside acetyltransferase (AAC) Acetyltransferases of the cpa family confer resistance to capreomycin, an aminoglycoside antibiotic. http://purl.obolibrary.org/obo/ARO_3004260 Bah amidohydrolase http://purl.obolibrary.org/obo/ARO_3000557 antibiotic inactivation enzyme Bah amidohydrolases are membrane proteins that inactivate bacitracin. http://purl.obolibrary.org/obo/ARO_3004261 viomycin phosphotransferase http://purl.obolibrary.org/obo/ARO_3000557 antibiotic inactivation enzyme Viomycin family of phosphotransferases confer resistance to viomycin antibiotics. http://purl.obolibrary.org/obo/ARO_3004262 daptomycin resistant liaF http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations to the liaF accessory protein that confer resistance to daptomycin. http://purl.obolibrary.org/obo/ARO_3004263 daptomycin resistant liaR http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations to the liaR response regulator that confer resistance to daptomycin. http://purl.obolibrary.org/obo/ARO_3004264 daptomycin resistant liaS http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations in the liaS histidine kinase that confer daptomycin resistance. http://purl.obolibrary.org/obo/ARO_3004265 lysocin resistant menA http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Mutations to demA confer lycosin resistance. http://purl.obolibrary.org/obo/ARO_3007227 MCR-8.3 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-8-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007228 MCR-8.4 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-8-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007229 MCR-8.2 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-8-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007230 MCR-1.34 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-1-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007231 MCR-4.6 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-4-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007232 MCR-1.27 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-1-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007233 MCR-1.18 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-1-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007234 MCR-1.23 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-1-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007235 MCR-1.20 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-1-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007236 MCR-1.28 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-1-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007237 MCR-1.21 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-1-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007238 MCR-1.16 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-1-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007239 MCR-1.22 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-1-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007240 MCR-1.19 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-1-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007241 MCR-1.29 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-1-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007242 MCR-1.30 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-1-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007243 MCR-1.24 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-1-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007244 MCR-1.17 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-1-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007245 MCR-1.31 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-1-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007246 MCR-1.14 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-1-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007247 MCR-1.25 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-1-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007248 MCR-3.33 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-3-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007249 MCR-3.14 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-3-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007250 MCR-3.37 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-3-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007251 MCR-3.38 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-3-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007252 MCR-3.15 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-3-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007253 MCR-3.27 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-3-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007254 MCR-3.32 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-3-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007255 MCR-3.31 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-3-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007256 MCR-3.23 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-3-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007257 MCR-3.36 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-3-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007258 MCR-3.25 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-3-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007259 MCR-3.22 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-3-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007260 MCR-3.16 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-3-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007261 MCR-3.26 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-3-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007262 MCR-3.21 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-3-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007263 MCR-3.18 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-3-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007264 MCR-3.40 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-3-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007265 MCR-3.24 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-3-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007266 MCR-3.20 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-3-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007267 MCR-3.35 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-3-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007268 MCR-3.34 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-3-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007269 MCR-3.13 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-3-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007270 MCR-3.28 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-3-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007271 MCR-3.39 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-3-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007272 MCR-3.29 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-3-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007273 MCR-3.19 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-3-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007274 MCR-10.5 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-10-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007275 MCR-10.3 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-10-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007276 MCR-10.4 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-10-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007277 MCR-10.2 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-10-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007278 MCR-3.17 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-3-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007279 MCR-1.15 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-1-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007280 MCR-1.26 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-1-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007281 MCR-5.4 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-5-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007282 MCR-5.3 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-5-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007283 MCR-2.4 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-2-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007284 MCR-2.3 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-2-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007285 MCR-2.8 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-2-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007286 MCR-2.5 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-2-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007287 MCR-2.7 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-2-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007288 MCR-2.6 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-2-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007289 MCR-1.32 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-1-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007290 fosfomycin thiol transferase inhibitor http://purl.obolibrary.org/obo/ARO_3007222 inhibitor of antibiotic resistance mechanism Adjuvants shown to inhibit the action of fosfomycin thiol transferases. http://purl.obolibrary.org/obo/ARO_3007291 inhibitor of aminoglycoside inactivation enzyme http://purl.obolibrary.org/obo/ARO_3007222 inhibitor of antibiotic resistance mechanism Adjuvants shown to inhibit the action of aminoglycoside inactivating enzymes, such as the APH and AAC enzyme families. http://purl.obolibrary.org/obo/ARO_3007292 MCR phosphoethanolamine transferase inhibitor http://purl.obolibrary.org/obo/ARO_3007222 inhibitor of antibiotic resistance mechanism Adjuvants shown to inhibit the action of mobile colistin resistance phosphoethanolamine transferase genes. http://purl.obolibrary.org/obo/ARO_3007293 durlobactam http://purl.obolibrary.org/obo/ARO_3007008 diazabicyclooctane Durlobactam is a broad-spectrum diazabicyclooctane beta-lactamase inhibitor capable to inhibiting class A, C, and D beta-lactamases. http://purl.obolibrary.org/obo/ARO_3007294 ANT-431 http://purl.obolibrary.org/obo/ARO_3007136 unclassified metallo-beta-lactamase inhibitor ANT-431 is an experimental beta-lactamase inhibitor shown to inhibit the action of NDM-1 and VIM-2. http://purl.obolibrary.org/obo/ARO_3007295 nacubactam http://purl.obolibrary.org/obo/ARO_3007008 diazabicyclooctane Nacubactam is a diazabicyclooctane that inhibits a variety of class A and C beta-lactamases. http://purl.obolibrary.org/obo/ARO_3007296 zidebactam http://purl.obolibrary.org/obo/ARO_3007008 diazabicyclooctane Zidebactam is a diazabicyclooctane that inhibitors a variety of class A and C beta-lactamases. http://purl.obolibrary.org/obo/ARO_3007297 ARX1796 http://purl.obolibrary.org/obo/ARO_3007008 diazabicyclooctane ARX1796 is an orally bioavailable prodrug of avibactam. http://purl.obolibrary.org/obo/ARO_3007298 ledaborbactam http://purl.obolibrary.org/obo/ARO_3007131 boronic acid beta-lactamase inhibitor Ledaborbactam is an experimental boronic acid beta-lactamase inhibitor that has shown been show to inhibitor several serine beta-lactamases. http://purl.obolibrary.org/obo/ARO_3007299 ledaborbactam etzadroxil http://purl.obolibrary.org/obo/ARO_3007131 boronic acid beta-lactamase inhibitor Ledaborbactam Etzadroxil is an orally bioavailable prodrug of ledaborbactam. http://purl.obolibrary.org/obo/ARO_3007300 L-captopril http://purl.obolibrary.org/obo/ARO_3007136 unclassified metallo-beta-lactamase inhibitor L-captopril is a drug used to treat hypertension that has been shown to chelate certain metallo-beta-lactamases. http://purl.obolibrary.org/obo/ARO_3007301 D-captopril http://purl.obolibrary.org/obo/ARO_3007136 unclassified metallo-beta-lactamase inhibitor D-captopril is an isomer of L-captopril and is able to chelate certain metallo-beta-lactamases. http://purl.obolibrary.org/obo/ARO_3007302 thiorphan http://purl.obolibrary.org/obo/ARO_3007136 unclassified metallo-beta-lactamase inhibitor Thiorphan is the active metabolite of the antidieuretic drug racecadotril. It has shown inhibitory activity against various metallo-beta-lactamases. http://purl.obolibrary.org/obo/ARO_3007303 tiopronin http://purl.obolibrary.org/obo/ARO_3007136 unclassified metallo-beta-lactamase inhibitor Tiopronin is a drug used to prevent and manage kidney stones in cystinuria patients. It has shown inhibitory activity against various metallo-beta-lactamases. http://purl.obolibrary.org/obo/ARO_3007304 dimercaprol http://purl.obolibrary.org/obo/ARO_3007136 unclassified metallo-beta-lactamase inhibitor Dimercaprol is a compound used to treat acute arsenic poisoning, as well as poisoning of other metals such as mercury, gold, and antimony. It has shown inhibitory activity against various metallo-beta-lactamases. http://purl.obolibrary.org/obo/ARO_3007305 ME1071 http://purl.obolibrary.org/obo/ARO_3007136 unclassified metallo-beta-lactamase inhibitor ME1071 is an experimental metallo-beta-lactamase inhibitor. http://purl.obolibrary.org/obo/ARO_3007306 phosphonoformate http://purl.obolibrary.org/obo/ARO_3007290 fosfomycin thiol transferase inhibitor Phosphonoformate, also known as Forscarnet or Foscavir, is an antiviral drug used to treat Herpesviridae infections. It has also been shown to inhibit the fosfomycin thiol transferase fosA. http://purl.obolibrary.org/obo/ARO_3007307 phosphonoacetate http://purl.obolibrary.org/obo/ARO_3007290 fosfomycin thiol transferase inhibitor Phosphonoacetate is an experimental inhibitor of the fosfomycin thiol transferase fosA. http://purl.obolibrary.org/obo/ARO_3007308 acetylphosphonate http://purl.obolibrary.org/obo/ARO_3007290 fosfomycin thiol transferase inhibitor Phosphonoacetate is an experimental inhibitor of the fosfomycin thiol transferase fosA. http://purl.obolibrary.org/obo/ARO_3007309 quercetin http://purl.obolibrary.org/obo/ARO_3007322 inhibitors of AcrAB-TolC efflux pump Quercetin is a common plant flavonoid that has shown inhibitory activity against certain aminoglycoside inactivation enzymes. Quercetin is also able to inhibit antbiotic efflux pumps such as AcrAB-TolC. http://purl.obolibrary.org/obo/ARO_3007310 aranorosin http://purl.obolibrary.org/obo/ARO_3007291 inhibitor of aminoglycoside inactivation enzyme Aranorosin is a plant derived compound that has shown inhibitory activity against certain aminoglycoside inactivation enzymes. http://purl.obolibrary.org/obo/ARO_3007311 pterostilbene http://purl.obolibrary.org/obo/ARO_3007292 MCR phosphoethanolamine transferase inhibitor Pterostilbene is a stilbenoid compound with antioxidant effects found in members of the genus Vaccinium (blueberries). It has also been shown to partially inhibit the mobile colistin resistance gene MCR-1. http://purl.obolibrary.org/obo/ARO_3007312 SPR741 http://purl.obolibrary.org/obo/ARO_3007223 adjuvants enhancing antibiotic entry SPR741 is an experimental cationic peptide used to increase permeability of the outer membrane of Gram-negative bacteria. It is currently in clinical trials in combination with a variety of antibiotics. http://purl.obolibrary.org/obo/ARO_3007313 KL-L9P http://purl.obolibrary.org/obo/ARO_3007223 adjuvants enhancing antibiotic entry KL-L9P is an experimental peptide used to increase the permeability of Gram-negative bacterial membranes to enhance the entry of antibiotics such as linezolid, rifampicin, and clarithromycin. http://purl.obolibrary.org/obo/ARO_3007314 pentamidine http://purl.obolibrary.org/obo/ARO_3007223 adjuvants enhancing antibiotic entry Pentamidine is an antiparasitic compound used to treat a variety of infections such as African trypanosomiasis and leishamaniasis. It has also been shown to increase Gram-negative membrane permeability and enhance the entry of certain antibiotics. Pentamidine combined with linezolid had significant synergistic antibacterial effects against carbapenem-resistant Enterobacteriaceae pentamidine. The antimicrobial disrupts the outer membranes, dissipates the membrane potentials, and devitalizes the efflux pumps of CRE, thereby facilitating the intracellular accumulation of linezolid and reactive oxygen species (ROS), which ultimately kills the bacteria. http://purl.obolibrary.org/obo/ARO_3007315 MAC-0568743 http://purl.obolibrary.org/obo/ARO_3007223 adjuvants enhancing antibiotic entry MAC-0568743 is an experimental compound that has been shown to increase the permeability of Gram-negative membranes and enhance the entry of large-scaffold antibiotics. http://purl.obolibrary.org/obo/ARO_3007316 liproxstatin-1 http://purl.obolibrary.org/obo/ARO_3007223 adjuvants enhancing antibiotic entry Liproxstatin-1 is a ferroptosis inhibitor that has been shown to increase the permeability of Gram-negative membranes and enhance the entry of large-scaffold antibiotics. http://purl.obolibrary.org/obo/ARO_3007317 D-LANA14 http://purl.obolibrary.org/obo/ARO_3007225 adjuvants which alter physiology D-LANA-14 is a d-lysine conjugated aliphatic norspermidine analogue that has been shown to increase the permeability of Gram-negative membranes and enhance the entry of antibiotics. It is also able to inhibit the formation of bacterial biofilms. http://purl.obolibrary.org/obo/ARO_3007318 metformin http://purl.obolibrary.org/obo/ARO_3007223 adjuvants enhancing antibiotic entry Metformin is a first-line medication for type 2 diabetes. It has been shown to increase Gram-negative membrane permeability and enhance the entry of certain antibiotics, such as tetracyclines, beta-lactams, and rifampicin. Metformin is also able to inhibit antibiotic efflux pumps such as AcrAB-TolC and MdtK. http://purl.obolibrary.org/obo/ARO_3007319 bicarbonate http://purl.obolibrary.org/obo/ARO_3007223 adjuvants enhancing antibiotic entry Bicarbonate is an ion capable of increasing bacterial membrane permeability by altering the proton motive force. This enhances the entry of antibiotics. http://purl.obolibrary.org/obo/ARO_3007320 phenylalanine-arginine beta-naphthylamide http://purl.obolibrary.org/obo/ARO_3007225 adjuvants which alter physiology Phenylalanine-arginine beta-naphthylamide is a widely-used experimental efflux pump inhibitor. It has also been shown to increase Gram-negative membrane permeability and enhance the entry of antibiotics, even in efflux pump deficient strains. It is also able to inhibit the formation of bacterial biofilms and disrupt quorum sensing. http://purl.obolibrary.org/obo/ARO_3007321 inhibitors of tetK efflux pump http://purl.obolibrary.org/obo/ARO_3003932 antibiotic efflux inhibitor Compounds which inhibit the removal of antibiotics by the tetK efflux pump. http://purl.obolibrary.org/obo/ARO_3007322 inhibitors of AcrAB-TolC efflux pump http://purl.obolibrary.org/obo/ARO_3003932 antibiotic efflux inhibitor Compounds which inhibit the removal of antibiotics by the AcrAB-TolC efflux pump. http://purl.obolibrary.org/obo/ARO_3007323 inhibitors of MdeA efflux pump http://purl.obolibrary.org/obo/ARO_3003932 antibiotic efflux inhibitor Compounds which inhibit the removal of antibiotics by the MdeA efflux pump. http://purl.obolibrary.org/obo/ARO_3007324 inhibitors of Rv1258c efflux pump http://purl.obolibrary.org/obo/ARO_3003932 antibiotic efflux inhibitor Compounds which inhibit the removal of antibiotics by the Rv1258c (Tap) efflux pump. http://purl.obolibrary.org/obo/ARO_3007325 inhibitors of NorA efflux pump http://purl.obolibrary.org/obo/ARO_3003932 antibiotic efflux inhibitor Compounds which inhibit the removal of antibiotics by the NorA efflux pump. http://purl.obolibrary.org/obo/ARO_3007326 inhibitors of CmeABC efflux pump http://purl.obolibrary.org/obo/ARO_3003932 antibiotic efflux inhibitor Compounds which inhibit the removal of antibiotics by the CmeABC efflux pump. http://purl.obolibrary.org/obo/ARO_3007327 inhibitors of MexAB-OprM efflux pump http://purl.obolibrary.org/obo/ARO_3003932 antibiotic efflux inhibitor Compounds which inhibit the removal of antibiotics by the MexAB-OprM efflux pump. http://purl.obolibrary.org/obo/ARO_3007328 inhibitors of MdtK efflux pump http://purl.obolibrary.org/obo/ARO_3003932 antibiotic efflux inhibitor Compounds which inhibit the removal of antibiotics by the MdtK efflux pump. http://purl.obolibrary.org/obo/ARO_3007329 baicalin http://purl.obolibrary.org/obo/ARO_3007225 adjuvants which alter physiology Baicalin is a flavonoid compound that is able to inhibit the activity of tetK and MsrA antibiotic efflux pumps. It is also able to inhibit the formation of bacterial biofilms and disrupt quorum sensing. http://purl.obolibrary.org/obo/ARO_3007330 reserpine http://purl.obolibrary.org/obo/ARO_3007322 inhibitors of AcrAB-TolC efflux pump Reserpine is an alkaloid compound that is able to inhibit the activity of the AcrAB-TolC antibiotic efflux system. http://purl.obolibrary.org/obo/ARO_3007331 piperine http://purl.obolibrary.org/obo/ARO_3007325 inhibitors of NorA efflux pump Piperine is an alkaloid compound that is able to inhibit the activity of NorA, MdeA, and Rv1258c (Tap) antibiotic efflux pumps. http://purl.obolibrary.org/obo/ARO_3007332 piperidine http://purl.obolibrary.org/obo/ARO_3007325 inhibitors of NorA efflux pump Piperidine is an alkaloid compound that is able to inhibit the activity of the NorA antibiotic efflux pump. http://purl.obolibrary.org/obo/ARO_3007333 verapamil http://purl.obolibrary.org/obo/ARO_3007324 inhibitors of Rv1258c efflux pump Verapamil is a blood-pressure medication that acts by blocking calcium channels. It is also able to inhibit the antibiotic efflux pump Rv1258c (Tap). http://purl.obolibrary.org/obo/ARO_3007334 norverapamil http://purl.obolibrary.org/obo/ARO_3007324 inhibitors of Rv1258c efflux pump Norverapamil is a metabolite of verapamil that is able to inhibit the antibiotic efflux pump Rv1258c (Tap). http://purl.obolibrary.org/obo/ARO_3007335 chlorpromazine http://purl.obolibrary.org/obo/ARO_3007322 inhibitors of AcrAB-TolC efflux pump Chlorpromazine is a medication used to treat disorders such as schizophrenia. It is also able to inhibit bacterial antibiotic efflux pumps such as AcrAB-TolC. http://purl.obolibrary.org/obo/ARO_3007336 amitriptyline http://purl.obolibrary.org/obo/ARO_3007322 inhibitors of AcrAB-TolC efflux pump Amitriptyline is an antidepressant used to treat a variety of conditions such as cyclic vomiting syndrome, major depressive disorder, fibromyalgia. Is is also able to inhibit bacterial antibiotic efflux pumps such as AcrAB-TolC. http://purl.obolibrary.org/obo/ARO_3007337 thioridazine http://purl.obolibrary.org/obo/ARO_3007225 adjuvants which alter physiology Thioridazine is a phenothiazine drug used in the treatment of schizophrenia and psychosis. It is also able to inhibit mycobacterial antibiotic efflux pumps and the formation of bacterial biofilms. http://purl.obolibrary.org/obo/ARO_3007338 biochanin A http://purl.obolibrary.org/obo/ARO_3003932 antibiotic efflux inhibitor Biochanin A is a flavonoid compound that is able to inhibit mycobacterial antibiotic efflux pumps. http://purl.obolibrary.org/obo/ARO_3007339 phloretin http://purl.obolibrary.org/obo/ARO_3007325 inhibitors of NorA efflux pump Phloretin is a plant-derived phenol that is able to inhibit the antibiotic efflux pump NorA. http://purl.obolibrary.org/obo/ARO_3007340 epigallocatechin gallate http://purl.obolibrary.org/obo/ARO_3007326 inhibitors of CmeABC efflux pump Epigallocatechin gallate is a flavonol that is able to inhibit antibiotic efflux pumps such as CmeABC, NorA, and tetK. http://purl.obolibrary.org/obo/ARO_3007341 hesperetin http://purl.obolibrary.org/obo/ARO_3007325 inhibitors of NorA efflux pump Hesperetin is a flavonoid compound that is able to inhibit antibiotic efflux pumps such as NorA. http://purl.obolibrary.org/obo/ARO_3007342 naringenin http://purl.obolibrary.org/obo/ARO_3007325 inhibitors of NorA efflux pump Naringenin is a flavonoid compound that is able to inhibit antibiotic efflux pumps such as NorA. http://purl.obolibrary.org/obo/ARO_3007343 sophoraflavanone G http://purl.obolibrary.org/obo/ARO_3007325 inhibitors of NorA efflux pump Sophoraflavanone G is a phytoncide derived from members of the Sophora genus. It is able to inhibit antibiotic efflux pumps such as NorA. http://purl.obolibrary.org/obo/ARO_3007344 chrysoeriol http://purl.obolibrary.org/obo/ARO_3007325 inhibitors of NorA efflux pump Chrysoeriol is a derivative of the flavone luteolin. It has been shown to inhibit antibiotic efflux pumps such as NorA. http://purl.obolibrary.org/obo/ARO_3007345 sideroxylin http://purl.obolibrary.org/obo/ARO_3007325 inhibitors of NorA efflux pump Sideroxylin is a flavone compound that is able to inhibit antibiotic efflux pumps such as NorA. http://purl.obolibrary.org/obo/ARO_3007346 6-desmethylsideroxylin http://purl.obolibrary.org/obo/ARO_3007325 inhibitors of NorA efflux pump 6-desmethylsideroxylin is a flavone compound that is able to inhibit antibiotic efflux pumps such as NorA. http://purl.obolibrary.org/obo/ARO_3007347 8-desmethylsideroxylin http://purl.obolibrary.org/obo/ARO_3007325 inhibitors of NorA efflux pump 8-desmethylsideroxylin is a flavone compound that is able to inhibit antibiotic efflux pumps such as NorA. http://purl.obolibrary.org/obo/ARO_3007348 diosmetin http://purl.obolibrary.org/obo/ARO_3007325 inhibitors of NorA efflux pump Diosmetin is a flavone compound that is able to inhibit antibiotic efflux pumps such as NorA. http://purl.obolibrary.org/obo/ARO_3007349 chrysosplenetin http://purl.obolibrary.org/obo/ARO_3007325 inhibitors of NorA efflux pump Chrysoplenetin is a flavone compound that is able to inhibit antibiotic efflux pumps such as NorA. http://purl.obolibrary.org/obo/ARO_3007350 galangin http://purl.obolibrary.org/obo/ARO_3007325 inhibitors of NorA efflux pump Galangin is a flavone compound that is able to inhibit antibiotic efflux pumps such as NorA. http://purl.obolibrary.org/obo/ARO_3007351 kaempferol http://purl.obolibrary.org/obo/ARO_3007325 inhibitors of NorA efflux pump Kaempferol is a flavone compound that is able to inhibit antibiotic efflux pumps such as NorA. http://purl.obolibrary.org/obo/ARO_3007352 kaempferol rhamnoside http://purl.obolibrary.org/obo/ARO_3007325 inhibitors of NorA efflux pump Kaempferol rhamnoside is a flavone compound that is able to inhibit antibiotic efflux pumps such as NorA. http://purl.obolibrary.org/obo/ARO_3007353 myricitrin http://purl.obolibrary.org/obo/ARO_3007325 inhibitors of NorA efflux pump Myricitrin is a flavone compound that is able to inhibit antibiotic efflux pumps such as NorA. http://purl.obolibrary.org/obo/ARO_3007354 penduletin http://purl.obolibrary.org/obo/ARO_3007325 inhibitors of NorA efflux pump Pendeuletin is a flavone compound that is able to inhibit antibiotic efflux pumps such as NorA. http://purl.obolibrary.org/obo/ARO_3007355 tiliroside http://purl.obolibrary.org/obo/ARO_3007325 inhibitors of NorA efflux pump Tiliroside is a flavone compound that is able to inhibit antibiotic efflux pumps such as NorA. http://purl.obolibrary.org/obo/ARO_3007356 daidzein http://purl.obolibrary.org/obo/ARO_3007327 inhibitors of MexAB-OprM efflux pump Daidzein is a flavonolignan compound found in soybeans and other legumes. It has been shown to inhibit antibiotic efflux pumps such as AcrAB-TolC and MexAB-OprM. http://purl.obolibrary.org/obo/ARO_3007357 genistein http://purl.obolibrary.org/obo/ARO_3007325 inhibitors of NorA efflux pump Genistein is a flavonolignan compound that is able to inhibit antibiotic efflux pumps such as NorA. http://purl.obolibrary.org/obo/ARO_3007358 orobol http://purl.obolibrary.org/obo/ARO_3007325 inhibitors of NorA efflux pump Orobol is a flavonolignan compound that is able to inhibit antibiotic efflux pumps such as NorA. http://purl.obolibrary.org/obo/ARO_3007359 MBX-2319 http://purl.obolibrary.org/obo/ARO_3007322 inhibitors of AcrAB-TolC efflux pump MBX-2319 is an experimental compound used to inhibit the AcrAB-TolC antibiotic efflux system. http://purl.obolibrary.org/obo/ARO_3007360 capsaicin http://purl.obolibrary.org/obo/ARO_3007325 inhibitors of NorA efflux pump Capsaicin is a compound found in chili peppers and is used to treat nerve pain. It is also able to inhibit antibiotic efflux pumps such as NorA. http://purl.obolibrary.org/obo/ARO_3007361 rutin http://purl.obolibrary.org/obo/ARO_3007225 adjuvants which alter physiology Rutin is a plant pigment that is able to inhibit bacterial biofilm formation. http://purl.obolibrary.org/obo/ARO_3007362 citral http://purl.obolibrary.org/obo/ARO_3007225 adjuvants which alter physiology Citral is a monoterpene aldehyde derived from a variety of plant oils that is able to inhibit bacterial biofilm formation and quorum sensing. http://purl.obolibrary.org/obo/ARO_3007363 furanone http://purl.obolibrary.org/obo/ARO_3007225 adjuvants which alter physiology Furanone is a heterocyclic organic compound that disrupts bacterial quorum sensing. http://purl.obolibrary.org/obo/ARO_3007364 cefepime-tazobactam http://purl.obolibrary.org/obo/ARO_3000707 antibiotic mixture A mixture of the beta-lactam antibiotic cefepime and the beta-lactamase inhibitor tazobactam. http://purl.obolibrary.org/obo/ARO_3007365 cefepime-enmetazobactam http://purl.obolibrary.org/obo/ARO_3000707 antibiotic mixture A mixture of the beta-lactam antibiotic cepefime and the beta-lactamase inhibitor enmetazobactam. http://purl.obolibrary.org/obo/ARO_3007366 aztreonam-avibactam http://purl.obolibrary.org/obo/ARO_3000707 antibiotic mixture A mixture of the beta-lactam antibiotic aztreonam and the beta-lactamase inhibitor avibactam. http://purl.obolibrary.org/obo/ARO_3007367 L-CS319 http://purl.obolibrary.org/obo/ARO_3007135 bisthiazolidine metallo-beta-lactamase inhibitor L-CS319 is an experimental bisthiazolidine metallo-beta-lactamase inhibitor capable of inhibiting the action of NDM-1. http://purl.obolibrary.org/obo/ARO_3007368 FosG http://purl.obolibrary.org/obo/ARO_3000133 fosfomycin thiol transferase FosG is a glutathione transferase that confers resistance to fosfomycin. http://purl.obolibrary.org/obo/ARO_3007369 FosH http://purl.obolibrary.org/obo/ARO_3000133 fosfomycin thiol transferase FosH is a hydrolase that confers resistance to fosfomycin. http://purl.obolibrary.org/obo/ARO_3007370 FosI http://purl.obolibrary.org/obo/ARO_3000133 fosfomycin thiol transferase FosI is a fosfomycin resistance gene. http://purl.obolibrary.org/obo/ARO_3007371 FosA8 http://purl.obolibrary.org/obo/ARO_3000133 fosfomycin thiol transferase FosA8 is a plasmid-located fosfomycin resistance gene. http://purl.obolibrary.org/obo/ARO_3007372 FosBx1 http://purl.obolibrary.org/obo/ARO_3000133 fosfomycin thiol transferase FosBx1 is a fosfomycin resistance gene. http://purl.obolibrary.org/obo/ARO_3007373 PJM beta-lactamase http://purl.obolibrary.org/obo/ARO_3000571 subclass B3 (metallo-) beta-lactamase A family of subclass B3 metallo-beta-lactamases with activity against a range of beta-lactam antibiotics. http://purl.obolibrary.org/obo/ARO_3007374 PJM-1 http://purl.obolibrary.org/obo/ARO_3007373 PJM beta-lactamase PJM-1 is a chromosomally-encoded subclass B3 metallo-beta-lactamase found in P. japonensis confering resistance to a range of antibiotics including ampicillin, cefalotin, and cefoxitin. http://purl.obolibrary.org/obo/ARO_3007375 KPC-87 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-87 is a chromosome-encoded carbapenemase found in Klebsiella pneumonia. http://purl.obolibrary.org/obo/ARO_3007376 gentamicin X http://purl.obolibrary.org/obo/ARO_3007382 gentamicin Gentamicin X is an aminoglycoside antibiotic. It is a precursor of gentamicin C and a minor component of the gentamicin antibiotic mixture. http://purl.obolibrary.org/obo/ARO_3007377 6'-N-ethylnetilmicin http://purl.obolibrary.org/obo/ARO_0000016 aminoglycoside antibiotic 6'-N-ethylnetilmicin is an aminoglycoside antibiotic and a derivative of netilmicin. http://purl.obolibrary.org/obo/ARO_3007378 2'-N-ethylnetilmicin http://purl.obolibrary.org/obo/ARO_0000016 aminoglycoside antibiotic 2'-N-ethylnetilmicin is an aminoglycoside antibiotic and a derivative of netilmicin. http://purl.obolibrary.org/obo/ARO_3007379 5-episisomicin http://purl.obolibrary.org/obo/ARO_0000016 aminoglycoside antibiotic 5-episosomicin is a semisynthetic aminoglycoside antibiotic similar to sisomicin. http://purl.obolibrary.org/obo/ARO_3007380 aminoglycoside modifying enzyme http://purl.obolibrary.org/obo/ARO_3000557 antibiotic inactivation enzyme Resistance-conferring genetic elements encoding proteins involved in the enzymatic inactivation of aminoglycoside antibiotics through chemical modification. http://purl.obolibrary.org/obo/ARO_3007381 KPC-86 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-86 is a chromosome-encoded carbapenemase found in Klebsiella pneumonia. http://purl.obolibrary.org/obo/ARO_3007382 gentamicin http://purl.obolibrary.org/obo/ARO_3000707 antibiotic mixture Gentamicin is a commonly used aminoglycoside antibiotic derived from members of the Micromonospora genus of bacteria. It acts by binding the 30S ribosomal subunit, thus inhibiting protein synthesis. Gentamicin is typically used to treat Gram-negative infections of the repiratory and urinary tract, as well as infections of the bone and soft tissue. It also exhibits considerable nephrotoxicity and ototoxicity. Gentamicin is administered as a mixture of gentamicin type C (which makes about around 80% of the complex) and types A, B, and X (distributed in the remaining 20% of the complex). http://purl.obolibrary.org/obo/ARO_3007383 KPC-95 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-95 is a chromosome-encoded carbapenemase found in Klebsiella pneumonia. http://purl.obolibrary.org/obo/ARO_3007384 AAC(3)-I http://purl.obolibrary.org/obo/ARO_3000322 AAC(3) A family of aminoglycoside 3-N-acetyltransferase enzymes which inactivate gentamicin through enzymatic acetylation, thereby conferring resistance to these compounds. http://purl.obolibrary.org/obo/ARO_3007385 AAC(3)-II http://purl.obolibrary.org/obo/ARO_3000322 AAC(3) A family of aminoglycoside 3-N-acetyltransferase enzymes which inactivate gentamicin and tobramycin through enzymatic acetylation, thereby conferring resistance to these compounds. http://purl.obolibrary.org/obo/ARO_3007386 AAC(3)-III http://purl.obolibrary.org/obo/ARO_3000322 AAC(3) A family of aminoglycoside 3-N-acetyltransferase enzymes which inactivate gentamicin, tobramycin and kanamycin through enzymatic acetylation, thereby conferring resistance to these compounds. http://purl.obolibrary.org/obo/ARO_3007387 AAC(3)-IV http://purl.obolibrary.org/obo/ARO_3000322 AAC(3) A family of aminoglycoside 3-N-acetyltransferase enzymes which inactivate gentamicin, tobramycin and apramycin through enzymatic acetylation, thereby conferring resistance to these compounds. http://purl.obolibrary.org/obo/ARO_3007388 AAC(3)-VI http://purl.obolibrary.org/obo/ARO_3000322 AAC(3) A family of aminoglycoside 3-N-acetyltransferase enzymes which inactivate gentamicin and ethylnetilmicin through enzymatic acetylation, thereby conferring resistance to these compounds. http://purl.obolibrary.org/obo/ARO_3007389 AAC(3)-VII http://purl.obolibrary.org/obo/ARO_3000322 AAC(3) A family of aminoglycoside 3-N-acetyltransferase enzymes which inactivate paronomycin through enzymatic acetylation, thereby conferring resistance to these compounds. http://purl.obolibrary.org/obo/ARO_3007390 AAC(3)-VIII http://purl.obolibrary.org/obo/ARO_3000322 AAC(3) A family of aminoglycoside 3-N-acetyltransferase enzymes which inactivate neomycin through enzymatic acetylation, thereby conferring resistance to these compounds. http://purl.obolibrary.org/obo/ARO_3007391 AAC(3)-IX http://purl.obolibrary.org/obo/ARO_3000322 AAC(3) A family of aminoglycoside 3-N-acetyltransferase enzymes which inactivate neomycin through enzymatic acetylation, thereby conferring resistance to these compounds. http://purl.obolibrary.org/obo/ARO_3007392 AAC(3)-X http://purl.obolibrary.org/obo/ARO_3000322 AAC(3) A family of aminoglycoside 3-N-acetyltransferase enzymes which inactivate kanamycin through enzymatic acetylation, thereby conferring resistance to these compounds. http://purl.obolibrary.org/obo/ARO_3007393 AAC(2')-I http://purl.obolibrary.org/obo/ARO_3000341 AAC(2') A family of aminoglycoside 2'-N-acetyltransferase enzymes which inactivate gentamicin and tobramycin through enzymatic acetylation, thereby conferring resistance to these compounds. http://purl.obolibrary.org/obo/ARO_3007394 AAC(2')-II http://purl.obolibrary.org/obo/ARO_3000341 AAC(2') A family of aminoglycoside 2'-N-acetyltransferase enzymes which inactivate kasugamycin through enzymatic acetylation, thereby conferring resistance to these compounds. http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I http://purl.obolibrary.org/obo/ARO_3000345 AAC(6') A family of aminoglycoside 6'-N-acetyltransferase enzymes which inactivate amikacin and tobramycin through enzymatic acetylation, thereby conferring resistance to these compounds. http://purl.obolibrary.org/obo/ARO_3007396 AAC(6')-II http://purl.obolibrary.org/obo/ARO_3000345 AAC(6') A family of aminoglycoside 6'-N-acetyltransferase enzymes which inactivate gentamicin and tobramycin through enzymatic acetylation, thereby conferring resistance to these compounds. http://purl.obolibrary.org/obo/ARO_3007397 Swedish Reference Group for Antibiotics (SIR) http://purl.obolibrary.org/obo/ARO_3004360 antimicrobial resistance testing reference standard SIR is a revised system for antibiotic sensitivity testing in Sweden that was proposed in 1977. The SIR system included two main changes: three sensitivity groups instead of the previous four and new breakpoints for the sensitivity groups. http://purl.obolibrary.org/obo/ARO_3007398 Werkgroep Richtlijnen Gevoeligheidsbepalingen (WRG) http://purl.obolibrary.org/obo/ARO_3004360 antimicrobial resistance testing reference standard The WRG is a standardized antimicrobial susceptibility testing methodology created by the Dutch Commissie Richtlijnen Gevoeligheidsbepalingen in 1981. http://purl.obolibrary.org/obo/ARO_3007399 ANT(6)-I http://purl.obolibrary.org/obo/ARO_3000225 ANT(6) A family of aminoglycoside 6-O-nucleotidyltransferase enzymes which inactivate streptomycin by catalyzing the transfer of an AMP group from an ATP substrate, thereby conferring resistance to these compounds. http://purl.obolibrary.org/obo/ARO_3007400 ANT(9)-I http://purl.obolibrary.org/obo/ARO_3000228 ANT(9) A family of aminoglycoside 9-O-nucleotidyltransferase enzymes which inactivate spectinomycin by catalyzing the transfer of an AMP group from an ATP substrate, thereby conferring resistance to these compounds. http://purl.obolibrary.org/obo/ARO_3007401 ANT(9)-Ib http://purl.obolibrary.org/obo/ARO_3007400 ANT(9)-I A plasmid-borne ANT(9)-I variant identified from Enterococcus faecalis. ANT(9)-Ib confers resistance to spectinomycin through enzymatic inactivation. http://purl.obolibrary.org/obo/ARO_3007402 KPC-94 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-94 is a mutated carbapenemase allele found in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3007403 ANT(4')-I http://purl.obolibrary.org/obo/ARO_3000229 ANT(4') A family of aminoglycoside 4'-O-nucleotidyltransferase enzymes which inactivate amikacin, tobramycin & dibekacin by catalyzing the transfer of an AMP group from an ATP substrate, thereby conferring resistance to these compounds. http://purl.obolibrary.org/obo/ARO_3007404 ANT(4')-II http://purl.obolibrary.org/obo/ARO_3000229 ANT(4') A family of aminoglycoside 4'-O-nucleotidyltransferase enzymes which inactivate amikacin & tobramycin, but not dibekacin, by catalyzing the transfer of an AMP group from an ATP substrate, thereby conferring resistance to these compounds. http://purl.obolibrary.org/obo/ARO_3007405 ANT(2'')-I http://purl.obolibrary.org/obo/ARO_3004276 ANT(2'') A family of aminoglycoside 2''-O-nucleotidyltransferase enzymes which inactivate gentamicin, tobramycin & dibekacin by catalyzing the transfer of an AMP group from an ATP substrate, thereby conferring resistance to these compounds. http://purl.obolibrary.org/obo/ARO_3007406 APH(3')-I http://purl.obolibrary.org/obo/ARO_3000126 APH(3') A family of aminoglycoside 3'-O-phosphotransferase enzymes which inactivate kamamycin, neomycin & lividomycin by catalyzing the ATP-dependent phosphorylation of these antibiotics, thereby conferring resistance to these compounds. http://purl.obolibrary.org/obo/ARO_3007407 ANT(3'')-I http://purl.obolibrary.org/obo/ARO_3004275 ANT(3'') A family of aminoglycoside O-nucleotidyltransferase enzymes which inactivate streptomycin and spectinomycin by catalyzing the transfer of an AMP group from an ATP substrate, thereby conferring resistance to these compounds. These enzymes modify the 3''-hydroxyl position of streptomycin and the 9-hydroxyl position of spectinomycin. http://purl.obolibrary.org/obo/ARO_3007408 APH(3')-II http://purl.obolibrary.org/obo/ARO_3000126 APH(3') A family of aminoglycoside 3'-O-phosphotransferase enzymes which inactivate kanamycin, neomycin, paromomycin and butirosin by catalyzing the ATP-dependent phosphorylation of these antibiotics, thereby conferring resistance to these compounds. http://purl.obolibrary.org/obo/ARO_3007409 APH(3')-III http://purl.obolibrary.org/obo/ARO_3000126 APH(3') A family of aminoglycoside 3'-O-phosphotransferase enzymes which inactivate kanamycin, neomycin, paromomycin, butirosin and lividomycin by catalyzing the ATP-dependent phosphorylation of these antibiotics, thereby conferring resistance to these compounds. http://purl.obolibrary.org/obo/ARO_3007410 APH(3')-IV http://purl.obolibrary.org/obo/ARO_3000126 APH(3') A family of aminoglycoside 3'-O-phosphotransferase enzymes which inactivate kanamycin, neomycin, paromomycin, ribostamycin and butirosin by catalyzing the ATP-dependent phosphorylation of these antibiotics, thereby conferring resistance to these compounds. http://purl.obolibrary.org/obo/ARO_3007411 APH(3')-V http://purl.obolibrary.org/obo/ARO_3000126 APH(3') A family of aminoglycoside 3'-O-phosphotransferase enzymes which inactivate neomycin, paromomycin and ribostamycin by catalyzing the ATP-dependent phosphorylation of these antibiotics, thereby conferring resistance to these compounds. http://purl.obolibrary.org/obo/ARO_3007412 APH(3')-VI http://purl.obolibrary.org/obo/ARO_3000126 APH(3') A family of aminoglycoside 3'-O-phosphotransferase enzymes which inactivate kanamycin, neomycin, paromomycin, ribostamycin and butirosin, as well as amikacin and isepomicin, by catalyzing the ATP-dependent phosphorylation of these antibiotics, thereby conferring resistance to these compounds. http://purl.obolibrary.org/obo/ARO_3007413 APH(3')-VII http://purl.obolibrary.org/obo/ARO_3000126 APH(3') A family of aminoglycoside 3'-O-phosphotransferase enzymes which inactivate kanamycin and neomycin by catalyzing the ATP-dependent phosphorylation of these antibiotics, thereby conferring resistance to these compounds. It is also possible to observe low-level sub-breakpoint amikacin resistance dependent on testing standards and breakpoint criteria. http://purl.obolibrary.org/obo/ARO_3007414 APH(3'')-I http://purl.obolibrary.org/obo/ARO_3000127 APH(3'') A family of aminoglycoside 3''-O-phosphotransferase enzymes which inactivate streptomycin by catalyzing the ATP-dependent phosphorylation of the 3''-hydroxyl group, thereby conferring resistance. http://purl.obolibrary.org/obo/ARO_3007415 APH(6)-I http://purl.obolibrary.org/obo/ARO_3000151 APH(6) A family of aminoglycoside 6-O-phosphotransferase enzymes which inactivate streptomycin by catalyzing the ATP-dependent phosphorylation of the 6-hydroxyl group, thereby conferring resistance. http://purl.obolibrary.org/obo/ARO_3007416 APH(9)-I http://purl.obolibrary.org/obo/ARO_3000153 APH(9) A family of aminoglycoside 9-O-phosphotransferase enzymes which inactivate spectinomycin by catalyzing the ATP-dependent phosphorylation of the 9-hydroxyl group, thereby conferring resistance. http://purl.obolibrary.org/obo/ARO_3007417 APH(7'')-I http://purl.obolibrary.org/obo/ARO_3000154 APH(7'') A family of aminoglycoside 7''-O-phosphotransferase enzymes which inactivate hygromycin by catalyzing the ATP-dependent phosphorylation of the 7''-hydroxyl group, thereby conferring resistance. http://purl.obolibrary.org/obo/ARO_3007418 APH(4)-I http://purl.obolibrary.org/obo/ARO_3000155 APH(4) A family of aminoglycoside 4-O-phosphotransferase enzymes which inactivate hygromycin by catalyzing the ATP-dependent phosphorylation of the 4-hydroxyl group, thereby conferring resistance. http://purl.obolibrary.org/obo/ARO_3007419 aminoglycoside bifunctional resistance protein http://purl.obolibrary.org/obo/ARO_3007380 aminoglycoside modifying enzyme Bifunctional aminoglycoside-inactivating enzymes composed of two separate functional domains. These proteins possess activity from both enzyme components, thereby conferring resistance to the combination of antibiotics from both domains, and may include acetylation, phosphorylation or nucleotidylation activity. http://purl.obolibrary.org/obo/ARO_3007420 Klebsiella pneumoniae lamB with mutations conferring resistance to ceftazidime-avibactam http://purl.obolibrary.org/obo/ARO_3004279 Sugar Porin (SP) LamB is a maltoporin that negatively regulates antibiotic resistance. Knockout strains of lamB are shown to exhibit higher levels of resistance than wild-type strains. Mutations in the lamB gene of Klebsiella are associated with resistance to ceftazidime-avibactam. http://purl.obolibrary.org/obo/ARO_3007421 Klebsiella pneumoniae PBP3 mutants conferring resistance to ceftazidime-avibactam http://purl.obolibrary.org/obo/ARO_3003938 Penicillin-binding protein mutations conferring resistance to beta-lactam antibiotics Mutant PBP3 in Klebsiella pneumoniae conferring resistance to ceftazidime-avibactam. http://purl.obolibrary.org/obo/ARO_3007422 ceftaroline-avibactam http://purl.obolibrary.org/obo/ARO_3000707 antibiotic mixture A combination of the beta-lactam antibiotic ceftaroline and the beta-lactamase inhibitor avibactam. http://purl.obolibrary.org/obo/ARO_3007423 Escherichia coli PBP3 mutants conferring resistance to beta-lactam antibiotics http://purl.obolibrary.org/obo/ARO_3003938 Penicillin-binding protein mutations conferring resistance to beta-lactam antibiotics Mutant PBP3 in E. coli conferring resistance to beta-lactams, including beta-lactam/beta-lactamase inhibitor combinations. http://purl.obolibrary.org/obo/ARO_3007424 resistance by host-dependent nutrient acquisition http://purl.obolibrary.org/obo/ARO_1000002 mechanism of antibiotic resistance Resistance via uptake of host nutrients to bypass antibiotic mechanism. http://purl.obolibrary.org/obo/ARO_3007425 protein(s) conferring resistance via host-dependent nutrient acquisition http://purl.obolibrary.org/obo/ARO_3000000 determinant of antibiotic resistance Proteins involved in the uptake of host-nutrients to bypass antibiotic resistance mechanisms. http://purl.obolibrary.org/obo/ARO_3007426 ECF transporter S component http://purl.obolibrary.org/obo/ARO_3007425 protein(s) conferring resistance via host-dependent nutrient acquisition ECF transporter S component genes involved in host nutrient uptake. http://purl.obolibrary.org/obo/ARO_3007427 ThfT http://purl.obolibrary.org/obo/ARO_3007426 ECF transporter S component ThfT is an ECF transporter S component that expands the substrate profile of endogenous ECF transporters to include folate biosynthesis end products. It confers resistance to the folate synthesis inhibitor sulfamethoxazole by allowing uptake of host folate. http://purl.obolibrary.org/obo/ARO_3007428 polymyxin resistance operon http://purl.obolibrary.org/obo/ARO_0000010 antibiotic resistance gene cluster, cassette, or operon Operon or gene clusters confering resistance to polymyxin antibiotics. http://purl.obolibrary.org/obo/ARO_3007429 gene(s) or protein(s) associated with polymyxin resistance operon http://purl.obolibrary.org/obo/ARO_3000000 determinant of antibiotic resistance Various genes and proteins involved in intrinsic polymyxin resistance operons. http://purl.obolibrary.org/obo/ARO_3007430 alm glycyl carrier protein http://purl.obolibrary.org/obo/ARO_3007429 gene(s) or protein(s) associated with polymyxin resistance operon Glycyl carrier proteins associated with polymixin resistance operons. http://purl.obolibrary.org/obo/ARO_3007431 almF http://purl.obolibrary.org/obo/ARO_3007430 alm glycyl carrier protein almF is a glycine carrier protein associated with the almEFG operon in Vibrio cholerae. It is activated by almE and carries the glycyl molecule later added to lipid A by almG. http://purl.obolibrary.org/obo/ARO_3007432 alm glycyltransferase http://purl.obolibrary.org/obo/ARO_3007429 gene(s) or protein(s) associated with polymyxin resistance operon Glycyl transferase associated with polymyxin resistance operons not interacting with lipid A. http://purl.obolibrary.org/obo/ARO_3007433 almE http://purl.obolibrary.org/obo/ARO_3007432 alm glycyltransferase almE is a glycyltransferase found in Vibrio cholerae that transfers glycine to the carrier protein almF. almE is part of the almEFG polymyxin resistance operon. http://purl.obolibrary.org/obo/ARO_3007434 almEFG http://purl.obolibrary.org/obo/ARO_3007428 polymyxin resistance operon The almEFG operon is responsible for glycylation of lipid A as a mechanism of colistin resistance in Vibrio cholerae. Its mechanism involves transfer of a glycyl molecule to the carrier protein almF by almE followed by glycylation of lipid A by almG. http://purl.obolibrary.org/obo/NCIT_23014 gram stain http://purl.obolibrary.org/obo/ARO_3004389 reagent or protocol used for testing AMR Gram staining is a method for staining and identifying bacteria. It is based on the differential retention of a crystal violet-iodine complex within the cell membrane. The cell wall of gram-positive cells have a thick peptidoglycan layer that retains crystal violet after an alcohol wash (staining black-blue or purple by a counterstain). The cell wall of gram-negative cells have a thinner peptidoglycan layer that does not retain crystal violet after an alcohol wash (staining red after counterstain). Some cells have variable staining in culture (e.g. Bacillus, Clostridium) while others have indeterminate staining due to unique aspects of their cell membrane or wall (e.g. Mycobacterium, Mycoplasma). http://purl.obolibrary.org/obo/ARO_2000008 targeted_by_antibiotic A relationship ontology term in which the subject is targeted by a specific antibiotic. http://purl.obolibrary.org/obo/ARO_2000004 periplasmic_adaptor_protein_of A bridging component of tripartite efflux systems in Gram-negative bacteria, located in the periplasmic space. The periplasmiic adaptor protein links the inner membrane transporter and the outer membrane protein, stabilizing the efflux complex and facilitating substrate transport. http://purl.obolibrary.org/obo/ARO_3009166 fluxapyroxad http://purl.obolibrary.org/obo/ARO_3009165 antifungal without defined classification This compound is used to control a number of cereal fungal pathogens including those belonging to the Ascomycetes, Basidiomycetes and Zygomycetes families. http://purl.obolibrary.org/obo/ARO_3009177 cerulenin http://purl.obolibrary.org/obo/ARO_3009165 antifungal without defined classification Cerulenin has a role as an antifungal agent, an antiinfective agent, an antilipemic drug, an antimetabolite, a fatty acid synthesis inhibitor and an antimicrobial agent. It functions by inhibiting the biosynthesis of several lipids and sterols by interfering with enzyme function. In fatty acid synthesis, it is reported to bind in equimolar ratio to b-keto-acyl-ACP synthase. In sterol synthesis, it inhibits HMG-CoA synthetase activity. It is a monocarboxylic acid amide and an epoxide and is found naturally in several species including Cephalosporium caerulensfungus, Euglena gracilis, Acremonium, Acrocylindrum and Helicoceras. It is also shown to inhibit feeding and induce dramatic weight loss in mice. http://purl.obolibrary.org/obo/ARO_3004451 Agrobacterium fabrum chloramphenicol acetyltransferase http://purl.obolibrary.org/obo/ARO_3000122 chloramphenicol acetyltransferase (CAT) A chloramphenicol resistance determinant described in the Gram-negative bacterium Agrobacterium fabrum. http://purl.obolibrary.org/obo/ARO_3004452 Alkalihalobacillus clausii chloramphenicol acetyltransferase http://purl.obolibrary.org/obo/ARO_3000122 chloramphenicol acetyltransferase (CAT) A chloramphenicol resistance determinant described in Alkalihalobacillus clausii. http://purl.obolibrary.org/obo/ARO_3004454 Campylobacter coli chloramphenicol acetyltransferase http://purl.obolibrary.org/obo/ARO_3000122 chloramphenicol acetyltransferase (CAT) A chloramphenicol resistance determinant described in Campylobacter coli. http://purl.obolibrary.org/obo/ARO_3004455 Streptococcus suis chloramphenicol acetyltransferase http://purl.obolibrary.org/obo/ARO_3000122 chloramphenicol acetyltransferase (CAT) A chloramphenicol resistance determinant described in Streptococcus suis. http://purl.obolibrary.org/obo/ARO_3004456 Enterococcus faecium chloramphenicol acetyltransferase http://purl.obolibrary.org/obo/ARO_3000122 chloramphenicol acetyltransferase (CAT) A chloramphenicol resistance determinant described in an Enterococcus faecium plasmid. http://purl.obolibrary.org/obo/ARO_3004457 Staphylococcus intermedius chloramphenicol acetyltransferase http://purl.obolibrary.org/obo/ARO_3000122 chloramphenicol acetyltransferase (CAT) A chloramphenicol resistance determinant described in Staphylococcus intermedius. http://purl.obolibrary.org/obo/ARO_3004458 Enterococcus faecalis chloramphenicol acetyltransferase http://purl.obolibrary.org/obo/ARO_3000122 chloramphenicol acetyltransferase (CAT) A chloramphenicol acetyltransferase and resistance determinant described in Enterococcus faecalis. http://purl.obolibrary.org/obo/ARO_3004460 Vibrio anguillarum chloramphenicol acetyltransferase http://purl.obolibrary.org/obo/ARO_3000122 chloramphenicol acetyltransferase (CAT) A chloramphenicol resistance determinant described in a Vibrio anguillarum plasmid sequence. http://purl.obolibrary.org/obo/ARO_3004462 delafloxacin http://purl.obolibrary.org/obo/ARO_0000001 fluoroquinolone antibiotic Delafloxacin is a novel fluoroquinolone antibiotic, differentiated from other on-market fluoroquinolones by the absence of a protonatable substituent conferring a weakly acidic character to the molecule. This property results in increased intracellular penetration and enhanced bactericidal activity under acidic conditions. http://purl.obolibrary.org/obo/ARO_3004463 EBR-2 http://purl.obolibrary.org/obo/ARO_3004204 EBR beta-lactamase EBR-2 is a novel EBR-like class B beta-lactamase isolated from an extensively drug-resistant strain of Empedobacter falsenii. http://purl.obolibrary.org/obo/ARO_3004464 CFE-2 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CFE-2 is a plasmid-encoded AmpC beta-lactamase first described from Citrobacter freundii by Chen et al. 2018. http://purl.obolibrary.org/obo/ARO_3004465 intrinsic colistin resistant phosphoethanolamine transferase http://purl.obolibrary.org/obo/ARO_3004112 phosphoethanolamine transferase conferring colistin resistance Chromosomally-encoded phosphoethanolamine (PEtN) transferases shown to confer resistance to polymyxin antibiotics, including colistin. http://purl.obolibrary.org/obo/ARO_3004466 ICR-Mc http://purl.obolibrary.org/obo/ARO_3004465 intrinsic colistin resistant phosphoethanolamine transferase A chromosomally-encoded colistin resistance phosphoethanolamine (PEtN) transferase of Moraxella catarrhalis. ICR-Mc is the protein that represents the closest known ortholog to the colistin resistance MCR-1 and MCR-2 PEtN transferases. http://purl.obolibrary.org/obo/ARO_3004467 ciprofloxacin phosphotransferase http://purl.obolibrary.org/obo/ARO_3000557 antibiotic inactivation enzyme A class of phosphotransferase enzymes shown to confer resistance to ciprofloxacin by antibiotic inactivation through phosphorylation. The sole example, CrpP, was thought to confer resistance to ciprofloxacin by antibiotic inactivation through phosphorylation, however in the paper by Zubyk & Wright (2021) this was discovered to not be the case. There are no known experimentally validated examples of enzymes with this function. http://purl.obolibrary.org/obo/ARO_3004469 ABC-F ATP-binding cassette ribosomal protection protein http://purl.obolibrary.org/obo/ARO_3000185 antibiotic target protection protein A subfamily of the ATP-binding cassette protein superfamily. Unlike other ABC proteins, ABC-F genes are not fused to a transmembrane domain nor associated with transport. It has been shown that ABC-F proteins confer antibiotic resistance via ribosomal protection and not antibiotic efflux as in other ABC proteins. http://purl.obolibrary.org/obo/ARO_3004470 poxtA http://purl.obolibrary.org/obo/ARO_3007068 Miscellaneous ABC-F subfamily ATP-binding cassette ribosomal protection proteins PoxtA is an ABC-F subfamily ATP-binding cassette protein that confers resistance to tetracycline, -phenicol, and oxazolidinone via modification of the bacterial ribosome. The encoding gene was isolated from a methicillin-resistant Staphylococcus aureus strain. http://purl.obolibrary.org/obo/ARO_3004471 msr-type ABC-F protein http://purl.obolibrary.org/obo/ARO_3004469 ABC-F ATP-binding cassette ribosomal protection protein msr-type ABC-F subfamily ribosomal protection proteins expression in Staphylococci species and confer resistance to erythromycin and streptogramin B antibiotics through antibiotic target protection mechanisms. http://purl.obolibrary.org/obo/ARO_3004472 lsa-type ABC-F protein http://purl.obolibrary.org/obo/ARO_3004469 ABC-F ATP-binding cassette ribosomal protection protein A subgroup of the ABC-F protein subfamily of ATP-binding cassette proteins. lsa-type ABC-F proteins confer resistance to streptogramin, lincosamide and pleuromutilin antibiotics through antibiotic target protection of the ribosome. http://purl.obolibrary.org/obo/ARO_3004473 tebipenem http://purl.obolibrary.org/obo/ARO_0000020 carbapenem A carbapenem antibiotic, administered as the oral drug tebipenem-pivoxil, shown to be effective at treating bacterial infections. http://purl.obolibrary.org/obo/ARO_3004474 cefiderocol http://purl.obolibrary.org/obo/ARO_3009109 other cephalosporins and penems A siderophore cephalosporin with antibiotic activity against Gram-negative pathogens including and specifically Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005007 QnrVC2 http://purl.obolibrary.org/obo/ARO_3000419 quinolone resistance protein (qnr) QnrVC2 is a class 1 integron found in Ciprofloxacin-resistant Vibro choleraeO1. http://purl.obolibrary.org/obo/ARO_3005008 TxR http://purl.obolibrary.org/obo/ARO_3000750 protein of two-component regulatory system modulating antibiotic efflux TxR is a putative transcription regulator that plays a role in conferring tetracycline resistance. It is required for proper functioning of Tet35. http://purl.obolibrary.org/obo/ARO_3005009 qacE http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump QacE is a resistance gene conferring resistance to antiseptics. http://purl.obolibrary.org/obo/ARO_3005010 qacEdelta1 http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump QacEdelta1 is a resistance gene conferring resistance to antiseptics. It is different from QacE only at the 3'-terminus. http://purl.obolibrary.org/obo/ARO_3005011 IDC beta-lactamase http://purl.obolibrary.org/obo/ARO_3000076 class C beta-lactamase IDC beta-lactamases are class C beta-lactamases inc. cephalosporinases and carbapenemases. http://purl.obolibrary.org/obo/ARO_3005012 IDC-1 http://purl.obolibrary.org/obo/ARO_3005011 IDC beta-lactamase IDC-2 is an IDC beta-lactamase and an integron cephalosprinase. http://purl.obolibrary.org/obo/ARO_3005013 IDC-2 http://purl.obolibrary.org/obo/ARO_3005011 IDC beta-lactamase IDC-2 is an IDC beta-lactamase and an integron cephalosprinase. http://purl.obolibrary.org/obo/ARO_3005014 VMB beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase Vibro metallo-B-lactamase, also known as VMB is a carbapenemase beta-lactamase gene family. http://purl.obolibrary.org/obo/ARO_3005015 VMB-1 http://purl.obolibrary.org/obo/ARO_3005014 VMB beta-lactamase Vibrio metallo-B-lactamase 1, also known as VMB-1, is carbapenemase beta-lactamase that is found in plasmid pVB1796 from Vibrio alginolyticus. http://purl.obolibrary.org/obo/ARO_3005016 CMY-150 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-150 is a CMY-2 variant differing by 15 amino-acid substitutions. It confers higher resistance levels to ceftazidime and aztreonam compared to CMY-2. http://purl.obolibrary.org/obo/ARO_3005017 LMB beta-lactamase http://purl.obolibrary.org/obo/ARO_3000571 subclass B3 (metallo-) beta-lactamase LMB is an AMR Gene family belonging to subclass B3 metallo-beta-lactamases. http://purl.obolibrary.org/obo/ARO_3005018 LMB-1 http://purl.obolibrary.org/obo/ARO_3005017 LMB beta-lactamase LMB-1 is a subclass B3 metallo-beta-lactamase that confers resistance to penams, cephalosporins, and carbapenems. http://purl.obolibrary.org/obo/ARO_3005019 IMP-68 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-68 is a subclass B1 metallo-beta-lactamase that confers resistance to carbapenems. http://purl.obolibrary.org/obo/ARO_3005020 cfr(D) Group http://purl.obolibrary.org/obo/ARO_3000202 Cfr 23S ribosomal RNA methyltransferase The cfr(D) group are cfr(D) genes found in Enterococcus faecium that confer resistance to vancomycin, teicoplanin and linezolid. http://purl.obolibrary.org/obo/ARO_3005021 cfr(D) http://purl.obolibrary.org/obo/ARO_3005020 cfr(D) Group cfr(D) is found in Enterococcus faecium. It confers resistance to vancomycin, teicoplanin, and linezolid. http://purl.obolibrary.org/obo/ARO_3005022 cfr(E) Group http://purl.obolibrary.org/obo/ARO_3000202 Cfr 23S ribosomal RNA methyltransferase cfr(E) is a cfr-like gene described by (Stojkovic et al, 2019). It is found on transposon Tn6218 and found in Clostridioides difficile. http://purl.obolibrary.org/obo/ARO_3005023 cfrE http://purl.obolibrary.org/obo/ARO_3005022 cfr(E) Group The gene cfr(E) is a cfr-like gene found in Clostridioides difficile isolate DF11. It confers resistance to antibiotics targeting to the 23s rRNA through hypermethylation of nucleotide A2503. http://purl.obolibrary.org/obo/ARO_3005024 FosL1 http://purl.obolibrary.org/obo/ARO_3000133 fosfomycin thiol transferase FosL1 is related to FosA-like genes. It is a plasmid-encoded fosfomycin resistant gene found in E. coli. http://purl.obolibrary.org/obo/ARO_3005025 ATP synthase inhibitor http://purl.obolibrary.org/obo/ARO_3007223 adjuvants enhancing antibiotic entry Antibiotic adjuvants shown to inhibit the action of ATP synthase, restoring antibiotic activity by depolarizing the bacterial membrane. http://purl.obolibrary.org/obo/ARO_3005026 venturicidin A http://purl.obolibrary.org/obo/ARO_3005025 ATP synthase inhibitor Venturicidin A is an ATP synthase inhibitor and antibiotic adjuvant produced in actinomycetes. In the presence of aminoglycoside antibiotics such as gentamicin, Venturicidin A showed to restore susceptibility to aminoglycosides in resistant bacteria. http://purl.obolibrary.org/obo/ARO_3005027 FRI-4 http://purl.obolibrary.org/obo/ARO_3004796 FRI beta-lactamase FRI-4 is a carbapenem-hydrolyzing Class A beta-lactamase gene found in Enterobacter asburiae. http://purl.obolibrary.org/obo/ARO_3005028 FRI-5 http://purl.obolibrary.org/obo/ARO_3004796 FRI beta-lactamase FRI-5 is a carbapenem-hydrolyzing Class A beta-lactamase gene found in Enterobacter cloacae. http://purl.obolibrary.org/obo/ARO_3005029 FRI-6 http://purl.obolibrary.org/obo/ARO_3004796 FRI beta-lactamase FRI-6 is a carbapenem-hydrolyzing Class A beta-lactamase gene found in Enterobacter cloacae. http://purl.obolibrary.org/obo/ARO_3005030 FRI-7 http://purl.obolibrary.org/obo/ARO_3004796 FRI beta-lactamase FRI-7 is a carbapenem-hydrolyzing Class A beta-lactamase gene found in Enterobacter asburiae. http://purl.obolibrary.org/obo/ARO_3005031 FRI-8 http://purl.obolibrary.org/obo/ARO_3004796 FRI beta-lactamase FRI-8 is a carbapenem-hydrolyzing Class A beta-lactamase gene found in Enterobacter sp. 18A13. It is from a plasmid. http://purl.obolibrary.org/obo/ARO_3005032 FRI-9 http://purl.obolibrary.org/obo/ARO_3004796 FRI beta-lactamase FRI-9 is a carbapenem-hydrolyzing Class A beta-lactamase gene found in Enterobacter asburiae. http://purl.obolibrary.org/obo/ARO_3005033 FLC-1 http://purl.obolibrary.org/obo/ARO_3004796 FRI beta-lactamase FLC-1 is part of the FRI beta-lactamase family. It is a class A carbapenem-hydrolyzing beta-lactamase from Enterobacter cloacae. http://purl.obolibrary.org/obo/ARO_3005034 YRC beta-lactamase http://purl.obolibrary.org/obo/ARO_3000076 class C beta-lactamase YRC is a ambler class C beta-lactamase from Yersinia ruckeri. It confers resistance penams and cephalosporins. http://purl.obolibrary.org/obo/ARO_3005035 YRC-1 http://purl.obolibrary.org/obo/ARO_3005034 YRC beta-lactamase YRC-1 is a ampC-like beta-lactamase that confers resistance to penams and cephalosporins. It is an ambler class C beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005036 BLMT http://purl.obolibrary.org/obo/ARO_3004256 Bleomycin resistant protein BLMT is a bleomycin (Bm) resistance protein, encoded by the ble gene on the transposon Tn5. This protein confers a survival advantage to Escherichia coli host cells. BLMT confers resistance to bleomycin. http://purl.obolibrary.org/obo/ARO_3005037 ADC-159 http://purl.obolibrary.org/obo/ARO_3003846 ADC beta-lactamase without carbapenemase activity ADC-159 is an ADC beta-lactamase and a ambler class C beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005038 PDC-65 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-65 is an ambler class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005039 PDC-55 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-55 is an ambler class C beta-lactamase from Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005040 YajC http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance YajC interacts with the AcrAB-TolC efflux pump in a way that in uncharacterized but is shown to grant increased fitness in the presence of linezolid, rifampicin, and vancomycin. http://purl.obolibrary.org/obo/ARO_3005041 mlaF http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance mlaF from the mla system is a gene proposed to play a part in the transport of phospholipids to the outer membrane. Insertions in mlaF are shown to confer resistance to linezolid. http://purl.obolibrary.org/obo/ARO_3005042 mlaD http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance mlaD from the mla system is a gene proposed to play a part in the transport of phospholipids to the outer membrane. Insertions in mlaD are shown to confer resistance to linezolid. http://purl.obolibrary.org/obo/ARO_3005043 cmlA9 http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump cmlA9 is a Major Facilitator Superfamily efflux gene that is found in Salmonella enterica. http://purl.obolibrary.org/obo/ARO_3005044 OmpA http://purl.obolibrary.org/obo/ARO_3004282 General Bacterial Porin with reduced permeability to peptide antibiotics OmpA is a porin that confers resistance to beta-lactam antibiotics. http://purl.obolibrary.org/obo/ARO_3005045 SatA http://purl.obolibrary.org/obo/ARO_3000869 streptothricin acetyltransferase (SAT) SatA is part of the Streptothricin acetyltransferase gene family. It confers resistance to nucleoside antibiotics. http://purl.obolibrary.org/obo/ARO_3005046 MecC-type methicillin resistance repressor MecI http://purl.obolibrary.org/obo/ARO_3001208 methicillin resistant PBP2 This MecI is a methicillin-resistant repressor resembling MecC. It confers resistance to penams. http://purl.obolibrary.org/obo/ARO_3005047 eptB http://purl.obolibrary.org/obo/ARO_3004269 pmr phosphoethanolamine transferase eptB is a phosphoethanolamine transferase. It confers resistance to peptide antibiotics. http://purl.obolibrary.org/obo/ARO_3005049 CrcB http://purl.obolibrary.org/obo/ARO_3000112 multidrug and toxic compound extrusion (MATE) transporter CrcB is part of the Camphor Resistance Protein Family. It confers resistance to aminoglycoside antibiotics. http://purl.obolibrary.org/obo/ARO_3005050 Intrinsic peptide antibiotic resistant Lps http://purl.obolibrary.org/obo/ARO_3000270 protein modulating permeability to antibiotic LpsB is involved in lipopolysaccharide synthesis. It provides intrinsic resistance to colistin and other peptide antibiotics such as polymyxins. http://purl.obolibrary.org/obo/ARO_3005051 LpsB http://purl.obolibrary.org/obo/ARO_3005050 Intrinsic peptide antibiotic resistant Lps LpsB is involved in lipopolysaccharide synthesis. It confers intrinsic resistance to colistin and other peptide antibiotics. http://purl.obolibrary.org/obo/ARO_3005052 LpsA http://purl.obolibrary.org/obo/ARO_3005050 Intrinsic peptide antibiotic resistant Lps LpsA plays a role in Lipooligosaccharide biosynthesis. LpsA confers resistance to polymyxin antibiotics. http://purl.obolibrary.org/obo/ARO_3005053 ArnT http://purl.obolibrary.org/obo/ARO_3004269 pmr phosphoethanolamine transferase ArnT is involved in Cell Wall Biosynthesis, specifically 4-amino-4-deoxy-L-arabinose (Ara4N). It confers resistance to peptide antibiotics. http://purl.obolibrary.org/obo/ARO_3005056 tet(X6) http://purl.obolibrary.org/obo/ARO_3000036 tetracycline inactivation enzyme Tet(X6) is a tetracycline inactivating enzyme. It is a tet(X) variant. http://purl.obolibrary.org/obo/ARO_3005057 tet(X5) http://purl.obolibrary.org/obo/ARO_3000036 tetracycline inactivation enzyme Tet(X5) is a tetracycline inactivating enzyme. It is a variant of tet(X). http://purl.obolibrary.org/obo/ARO_3005058 mlaFEDB http://purl.obolibrary.org/obo/ARO_0010001 ATP-binding cassette (ABC) antibiotic efflux pump ABC transporter complex which is involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. http://purl.obolibrary.org/obo/ARO_3005059 LptD http://purl.obolibrary.org/obo/ARO_0010001 ATP-binding cassette (ABC) antibiotic efflux pump LptD is involved in LPS transport in a ABC Transporter efflux system. It confers resistance to rifamycin, aminocoumarin, and peptide antibiotics. http://purl.obolibrary.org/obo/ARO_3005060 OXA-837 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase A class D OXA-like beta-lactamase described in the emerging pathogen Cupriavidus gilardii. http://purl.obolibrary.org/obo/ARO_3005061 AAC(3)-IVb http://purl.obolibrary.org/obo/ARO_3007387 AAC(3)-IV A novel aminoglycoside resistance gene identified from Cupriavidus gilardii; AAC(3)-IVb / aacC10 is an aminoglycoside-3-N-acetyltransferase gene which confers resistance to gentamicin and tobramycin. http://purl.obolibrary.org/obo/ARO_3005062 ANT(3'')-Ib http://purl.obolibrary.org/obo/ARO_3007407 ANT(3'')-I A novel aminoglycoside 3''-adenyltransferase gene and aminoglycoside resistance gene identified from Cupriavidus gilardii. ANT(3'')-Ib / aadA32 confers resistance to spectinomycin and streptomycin. http://purl.obolibrary.org/obo/ARO_3005063 cprR http://purl.obolibrary.org/obo/ARO_3000750 protein of two-component regulatory system modulating antibiotic efflux cprR is one part of a two-component regulatory system. It with its counterpart cprS induce the Arn operon to confer resistance to peptide antibiotics. http://purl.obolibrary.org/obo/ARO_3005064 cprS http://purl.obolibrary.org/obo/ARO_3000750 protein of two-component regulatory system modulating antibiotic efflux cprS is part of a two-component regulatory system that, with its counterpart cprR, induces the Arn operon in the presence of cationic peptides to confer resistance. http://purl.obolibrary.org/obo/ARO_3005065 cprRS http://purl.obolibrary.org/obo/ARO_3004269 pmr phosphoethanolamine transferase cprRS is a two-component regulatory system. In the presence of cationic peptides, it induces the Arn operon to confer resistance. http://purl.obolibrary.org/obo/ARO_3005066 parRS http://purl.obolibrary.org/obo/ARO_3000750 protein of two-component regulatory system modulating antibiotic efflux parRS is a two-component sensor that mediates MexXY/OprM and porin OprD to confer resistance to polycationic antibiotics. It has multiple mechanisms of resistance such as LPS modification, efflux mediation and reduced porin pathway. http://purl.obolibrary.org/obo/ARO_3005067 ParS http://purl.obolibrary.org/obo/ARO_3000750 protein of two-component regulatory system modulating antibiotic efflux ParS is the sensor component of the two-component ParRS system. Alongside its counterpart ParR, it confers resistance to polycationic antibiotics though regulation of efflux pumps and porins. http://purl.obolibrary.org/obo/ARO_3005068 ParR http://purl.obolibrary.org/obo/ARO_3000750 protein of two-component regulatory system modulating antibiotic efflux ParR is a component of the two-component sensor ParRS. Alongside its counterpart ParS, it confers resistance to polycationic antibiotics through the regulation of efflux components and porins. http://purl.obolibrary.org/obo/ARO_3005069 rsmA http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux rsmA is a gene that regulates virulence of Pseudomonas aeruginosa. However, its negative effect on MexEF-OprN overexpression has been noted to confer resistance to various antibiotics. It's Escherichia coli homolog is csrA. http://purl.obolibrary.org/obo/ARO_3005070 complestatin http://purl.obolibrary.org/obo/ARO_3000081 glycopeptide antibiotic A glycopeptide antibiotic which binds to essential peptidoglycan hydrolases, thereby preventing autolysis and inhibited cell wall remodelling during growth. http://purl.obolibrary.org/obo/ARO_3005071 corbomycin http://purl.obolibrary.org/obo/ARO_3000081 glycopeptide antibiotic A glycopeptide antibiotic which binds to essential peptidoglycan hydrolases, thereby preventing autolysis and cell wall remodelling. http://purl.obolibrary.org/obo/ARO_3005072 ROB-13 http://purl.obolibrary.org/obo/ARO_3002994 ROB beta-lactamase ROB-13 is a beta-lactamase from the blaROB AMR gene family. It was found in Bibersteinia trehalosi. http://purl.obolibrary.org/obo/ARO_3005073 ROB-3 http://purl.obolibrary.org/obo/ARO_3002994 ROB beta-lactamase ROB-3 is a beta-lactamase from the blaROB AMR gene family. It was found in Moraxella pluranimalium. http://purl.obolibrary.org/obo/ARO_3005074 ROB-4 http://purl.obolibrary.org/obo/ARO_3002994 ROB beta-lactamase ROB-4 is a beta-lactamase from the blaROB AMR gene family. It was found in Moraxella porci. http://purl.obolibrary.org/obo/ARO_3005075 ROB-5 http://purl.obolibrary.org/obo/ARO_3002994 ROB beta-lactamase ROB-5 is a class A beta-lactamase from the blaROB AMR gene family. It was found in Moraxella sp. RCAD0137. http://purl.obolibrary.org/obo/ARO_3005076 ROB-6 http://purl.obolibrary.org/obo/ARO_3002994 ROB beta-lactamase ROB-6 is a class A beta-lactamase from the blaROB AMR gene family. It was first described by Clemente et al. http://purl.obolibrary.org/obo/ARO_3005077 ROB-7 http://purl.obolibrary.org/obo/ARO_3002994 ROB beta-lactamase ROB-7 is a class A beta-lactamase from the blaROB AMR gene family. It was first described by Clemente et al. http://purl.obolibrary.org/obo/ARO_3005078 ROB-8 http://purl.obolibrary.org/obo/ARO_3002994 ROB beta-lactamase ROB-8 is a class A beta-lactamase from the blaROB AMR gene family. It was first described by Clemente et al. http://purl.obolibrary.org/obo/ARO_3005079 ROB-2 http://purl.obolibrary.org/obo/ARO_3002994 ROB beta-lactamase ROB-2 is an extended spectrum class A beta-lactamase from the blaROB AMR gene family It is described by Kadlec et al. http://purl.obolibrary.org/obo/ARO_3005080 ROB-10 http://purl.obolibrary.org/obo/ARO_3002994 ROB beta-lactamase ROB-10 is a class A beta-lactamase from the blaROB AMR gene family. It was found in Glaesserella parasuis. http://purl.obolibrary.org/obo/ARO_3005081 Thermus thermophilus uL3 mutations conferring resistance to pleuromutilin antibiotics http://purl.obolibrary.org/obo/ARO_3005082 Ribosomal protein mutation conferring resistance to pleuromutilin antibiotics Thermus thermophilus ribosomal protein uL3 containing various mutations conferring resistance to tiamulin. Mutations in the ribosomal protein of uL3 acts by interfering with local rRNA conformation thus conferring resistance. http://purl.obolibrary.org/obo/ARO_3005082 Ribosomal protein mutation conferring resistance to pleuromutilin antibiotics http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Ribosomal protein mutations that interfere with the rRNA conformation at the active site thus conferring antibiotic resistance. http://purl.obolibrary.org/obo/ARO_3005083 Thermus thermophilus 23s rRNA conferring resistance to pleuromutilin antibiotics http://purl.obolibrary.org/obo/ARO_3004178 23S rRNA with mutation conferring resistance to pleuromutilin antibiotics Mutations in the 23s rRNA of Thermus thermophilus confers resistance to pleuromutilin antibiotics such as tiamulin. http://purl.obolibrary.org/obo/ARO_3005084 dfrA31 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr dfrA31 is an antibiotic resistance dihydrofolate reductase from an integron found from Vibrio cholerae. http://purl.obolibrary.org/obo/ARO_3005085 AAC(3)-IIg http://purl.obolibrary.org/obo/ARO_3007385 AAC(3)-II AAC(3)-IIg is part of the AAC(3) family. It was initially found in clinical isolates of Enterobacter cloacae. http://purl.obolibrary.org/obo/ARO_3005086 Target protecting FusB-type protein conferring resistance to Fusidic acid http://purl.obolibrary.org/obo/ARO_3000185 antibiotic target protection protein Fusidic acid resistance determinants through the mediation of target protection. These protein drive the dissociation of EF-G from the ribosome thus counteracting the action of Fusidic acid. http://purl.obolibrary.org/obo/ARO_3005087 msrF http://purl.obolibrary.org/obo/ARO_3004471 msr-type ABC-F protein msrF is an ABC-F binding cassette ribosomal protection protein. It confers resistance to macrolide antibiotics. http://purl.obolibrary.org/obo/ARO_3005088 msrH http://purl.obolibrary.org/obo/ARO_3004471 msr-type ABC-F protein msrH is a ABC-F binding cassette ribosomal protection protein. It confers resistance to macrolide antibiotics. http://purl.obolibrary.org/obo/ARO_3005089 mef(D) http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump mef(D) is a major facilitator superfamily efflux pump protein. It works together with the msr proteins to confer resistance to macrolide antibiotics. http://purl.obolibrary.org/obo/ARO_3005090 RanB http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance RanB is the determinant of antibiotic resistance within the RanARanB ABC-type efflux system. It confers resistance to aminoglycoside antibiotics. http://purl.obolibrary.org/obo/ARO_3005091 RanA http://purl.obolibrary.org/obo/ARO_3000748 subunit of efflux pump conferring antibiotic resistance RanA is a part of the RanARanB ABC-type efflux system. Alongside RanB, it confers resistance to aminoglycoside antibiotics. http://purl.obolibrary.org/obo/ARO_3005092 RanARanB http://purl.obolibrary.org/obo/ARO_0010001 ATP-binding cassette (ABC) antibiotic efflux pump RanARanB is the combination of both RanA and RanB to form an ABC-type efflux system. RanB confers resistance to aminoglycoside antibiotics. http://purl.obolibrary.org/obo/ARO_3005093 OXA-899 http://purl.obolibrary.org/obo/ARO_3007708 OXA-22-like beta-lactamase OXA-899 is a class D beta-lactamase and part of the OXA family. It confers resistance to B-lactams and was originally found in Ralstonia pikettii. http://purl.obolibrary.org/obo/ARO_3005094 OXA-898 http://purl.obolibrary.org/obo/ARO_3007729 OXA-60-like beta-lactamase OXA-898 is a class D beta-lactamase from the OXA family. It confers resistance to B-lactams and was originally found in Ralstonia pikettii. http://purl.obolibrary.org/obo/ARO_3005095 GPC beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase GPC is a class A beta-lactamase family. It is found initially in Pseudomonas aeruginosa. It confers resistance to B-lactams. http://purl.obolibrary.org/obo/ARO_3005096 GPC-1 http://purl.obolibrary.org/obo/ARO_3005095 GPC beta-lactamase GPC-1 is a class A beta-lactamase. It is part of the GPC beta-lactamase gene family. Originally found in Pseudomonas aeruginosa. Confers resistance to B-lactams. http://purl.obolibrary.org/obo/ARO_3007196 KPC-123 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-123 is a KPC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007197 enramycin http://purl.obolibrary.org/obo/ARO_3000053 peptide antibiotic Enramycin is a polypeptide antibiotic commonly used as a feed additive for livestock. It is produced by species of the Streptomyces genus and is used to prevent necrotic enteritis in poultry and pigs. Enramycin disrupts cell wall synthesis by inhibiting MurG. http://purl.obolibrary.org/obo/ARO_3007198 PAM beta-lactamase http://purl.obolibrary.org/obo/ARO_3000571 subclass B3 (metallo-) beta-lactamase A family of subclass B3 metallo-beta-lactamases discovered in Pseudomonas alcaligenes and found in other members of the Pseudomonas genus. PAM beta-lactamases hydrolyze cephalosporins and carbenems. http://purl.obolibrary.org/obo/ARO_3007199 PAM-1 http://purl.obolibrary.org/obo/ARO_3007198 PAM beta-lactamase PAM-1 is a member of the PAM family of subclass B3 metallo-beta-lactamases found in members of the Psuedomonas genus. http://purl.obolibrary.org/obo/ARO_3007200 PAM-2 http://purl.obolibrary.org/obo/ARO_3007198 PAM beta-lactamase PAM-2 is a member of the PAM family of subclass B3 metallo-beta-lactamases found in members of the Pseudomonas genus. http://purl.obolibrary.org/obo/ARO_3007201 PAM-3 http://purl.obolibrary.org/obo/ARO_3007198 PAM beta-lactamase PAM-3 is a member of the PAM family of subclass B3 metallo-beta-lactamases found in members of the Pseudomonas genus. http://purl.obolibrary.org/obo/ARO_3007202 NDM-16b http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase New Delhi class B metallo-beta-lactamase 16b variant. http://purl.obolibrary.org/obo/ARO_3007203 Klebsiella pneumoniae mutant PhoQ conferring resistance to colistin http://purl.obolibrary.org/obo/ARO_3000835 phoQ Mutations in Klebsiella pneumoniae PhoQ of the two-component PhoPQ regulatory system conferring resistance to colistin. http://purl.obolibrary.org/obo/ARO_3007204 AAC(6')-Iap http://purl.obolibrary.org/obo/ARO_3007395 AAC(6')-I AAC(6')-Iap is an aminoglycoside acetyltransferase that confers resistance to a number of aminoglycoside antibiotics. http://purl.obolibrary.org/obo/ARO_3007205 KBL beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase Kathmandu beta-lactamases are a group of class A beta-lactamases that hydrolyze penicillin antibiotics. http://purl.obolibrary.org/obo/ARO_3007206 KBL-1 http://purl.obolibrary.org/obo/ARO_3007205 KBL beta-lactamase KBL-1 is a KBL class A beta-lactamase that confers resistance to a number of penicillin antibiotics. http://purl.obolibrary.org/obo/ARO_3007207 helicase-like RNA polymerase protection protein http://purl.obolibrary.org/obo/ARO_3000507 rifampin-resistant RNA polymerase-binding protein Helicase-like proteins that confer resistance to antibiotics such as rifamycins by preventing or disrupting their binding to RNA polymerase. http://purl.obolibrary.org/obo/ARO_3007208 HelR http://purl.obolibrary.org/obo/ARO_3007207 helicase-like RNA polymerase protection protein HelR is a helicase-like protein that confers resistance to rifamycins by displacing them from the RNA polymerase complex. The protein forces the antibiotic away from the polymerase by binding in its place. It then ejects itself from the complex, allowing the polymerase to resume normal function. http://purl.obolibrary.org/obo/ARO_3007209 Streptomyces venezuelae rox http://purl.obolibrary.org/obo/ARO_3000445 rifampin monooxygenase Streptomyces venezuelae rox is a class A flavoprotein monooxygenase that confers resistance to rifamycin antibiotics. It acts by oxygenating the naphthyl group of the antibiotic, leading to a ring opening event and linearization of the molecule. http://purl.obolibrary.org/obo/ARO_3007210 Nocardia farcinica rox http://purl.obolibrary.org/obo/ARO_3000445 rifampin monooxygenase Nocardia farcinica rox is a rifampin monooxygenase that inactivates rifampin. http://purl.obolibrary.org/obo/ARO_3007211 NDM-34 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase NDM-34 is a NDM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007212 NDM-35 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase NDM-35 is a NDM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007213 NDM-36 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase NDM-36 is a NDM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007214 NDM-37 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase NDM-37 is a NDM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007215 NDM-38 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase NDM-38 is a NDM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007216 NDM-39 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase NDM-39 is a NDM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007217 NDM-40 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase NDM-40 is a NDM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007218 NDM-41 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase NDM-41 is a NDM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007219 NDM-42 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase NDM-42 is a NDM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007220 NDM-43 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase NDM-43 is a NDM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007221 trispicen A http://purl.obolibrary.org/obo/ARO_3007133 polypyridine metallo-beta-lactamase inhibitor An experimental polypyridine ligand used as a metallo-beta-lactamase inhibitor. http://purl.obolibrary.org/obo/ARO_3007222 inhibitor of antibiotic resistance mechanism http://purl.obolibrary.org/obo/ARO_0000076 resistance-modifying agents A class of antibiotic adjuvant in which the adjuvant directly or indirectly inhibits the mechanism of resistance, restoring antibiotic susceptibility or decreasing the minimum inhibitory concentration. http://purl.obolibrary.org/obo/ARO_3007223 adjuvants enhancing antibiotic entry http://purl.obolibrary.org/obo/ARO_0000076 resistance-modifying agents A class of antibiotic adjuvants which enhance the antibiotic capability to enter the cell through passive or active membrane transport. http://purl.obolibrary.org/obo/ARO_3007224 adjuvants inhibiting antibiotic removal http://purl.obolibrary.org/obo/ARO_0000076 resistance-modifying agents A class of adjuvants which inhibit or prevent the cellular removal of an antibiotic through mechanisms including antibiotic efflux. http://purl.obolibrary.org/obo/ARO_3007225 adjuvants which alter physiology http://purl.obolibrary.org/obo/ARO_0000076 resistance-modifying agents A class of antibiotic adjuvants which indirectly increase antibiotic susceptibility through alterations to cellular physiology, for example those adjuvants which inhibit biofilm formation. http://purl.obolibrary.org/obo/ARO_3007226 host-related antibiotic adjuvants http://purl.obolibrary.org/obo/ARO_0000076 resistance-modifying agents A class of antibiotic adjuvants which indirectly improve antibiotic susceptibility or retention through alterations to host physiology or metabolism. http://purl.obolibrary.org/obo/ARO_3007435 WUS-1 http://purl.obolibrary.org/obo/ARO_3007440 WUS beta-lactamase WUS-1 is a WUS beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007436 KPC-96 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-96 is a KPC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007437 EBR-5 http://purl.obolibrary.org/obo/ARO_3004204 EBR beta-lactamase EBR-5 is an EBR beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007438 LAQ-1 http://purl.obolibrary.org/obo/ARO_3007441 LAQ beta lactamase LAQ-1 beta lactamase is a class C beta lactamase. http://purl.obolibrary.org/obo/ARO_3007439 SSA beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase SSA beta-lactamases are a family of Class A beta-lactamases. http://purl.obolibrary.org/obo/ARO_3007440 WUS beta-lactamase http://purl.obolibrary.org/obo/ARO_3000004 class B (metallo-) beta-lactamase WUS is a family of the metallo-beta-lactamases. http://purl.obolibrary.org/obo/ARO_3007441 LAQ beta lactamase http://purl.obolibrary.org/obo/ARO_3000076 class C beta-lactamase LAQ is a class C beta lactamase. http://purl.obolibrary.org/obo/ARO_3007442 SSA http://purl.obolibrary.org/obo/ARO_3007439 SSA beta-lactamase SSA is an SSA beta lactamase. http://purl.obolibrary.org/obo/ARO_3007443 NDM-44 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase NDM-44 is a subclass B1 NDM metallo-beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007444 NDM-45 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase NDM-45 is a NDM class B metallo beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007445 NDM-46 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase NDM-46 is an NDM metallo-beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007446 KPC-100 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-100 is an inhibitor-resistant carbapenem-hydrolyzing KPC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007447 NDM-47 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase NDM-47 is a NDM metallo-beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007448 TEM-246 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-246 is a class A TEM beta-lactamase found in Neisseria gonorrhoeae. http://purl.obolibrary.org/obo/ARO_3007449 KPC-97 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-97 is a KPC class A beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007450 KPC-98 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-98 is a KPC beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007451 TEM-247 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-247 is a TEM class A beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007452 KPC-99 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-99 is a KPC class A beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007453 TEM-244 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-244 is a TEM beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007454 TEM-245 http://purl.obolibrary.org/obo/ARO_3000014 TEM beta-lactamase TEM-245 is a TEM class A beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007455 cethromycin http://purl.obolibrary.org/obo/ARO_0000000 macrolide antibiotic Cethromycin is a ketolide (macrolide) antibiotic, with a similar mechanism to telithromycin, with activity against selected gram-positive, gram-negative, atypical bacteria, and even designed for tularemia, plague, and anthrax prophylaxis. http://purl.obolibrary.org/obo/ARO_3007456 dfrL http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr dfrL is a gene encoding a trimethoprim-resistant dihydrofolate reductase (DHFR) identified in Staphylococcus aureus. http://purl.obolibrary.org/obo/ARO_3007457 carrimycin http://purl.obolibrary.org/obo/ARO_0000000 macrolide antibiotic Carrimycin is a macrolide antibiotic produced by genetically engineered Streptomyces spiramyceticus and may be active against some Gram-positive bacteria and Mycobacterium tuberculosis. http://purl.obolibrary.org/obo/ARO_3007458 cefovecin http://purl.obolibrary.org/obo/ARO_3009107 third-generation cephalosporin Cefovecin is a cephalosporin antibiotic used for the treatment of skin infections in cats and dogs. It is used for the treatment of skin infections caused by Pasturella multocida in cats, and Staphylococcus in dogs. http://purl.obolibrary.org/obo/ARO_3007459 EstT http://purl.obolibrary.org/obo/ARO_3000320 macrolide esterase EstT is a gene encoding for a serine-dependent macrolide alpha/beta-hydrolase. http://purl.obolibrary.org/obo/ARO_3007460 IMP-91 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-91 is an IMP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007461 IMP-96 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-96 is an IMP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007462 IMP-92 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-92 is an IMP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007463 IMP-93 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-93 is an IMP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007464 IMP-94 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-94 is an IMP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007465 IMP-95 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase IMP-95 is an IMP beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007466 BP2 http://purl.obolibrary.org/obo/ARO_3007136 unclassified metallo-beta-lactamase inhibitor BP2 is a novel beta-lactam-derived beta-lactamase inhibitor, efficacious when co-administered with meropenem in K. pneumoniae. http://purl.obolibrary.org/obo/ARO_3007467 sulbactam-durlobactam http://purl.obolibrary.org/obo/ARO_3000707 antibiotic mixture SUL-DUR or sulbactam-durlobactam (formerly ETX2514SUL) is a novel beta-lactam-beta-lactamase inhibitor designed specifically for the treatment of carbapenem-resistant Acinetobacter baumannii (CRAB). http://purl.obolibrary.org/obo/ARO_3007468 sulfanilamide http://purl.obolibrary.org/obo/ARO_3000282 sulfonamide antibiotic Sulfanilamide is a sulfonamide anti-infective used to treat vulvovaginal candidiasis caused by Candida albicans. http://purl.obolibrary.org/obo/ARO_3007469 sulfamerazine http://purl.obolibrary.org/obo/ARO_3000282 sulfonamide antibiotic Sulfamerazine is a sulfonamide anti-infective used to treat bacterial infections, such as bronchitis, prostatitis, and urinary tract infections. http://purl.obolibrary.org/obo/ARO_3007470 IND-17 http://purl.obolibrary.org/obo/ARO_3000060 IND beta-lactamase IND-17 is an IND beta-lactamase and confers resistance to ampicillin, nitrocefin, cefazolin, cefuroxime, ceftazidime, imipenem, meropenem in Chryseobacterium spp. http://purl.obolibrary.org/obo/ARO_3007471 narasin http://purl.obolibrary.org/obo/ARO_3005163 ionophore with antibiotic activity Narasin is polyether ionophore antibiotic. It is a derivative of salinomycin with an additional methyl group. Narasin is produced by fermentation of a strain of Streptomyces aureofaciens. http://purl.obolibrary.org/obo/ARO_3007472 tilmicosin http://purl.obolibrary.org/obo/ARO_0000000 macrolide antibiotic Tilmicosin is a macrolide antibiotic used for livestock and poultry synthesized from tylomycin. It is mainly used to treat common bacterial infections and diseases caused by mycoplasma infection in livestock and poultry breeding. Tilmicosin has broad-spectrum antibacterial properties and has a strong inhibitory effect on most Gram positive and negative bacteria. http://purl.obolibrary.org/obo/ARO_3007473 Mycobacterium avium gyrA with mutation conferring resistance to fluoroquinolone http://purl.obolibrary.org/obo/ARO_3003292 fluoroquinolone resistant gyrA Amino acid substitution mutations in Mycobacterium avium gyrA observed to confer resistance to fluoroquinolone antibiotics. http://purl.obolibrary.org/obo/ARO_3007760 tulathromycin http://purl.obolibrary.org/obo/ARO_0000000 macrolide antibiotic Tulathromycin is an antibacterial of the macrolide class of drugs. It is a 15-membered macrolide structure and considered a triamilide macrolide with three charged nitrogens. It is derived from azalide macrolides, such as azithromycin. http://purl.obolibrary.org/obo/ARO_3007761 gamithromycin http://purl.obolibrary.org/obo/ARO_0000000 macrolide antibiotic Gamithromycin, a novel semi-synthetic macrolide, is approved for the treatment and prevention of bovine respiratory disease. It plays a bacteriostatic and bactericidal role by inhibiting the ribosomal 50S subunit. http://purl.obolibrary.org/obo/ARO_3007762 tildipirosin http://purl.obolibrary.org/obo/ARO_0000000 macrolide antibiotic Tildipirosin, a 16-membered-ring macrolide antimicrobial, has recently been approved for the treatment of swine respiratory disease and bovine respiratory disease. This macrolide is extensively distributed to the site of respiratory infection followed by slow elimination. http://purl.obolibrary.org/obo/ARO_3007763 Marinomycin http://purl.obolibrary.org/obo/ARO_0000000 macrolide antibiotic Four antitumor-antibiotics of a new structure class, the marinomycins A-D (1-4), were isolated from the saline culture of a new group of marine actinomycetes. The structures of the marinomycins are unusual macrodiolides composed of dimeric 2-hydroxy-6-alkenyl-benzoic acid lactones with conjugated tetraene-pentahydroxy polyketide chains. http://purl.obolibrary.org/obo/ARO_3007764 Marinomycin A http://purl.obolibrary.org/obo/ARO_3007763 Marinomycin Marinomycin A is a member of a new class of bis-salicylate-containing polyene macrodiolides, which have potent antibiotic activity against methicillin-resistant Staphylococcus aureus and vancomycin-resistant Enterococcus faecium. http://purl.obolibrary.org/obo/ARO_3007765 Marinomycin B http://purl.obolibrary.org/obo/ARO_3007763 Marinomycin Marinomycin B is a member of a new class of bis-salicylate-containing polyene macrodiolides, which have potent antibiotic activity against methicillin-resistant Staphylococcus aureus and vancomycin-resistant Enterococcus faecium. http://purl.obolibrary.org/obo/ARO_3007766 Marinomycin C http://purl.obolibrary.org/obo/ARO_3007763 Marinomycin Marinomycin C is a member of a new class of bis-salicylate-containing polyene macrodiolides, which have potent antibiotic activity against methicillin-resistant Staphylococcus aureus and vancomycin-resistant Enterococcus faecium. http://purl.obolibrary.org/obo/ARO_3007767 Marinomycin D http://purl.obolibrary.org/obo/ARO_3007763 Marinomycin Marinomycin D is a member of a new class of bis-salicylate-containing polyene macrodiolides, which have potent antibiotic activity against methicillin-resistant Staphylococcus aureus and vancomycin-resistant Enterococcus faecium. http://purl.obolibrary.org/obo/ARO_3007768 tetronomycin http://purl.obolibrary.org/obo/ARO_3005163 ionophore with antibiotic activity Tetronomycin, C34H50O8, isolated from a strain of Streptomyces sp. nov. represents a novel polycyclic ionophore polyether. http://purl.obolibrary.org/obo/ARO_3007769 cezomycin http://purl.obolibrary.org/obo/ARO_3005163 ionophore with antibiotic activity Cezomycin is a polyether divalent cation ionophore secondary metabolite produced by Streptomyces chartreusis. http://purl.obolibrary.org/obo/ARO_3007770 aac(6')-Ib-cr10 http://purl.obolibrary.org/obo/ARO_3005113 AAC(6')-Ib-cr A fluoroquinolone-acetylating aminoglycoside acetyltransferase variant, identified from Escherichia coli. These variants confers resistance to both aminoglycoside and fluoroquinolone antibiotics. http://purl.obolibrary.org/obo/ARO_3007771 aac(6')-Ib-cr11 http://purl.obolibrary.org/obo/ARO_3005113 AAC(6')-Ib-cr A fluoroquinolone-acetylating aminoglycoside acetyltransferase variant identified from Proteus mirabilis. These proteins confer resistance to both fluoroquinolone and aminoglycoside antibiotics. http://purl.obolibrary.org/obo/ARO_3007772 valinomycin http://purl.obolibrary.org/obo/ARO_3005163 ionophore with antibiotic activity Valinomycin is a depsipeptide antibiotic which selectively translocates potassium across biologic membranes. This potassium ionophore was observed to inhibit phytohemagglutinin-stimulated blastogenesis and proliferation in human lymphocytes. http://purl.obolibrary.org/obo/ARO_3007773 bis-indole alkaloid with antibiotic activity http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule Bisindoles are structurally complex dimers and are intriguing targets for partial and total synthesis. They exhibit stronger biological activity than their corresponding monomeric units. http://purl.obolibrary.org/obo/ARO_3007774 dragmacidin A http://purl.obolibrary.org/obo/ARO_3007773 bis-indole alkaloid with antibiotic activity Spongosorites has yielded a bis-indole alkaloid which we have named dragmacidin G. Dragmacidin G is the first in this series of compounds to have a pyrazine ring linking the two indole rings. It also has a rare N-(2-mercaptoethyl)-guanidine side chain. Dragmacidin G shows a broad spectrum of biological activity including inhibition of methicillin-resistant Staphylococcus aureus, Mycobacterium tuberculosis, Plasmodium falciparum, and a panel of pancreatic cancer cell lines. http://purl.obolibrary.org/obo/ARO_3007775 dragmacidin B http://purl.obolibrary.org/obo/ARO_3007773 bis-indole alkaloid with antibiotic activity Spongosorites has yielded a bis-indole alkaloid which we have named dragmacidin G. Dragmacidin G is the first in this series of compounds to have a pyrazine ring linking the two indole rings. It also has a rare N-(2-mercaptoethyl)-guanidine side chain. Dragmacidin G shows a broad spectrum of biological activity including inhibition of methicillin-resistant Staphylococcus aureus, Mycobacterium tuberculosis, Plasmodium falciparum, and a panel of pancreatic cancer cell lines. http://purl.obolibrary.org/obo/ARO_3007776 dragmacidin D http://purl.obolibrary.org/obo/ARO_3007773 bis-indole alkaloid with antibiotic activity Spongosorites has yielded a bis-indole alkaloid which we have named dragmacidin G. Dragmacidin G is the first in this series of compounds to have a pyrazine ring linking the two indole rings. It also has a rare N-(2-mercaptoethyl)-guanidine side chain. Dragmacidin G shows a broad spectrum of biological activity including inhibition of methicillin-resistant Staphylococcus aureus, Mycobacterium tuberculosis, Plasmodium falciparum, and a panel of pancreatic cancer cell lines. http://purl.obolibrary.org/obo/ARO_3007777 dragmacidin E http://purl.obolibrary.org/obo/ARO_3007773 bis-indole alkaloid with antibiotic activity Spongosorites has yielded a bis-indole alkaloid which we have named dragmacidin G. Dragmacidin G is the first in this series of compounds to have a pyrazine ring linking the two indole rings. It also has a rare N-(2-mercaptoethyl)-guanidine side chain. Dragmacidin G shows a broad spectrum of biological activity including inhibition of methicillin-resistant Staphylococcus aureus, Mycobacterium tuberculosis, Plasmodium falciparum, and a panel of pancreatic cancer cell lines. http://purl.obolibrary.org/obo/ARO_3007778 dragmacidin F http://purl.obolibrary.org/obo/ARO_3007773 bis-indole alkaloid with antibiotic activity Spongosorites has yielded a bis-indole alkaloid which we have named dragmacidin G. Dragmacidin G is the first in this series of compounds to have a pyrazine ring linking the two indole rings. It also has a rare N-(2-mercaptoethyl)-guanidine side chain. Dragmacidin G shows a broad spectrum of biological activity including inhibition of methicillin-resistant Staphylococcus aureus, Mycobacterium tuberculosis, Plasmodium falciparum, and a panel of pancreatic cancer cell lines. http://purl.obolibrary.org/obo/ARO_3007779 halolitoralin http://purl.obolibrary.org/obo/ARO_3000053 peptide antibiotic Three new cyclopeptides, including halolitoralin A (a cyclic hexapeptide), halolitoralin B and C (two cyclic tetrapeptides), were isolated from Halobacillus litoralis YS3106. http://purl.obolibrary.org/obo/ARO_3007780 halolitoralin A http://purl.obolibrary.org/obo/ARO_3007779 halolitoralin Halolitoralin A is an alanine-rich cyclic hexapeptide. It exhibits potent activity against the pathogenic fungi Candida albicans and Trichophyton mentagrophytes and the gram negative bacteria Pseudomonas aeruginosa and Escherichia coli. Gram negative bacteria were found to be more sensitive than gram positive bacteria. It was also found to exhibit moderate anthelmintic activity against the earthworms Megascoplex konkanensis and Eudrilus sp. http://purl.obolibrary.org/obo/ARO_3007781 halolitoralin B http://purl.obolibrary.org/obo/ARO_3007779 halolitoralin Halolitoralin B is an alanine-rich cyclic hexapeptide. It exhibits potent activity against the pathogenic fungi Candida albicans and Trichophyton mentagrophytes and the gram negative bacteria Pseudomonas aeruginosa and Escherichia coli. Gram negative bacteria were found to be more sensitive than gram positive bacteria. It was also found to exhibit moderate anthelmintic activity against the earthworms Megascoplex konkanensis and Eudrilus sp. http://purl.obolibrary.org/obo/ARO_3007782 halolitoralin C http://purl.obolibrary.org/obo/ARO_3007779 halolitoralin Halolitoralin C is an alanine-rich cyclic hexapeptide. It exhibits potent activity against the pathogenic fungi Candida albicans and Trichophyton mentagrophytes and the gram negative bacteria Pseudomonas aeruginosa and Escherichia coli. Gram negative bacteria were found to be more sensitive than gram positive bacteria. It was also found to exhibit moderate anthelmintic activity against the earthworms Megascoplex konkanensis and Eudrilus sp. http://purl.obolibrary.org/obo/ARO_3007783 macrocyclic peptide antibiotics http://purl.obolibrary.org/obo/ARO_3000053 peptide antibiotic Macrocyclic peptides are predominantly peptide structures bearing one or more rings and spanning multiple amino acid residues. Macrocyclization has become a common approach for improving the pharmacological properties and bioactivity of peptides. http://purl.obolibrary.org/obo/ARO_3007784 zosurabalpin http://purl.obolibrary.org/obo/ARO_3007783 macrocyclic peptide antibiotics Zosurabalpin is a macrocyclic peptide (MCP) antibiotic with potent antibacterial activity against Carbapenem-resistant Acinetobacter baumannii. The mechanism of action involves blocking the transport of bacterial lipopolysaccharide from the inner membrane to its destination on the outer membrane, through inhibition of the LptB2FGC complex. http://purl.obolibrary.org/obo/ARO_3007785 nocardamine http://purl.obolibrary.org/obo/ARO_3000053 peptide antibiotic Nocardamine is a cyclic trihydroxamate. It belongs to a group of microbial siderophores which form complexes with iron and aluminum ions. Nocardamine was described first as an antibiotic active against mycobacteria and proteus. It is produced by Nocardia species, several Streptomyces species, Chromobacterium and Pseudomonas. http://purl.obolibrary.org/obo/ARO_3007786 Tartrolon http://purl.obolibrary.org/obo/ARO_0000000 macrolide antibiotic Tartrolons are a group of boron-containing macrolide antibiotics discovered in 1994 from the culture broth of the myxobacterium Sorangium cellulosum. http://purl.obolibrary.org/obo/ARO_3007787 tartrolon A http://purl.obolibrary.org/obo/ARO_3007786 Tartrolon Tartrolons are a group of boron-containing (excluding tartrolon A) macrolide antibiotics discovered in 1994 from the culture broth of the myxobacterium Sorangium cellulosum. http://purl.obolibrary.org/obo/ARO_3007788 tartrolon B http://purl.obolibrary.org/obo/ARO_3007786 Tartrolon Tartrolons are a group of boron-containing (excluding tartrolon A) macrolide antibiotics discovered in 1994 from the culture broth of the myxobacterium Sorangium cellulosum. http://purl.obolibrary.org/obo/ARO_3007789 tartrolon D http://purl.obolibrary.org/obo/ARO_3007786 Tartrolon Tartrolons are a group of boron-containing (excluding tartrolon A) macrolide antibiotics discovered in 1994 from the culture broth of the myxobacterium Sorangium cellulosum. http://purl.obolibrary.org/obo/ARO_3007790 tartrolon F http://purl.obolibrary.org/obo/ARO_3007786 Tartrolon Tartrolons are a group of boron-containing (excluding tartrolon A) macrolide antibiotics discovered in 1994 from the culture broth of the myxobacterium Sorangium cellulosum. http://purl.obolibrary.org/obo/ARO_3007791 tartrolon G http://purl.obolibrary.org/obo/ARO_3007786 Tartrolon Tartrolons are a group of boron-containing (excluding tartrolon A) macrolide antibiotics discovered in 1994 from the culture broth of the myxobacterium Sorangium cellulosum. http://purl.obolibrary.org/obo/ARO_3007792 aplasmomycin http://purl.obolibrary.org/obo/ARO_0000000 macrolide antibiotic Aplasmomycin was isolated from a broth cultivated with a marine isolate of actinomycete, and inhibits Gram-positive bacteria in vitro and Plasmodium berghei in vivo. It is a natural ionophore. http://purl.obolibrary.org/obo/ARO_3007793 boromycin http://purl.obolibrary.org/obo/ARO_0000000 macrolide antibiotic Boromycin is a bacteriocidal polyether-macrolide antibiotic initially isolated from the Streptomyces antibioticus. It is effective against most Gram-positive bacteria, but is ineffective against Gram-negative bacteria. http://purl.obolibrary.org/obo/ARO_3007794 Vibrio vulnificus rpoB mutants conferring resistance to rifampin http://purl.obolibrary.org/obo/ARO_3000210 rifamycin-resistant beta-subunit of RNA polymerase (rpoB) Point mutations that occur within the Vibrio vulnificus rpoB gene resulting in resistance to rifampin. http://purl.obolibrary.org/obo/ARO_3007795 Azalomycin F http://purl.obolibrary.org/obo/ARO_0000000 macrolide antibiotic Azalomycin F, a natural guanidyl-containing polyhydroxy macrolide produced by many streptomycete strains, can target the LTA of Staphylococcus aureus. http://purl.obolibrary.org/obo/ARO_3007796 tylvalosin http://purl.obolibrary.org/obo/ARO_0000000 macrolide antibiotic Tylvalosin is indicated for the control of porcine proliferative enteropathy associated with Lawsonia intracellularis infection in groups of swine. http://purl.obolibrary.org/obo/ARO_3007797 ampR transcriptional regulator with mutation conferring resistance to monobactam antibiotics http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant ampR is a LysR-type transcriptional regulator for beta-lactamase-encoding gene expression. Mutations in ampR of certain organisms have been shown to confer resistance to antibiotics due to beta-lactamase overexpression. http://purl.obolibrary.org/obo/ARO_3007798 Mycobacterium tuberculosis iniA mutations conferring resistance to isoniazid http://purl.obolibrary.org/obo/ARO_3007799 isoniazid resistant iniA Known mutations in Mycobacterium tuberculosis iniA which confer resistance to isoniazid. http://purl.obolibrary.org/obo/ARO_3007799 isoniazid resistant iniA http://purl.obolibrary.org/obo/ARO_3003446 antibiotic resistant iniA Mutations that occurs on the iniA genes resulting in the resistance to isoniazid. http://purl.obolibrary.org/obo/ARO_3007800 RATA beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase RATA is a family of class A carbapenemases identified from the chromosome of Riemerella anatipestifer. http://purl.obolibrary.org/obo/ARO_3007801 RATA-1 http://purl.obolibrary.org/obo/ARO_3007800 RATA beta-lactamase RATA-1 is a class A RATA-family carbapenemase. http://purl.obolibrary.org/obo/ARO_3007802 RATA-2 http://purl.obolibrary.org/obo/ARO_3007800 RATA beta-lactamase RATA-2 is a class A RATA-family carbapenemase. http://purl.obolibrary.org/obo/ARO_3007803 CARB-56 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-56 is a class A CARB-17-like beta-lactamase identified from Vibrio alginolyticus. http://purl.obolibrary.org/obo/ARO_3007804 VIM-74 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-74 is a subclass B1 carbapenem-hydrolyzing metallo-beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007805 Mycobacterium tuberculosis tlyA mutations conferring resistance to capreomycin http://purl.obolibrary.org/obo/ARO_3003443 Antibiotic resistant tlyA Specific mutations in Mycobacterium tuberculosis tlyA resulting in resistance to capreomycin. http://purl.obolibrary.org/obo/ARO_3007806 Mycobacterium tuberculosis gyrA mutations conferring resistance to moxifloxacin http://purl.obolibrary.org/obo/ARO_3003292 fluoroquinolone resistant gyrA Specific mutations in Mycobacterium tuberculosis gyrA resulting in resistance to moxifloxacin. http://purl.obolibrary.org/obo/ARO_3007807 Mycobacterium tuberculosis gyrA mutations conferring resistance to ofloxacin http://purl.obolibrary.org/obo/ARO_3003292 fluoroquinolone resistant gyrA Specific mutations in Mycobacterium tuberculosis gyrA resulting in resistance to ofloxacin. http://purl.obolibrary.org/obo/ARO_3007808 Mycobacterium tuberculosis gyrB mutations conferring resistance to ofloxacin http://purl.obolibrary.org/obo/ARO_3000864 fluoroquinolone resistant gyrB Specific mutations in Mycobacterium tuberculosis gyrB resulting in resistance to ofloxacin. http://purl.obolibrary.org/obo/ARO_3007809 Mycobacterium tuberculosis gyrA mutations conferring resistance to levofloxacin http://purl.obolibrary.org/obo/ARO_3003292 fluoroquinolone resistant gyrA Specific mutations in Mycobacterium tuberculosis gyrA resulting in resistance to levofloxacin. http://purl.obolibrary.org/obo/ARO_3007810 Mycobacterium tuberculosis gyrB mutations conferring resistance to levofloxacin http://purl.obolibrary.org/obo/ARO_3000864 fluoroquinolone resistant gyrB Specific mutations in Mycobacterium tuberculosis gyrB resulting in resistance to levofloxacin. http://purl.obolibrary.org/obo/ARO_3007811 Mycobacterium tuberculosis fabG1 with mutations conferring resistance to prothionamide http://purl.obolibrary.org/obo/ARO_3007841 prothionamide resistant fabG1 Specific mutations in Mycobacterium tuberculosis fabG1 resulting in resistance to prothionamide. http://purl.obolibrary.org/obo/ARO_3007812 VIM-75 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-75 is a subclass B1 carbapenem-hydrolyzing metallo-beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007813 VIM-76 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-76 is a subclass B1 carbapenem-hydrolyzing metallo-beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007814 VIM-77 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-77 is a subclass B1 carbapenem-hydrolyzing metallo-beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007815 VIM-78 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-78 is a subclass B1 carbapenem-hydrolyzing metallo-beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007816 VIM-79 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-79 is a subclass B1 carbapenem-hydrolyzing metallo-beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007817 VIM-80 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-80 is a subclass B1 carbapenem-hydrolyzing metallo-beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007818 VIM-81 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-81 is a subclass B1 carbapenem-hydrolyzing metallo-beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007819 VIM-82 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-82 is a subclass B1 carbapenem-hydrolyzing metallo-beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007820 VIM-83 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-83 is a subclass B1 carbapenem-hydrolyzing metallo-beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007821 VIM-84 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-84 is a subclass B1 carbapenem-hydrolyzing metallo-beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007822 VIM-85 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-85 is a subclass B1 carbapenem-hydrolyzing metallo-beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007823 VIM-86 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-86 is a subclass B1 carbapenem-hydrolyzing metallo-beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007824 VIM-87 http://purl.obolibrary.org/obo/ARO_3000021 VIM beta-lactamase VIM-87 is a subclass B1 carbapenem-hydrolyzing metallo-beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007825 GES-47 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-47 is a class A carbapenem-hydrolyzing GES-like beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007826 GES-48 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-48 is a class A carbapenem-hydrolyzing GES-like beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007827 GES-49 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES_49 is a class A carbapenem-hydrolyzing GES-like beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007828 GES-50 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-50 is a class A carbapenem-hydrolyzing GES-like beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007829 GES-51 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-51 is a class A carbapenem-hydrolyzing GES-like beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007830 GES-52 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-52 is a class A GES-like extended-spectrum beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007831 GES-53 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-53 is a class A carbapenem-hydrolyzing GES-like beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007832 GES-54 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-54 is a class A carbapenem-hydrolyzing GES-like beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007833 GES-55 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES is a class A GES-like beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007834 GES-56 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-56 is a class A GES-like beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007835 GES-57 http://purl.obolibrary.org/obo/ARO_3000066 GES beta-lactamase GES-57 is a class A GES-like beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007836 CARB-57 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-57 is a class A carbenicillin-hydrolyzing CARB-like beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007837 CARB-58 http://purl.obolibrary.org/obo/ARO_3000091 CARB beta-lactamase CARB-58 is a PSE family class A carbenicillin-hydrolyzing CARB-like beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007838 tet(65) http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump tet(65) is a tetracycline efflux gene identified from a Corynebacterium oculi plasmid. http://purl.obolibrary.org/obo/ARO_3007839 CIM beta-lactamase http://purl.obolibrary.org/obo/ARO_3000568 subclass B1 (metallo-) beta-lactamase CIM (C. indologenes MBL) are a family of subclass B1 metallo-beta-lactamases originally identified from Chryseobacterium indologenes, and which exhibit carbapenem-hydrolyzing activity. http://purl.obolibrary.org/obo/ARO_3007840 CIM-1 http://purl.obolibrary.org/obo/ARO_3007839 CIM beta-lactamase CIM-1 is a CIM-like carbapenem-hydrolyzing metallo-beta-lactamase identified from Chryseobacterium indologenes. http://purl.obolibrary.org/obo/ARO_3007841 prothionamide resistant fabG1 http://purl.obolibrary.org/obo/ARO_3004887 antibiotic resistant fabG1 Antibiotic resistant gene variants of mycobacterial fabG1 which confer resistance to prothionamide antibiotics. http://purl.obolibrary.org/obo/ARO_3007842 Lahey list of beta-lactamases http://purl.obolibrary.org/obo/ARO_3000045 component of AMR genotypic or phenotypic terminology A historical list of beta-lactamase names, a minority without public sequence data, maintained by Drs. Karen Bush, George Jacoby, and Timothy Palzkill. Since subsumed by curation efforts at the National Center for Biotechnology Information, https://www.ncbi.nlm.nih.gov/bioproject/305729. http://purl.obolibrary.org/obo/ARO_2000007 targeted_by A relationship ontology term in which the subject is targeted by the object (usually a class of antibiotics). http://purl.obolibrary.org/obo/ARO_2000003 outer_membrane_protein_of A component of tripartite efflux systems that resides in the outer membrane of Gram-negative bacteria. The outer membrane protein forms a channel or pore that spans the outer membrane, enabling the export of substrates directly into the extracellular environment. http://purl.obolibrary.org/obo/ARO_3009193 ARO relationship type http://purl.obolibrary.org/obo/ARO_3000045 component of AMR genotypic or phenotypic terminology Ontological connectedness between entities and/or interactions representing their relatedness or influence (paraphrased from Systems Biology Ontology) specific to CARD's Antibiotic Resistance Ontology. http://purl.obolibrary.org/obo/ARO_3009185 azoxystrobin http://purl.obolibrary.org/obo/ARO_3009165 antifungal without defined classification Azoxystrobin (brand name Amistar, Syngenta) is widely used as a very broad spectrum fungicide in agriculture, particularly in wheat farming. It is an inhibitor of mitochondrial respiration by blocking electron transfer between cytochromes b and c1, and binds very tightly to the Qo site of Complex III of the mitochondrial electron transport chain, thereby ultimately preventing the generation of ATP. http://purl.obolibrary.org/obo/ARO_3005097 mecC-type BlaZ http://purl.obolibrary.org/obo/ARO_3004197 BlaZ beta-lactamase A blaZ-like beta-lactamase found in S. Aureus. http://purl.obolibrary.org/obo/ARO_3005098 qacL http://purl.obolibrary.org/obo/ARO_0010003 small multidrug resistance (SMR) antibiotic efflux pump A subunit of the qac multidrug efflux pump in Vibrio cholerae. http://purl.obolibrary.org/obo/ARO_3005099 23S rRNA (adenine(2058)-N(6))-methyltransferase Erm(A) http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase Variant of ErmA (ARO:3000347) found in Streptococcus pyogenes. Confers the MLSb phenotype. http://purl.obolibrary.org/obo/ARO_3005100 FosB2 http://purl.obolibrary.org/obo/ARO_3000133 fosfomycin thiol transferase Subtype of FosB (ARO:3000172). Present in multiple species. http://purl.obolibrary.org/obo/ARO_3005101 prothionamide resistant katG http://purl.obolibrary.org/obo/ARO_3004266 antibiotic resistant katG Mutations associated with katG conferring resistance to prothionamide, an analogue of isoniazid. Like isoniazid, prothionamide targets lnhA. http://purl.obolibrary.org/obo/ARO_3005102 Mycobacterium tuberculosis katG mutations conferring resistance to prothionamide http://purl.obolibrary.org/obo/ARO_3005101 prothionamide resistant katG Mutations in Mycobacterium tuberculosis katG conferring resistance to prothionamide, an analogue of isoniazid. http://purl.obolibrary.org/obo/ARO_3005103 isoniazid resistant ethA http://purl.obolibrary.org/obo/ARO_3003456 antibiotic resistant ethA Mutations in ethA conferring resistance to isoniazid. http://purl.obolibrary.org/obo/ARO_3005104 prothionamide resistant ethA http://purl.obolibrary.org/obo/ARO_3003456 antibiotic resistant ethA Mutations in ethA conferring resistance to prothionamide, an analogue of isoniazid. http://purl.obolibrary.org/obo/ARO_3005105 Mycobacterium tuberculosis ethA mutations conferring resistance to isoniazid http://purl.obolibrary.org/obo/ARO_3005103 isoniazid resistant ethA Mutations in Mycobacterium tuberculosis ethA conferring resistance to isoniazid. http://purl.obolibrary.org/obo/ARO_3005106 Mycobacterium tuberculosis ethA mutations conferring resistance to prothionamide http://purl.obolibrary.org/obo/ARO_3005104 prothionamide resistant ethA Mutations in Mycobacterium tuberculosis ethA conferring resistance to prothionamide, an analogue to isoniazid. http://purl.obolibrary.org/obo/ARO_3005107 prothionamide resistant mshA http://purl.obolibrary.org/obo/ARO_3004900 antibiotic resistant mshA Mutations in mshA conferring resistance to prothionamide, an analogue of isoniazid. http://purl.obolibrary.org/obo/ARO_3005108 Mycobacterium tuberculosis mshA mutations conferring resistance to prothionamide http://purl.obolibrary.org/obo/ARO_3005107 prothionamide resistant mshA Mutations in Mycobacterium tuberculosis mshA conferring resistance to prothionamide, an analogue to isoniazid. http://purl.obolibrary.org/obo/ARO_3005110 blaS http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase A class A beta-lactamase in Mycolicibacterium smegmatis. http://purl.obolibrary.org/obo/ARO_3005111 blaS1 http://purl.obolibrary.org/obo/ARO_3005110 blaS Predominant beta-lactamase in Mycolicibacterium smegmatis. http://purl.obolibrary.org/obo/ARO_3005112 AAC(6')-Ib-cr3 http://purl.obolibrary.org/obo/ARO_3005113 AAC(6')-Ib-cr A fluoroquinolone-acetylating aminoglycoside acetyltransferase variant identified from Aeromonas. These proteins confer resistance to both fluoroquinolone and aminoglycoside antibiotics. http://purl.obolibrary.org/obo/ARO_3005113 AAC(6')-Ib-cr http://purl.obolibrary.org/obo/ARO_3000345 AAC(6') A subfamily of aminoglycoside 6'-N-acetyltransferases, AAC(6'), which doubly confer resistance to aminoglycoside and fluoroquinolone antibiotics through fluoroquinolone-acetylating activity. http://purl.obolibrary.org/obo/ARO_3005114 AAC(6')-Ib-cr4 http://purl.obolibrary.org/obo/ARO_3005113 AAC(6')-Ib-cr A fluoroquinolone-acetylating aminoglycoside acetyltransferase variant identified from Enterobacter. These proteins confer resistance to both fluoroquinolone and aminoglycoside antibiotics. http://purl.obolibrary.org/obo/ARO_3005115 AAC(6')-Ib-cr5 http://purl.obolibrary.org/obo/ARO_3005113 AAC(6')-Ib-cr A fluoroquinolone-acetylating aminoglycoside acetyltransferase variant identified from Pseudomonas. These proteins confer resistance to both fluoroquinolone and aminoglycoside antibiotics. http://purl.obolibrary.org/obo/ARO_3005116 AAC(6')-Ib-cr6 http://purl.obolibrary.org/obo/ARO_3005113 AAC(6')-Ib-cr A fluoroquinolone-acetylating aminoglycoside acetyltransferase variant identified from Escherichia coli. These proteins confer resistance to both fluoroquinolone and aminoglycoside antibiotics. http://purl.obolibrary.org/obo/ARO_3005117 AAC(6')-Ib-cr7 http://purl.obolibrary.org/obo/ARO_3005113 AAC(6')-Ib-cr A fluoroquinolone-acetylating aminoglycoside acetyltransferase variant identified from Klebsiella. These proteins confer resistance to both fluoroquinolone and aminoglycoside antibiotics. http://purl.obolibrary.org/obo/ARO_3005118 AAC(6')-Ib-cr8 http://purl.obolibrary.org/obo/ARO_3005113 AAC(6')-Ib-cr A fluoroquinolone-acetylating aminoglycoside acetyltransferase variant, identified from Salmonella. These variants confers resistance to both aminoglycoside and fluoroquinolone antibiotics. http://purl.obolibrary.org/obo/ARO_3005119 AAC(6')-Ib-cr9 http://purl.obolibrary.org/obo/ARO_3005113 AAC(6')-Ib-cr A fluoroquinolone-acetylating aminoglycoside acetyltransferase variant, identified from Serratia. These variants confers resistance to both aminoglycoside and fluoroquinolone antibiotics. http://purl.obolibrary.org/obo/ARO_3005120 levonadifloxacin http://purl.obolibrary.org/obo/ARO_0000001 fluoroquinolone antibiotic A novel broad-spectrum anti-MRSA benzoquinolizine antibiotic effective against gram-positive and gram-negative pathogens. http://purl.obolibrary.org/obo/ARO_3005121 lsaD http://purl.obolibrary.org/obo/ARO_3004472 lsa-type ABC-F protein The lsa(D) gene represents an ABC-F subfamily protein expressed in Lactococcus garvieae. It confers resistance to Streptogramins A, Pleuromutilins and Lincosamides. http://purl.obolibrary.org/obo/ARO_3005122 PDC-68 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-68 is an ambler class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005123 PDC-70 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-70 is an ambler class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005124 PDC-63 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-63 is an ambler class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005125 PDC-57 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-57 is an ambler class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005126 PDC-66 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-66 is an ambler class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005127 PDC-14 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-14 is an ambler class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005128 PDC-47 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-47 is an ambler class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005129 PDC-51 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-51 is an ambler class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005130 OXA-846 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-846 is a class D beta-lactamase found in Pseudomonas aeruginosa. It is part of the OXA-50 family of oxacillin-hydrolyzing beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005131 NDM-29 http://purl.obolibrary.org/obo/ARO_3000057 NDM beta-lactamase An NDM metallo-beta-lactamase variant reported in Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3005132 PDC-11 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-11 is an ambler class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005133 PDC-62 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-62 is an ambler class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005134 PDC-43 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-43 is an ambler class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005135 PDC-54 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-54 is an ambler class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005136 OXA-906 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase OXA-906 is a class D beta-lactamase from the OXA-50 family found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005137 PDC-59 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-59 is an ambler class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005138 OXA-850 http://purl.obolibrary.org/obo/ARO_3007724 OXA-50-like beta-lactamase Pseudomonas aeruginosa strain OXA-50 family oxacillin-hydrolyzing class D beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005139 PDC-67 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-67 is an ambler class C beta-lactamase found in Pseudomonas aeruginosa strain 5065. http://purl.obolibrary.org/obo/ARO_3005140 PDC-56 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-56 is an ambler class C beta-lactamase found in Pseudomonas aeruginosa strain 4883. http://purl.obolibrary.org/obo/ARO_3005141 PDC-52 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-52 is an ambler class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005142 PDC-44 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-44 is an ambler class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005143 PDC-240 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-240 is an ambler class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005144 PDC-61 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-61 is an ambler class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005145 PDC-45 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-45 is an ambler class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005146 PDC-49 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-49 is an ambler class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005147 PDC-50 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-50 is an ambler class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005148 PDC-48 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-48 is an ambler class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005149 PAC beta-lactamase http://purl.obolibrary.org/obo/ARO_3000076 class C beta-lactamase PAC beta-lactamase is an inhibitior-resistant cephalosporin-hydrolyzing class C beta-lactamase. http://purl.obolibrary.org/obo/ARO_3005150 PAC-1 http://purl.obolibrary.org/obo/ARO_3005149 PAC beta-lactamase PAC-1 is an ambler class C beta-lactamase from the PAC beta-lactamase family. It is found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005151 PDC-53 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-53 is an ambler class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005152 PDC-72 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-72 is an ambler class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005153 PDC-69 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-69 is an ambler class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005155 PDC-23 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-23 is an ambler class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005156 PDC-28 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-28 is an ambler class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005157 PDC-41 http://purl.obolibrary.org/obo/ARO_3000098 PDC beta-lactamase PDC-41 is an ambler class C beta-lactamase found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3005158 OXA-668 http://purl.obolibrary.org/obo/ARO_3007713 OXA-274-like beta-lactamase OXA-668 is a class D beta-lactamase from the OXA-274 family of OXA beta-lactamases. http://purl.obolibrary.org/obo/ARO_3005159 OXA-818 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-818 is a class D beta-lactamase from the OXA-23 family of OXA beta-lactamases. http://purl.obolibrary.org/obo/ARO_3005160 OXA-812 http://purl.obolibrary.org/obo/ARO_3007710 OXA-23-like beta-lactamase OXA-812 is a class D beta-lactamase from the OXA-23 family of OXA beta-lactamases. http://purl.obolibrary.org/obo/ARO_3005162 FosA7.5 http://purl.obolibrary.org/obo/ARO_3000133 fosfomycin thiol transferase FosA7.5 is a variant of the FosA7 gene. This gene is unique from FosA7 in that it is found in Escherichia coli as opposed to Salmonella enterica. It confers resistance to fosfomycin. http://purl.obolibrary.org/obo/ARO_3005163 ionophore with antibiotic activity http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule Ionophores are chemical entities which reversibly bind ions. Many ionophores display antibacterial and antifungal properties. An ionophore will bind and transport ions through a cell membrane, thereby potentially disrupting membrane potential and modifying permeability. http://purl.obolibrary.org/obo/ARO_3005164 dfrA35 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr dfrA35 is a trimethoprim resistant dihydrofolate reductase gene found in the lncC plasmid pEc158 from E.coli. http://purl.obolibrary.org/obo/ARO_3005165 antibiotic drug class http://purl.obolibrary.org/obo/ARO_3004299 antimicrobial phenotype In an antimicrobial context, a drug class is a set of antibiotic molecules, including antibiotic/adjuvant combination medications, with similar chemical structures, molecular targets, and/or modes and mechanisms of action. http://purl.obolibrary.org/obo/ARO_3005166 tet(X1) http://purl.obolibrary.org/obo/ARO_3000036 tetracycline inactivation enzyme Tetracycline resistance gene tet(X) ortholog described by Fang et al. 2020. http://purl.obolibrary.org/obo/ARO_3005167 quinone with antibiotic activity http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule A class of organic compounds derived from aromatic compounds and exhibiting antibiotic activity. http://purl.obolibrary.org/obo/ARO_3005168 ansamycin antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule A class of compounds containing an aromatic moiety and an aliphatic chain, produced as a bacterial metabolite and exhibiting antibiotic properties to many gram-positive pathogens. http://purl.obolibrary.org/obo/ARO_3005169 alkaloids with antibiotic activity http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule Alkaloids are naturally occurring organic compounds containing the element nitrogen. Some alkaloid compounds exhibit specific antibacterial activity. http://purl.obolibrary.org/obo/ARO_3005170 metallophores with antibiotic activity http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule A metallophore is any organic substance capable of carrying a metallic element such as zinc or iron, typically through chelation. Some metallophores exhibit specific antibiotic activity. http://purl.obolibrary.org/obo/ARO_3005171 polyketide with antibiotic activity http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule Polyketides are a large group of secondary metabolites. Some polyketide compounds have been shown to possess antibiotic activity and qualities. http://purl.obolibrary.org/obo/ARO_3005172 terpene with antibiotic activity http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule Terpenes are a large class of naturally produced organic compounds, predominantly produced by plants such as conifers. Some terpenes have been shown to possess antibiotic qualities or activity. http://purl.obolibrary.org/obo/ARO_3005174 thiacalixarene derivatives http://purl.obolibrary.org/obo/ARO_3005386 disinfecting agents and antiseptics Derivatives of thiacalixarene exhibit antiseptic and antibacterial activity. http://purl.obolibrary.org/obo/ARO_3005175 perchlozone http://purl.obolibrary.org/obo/ARO_3007161 thiosemicarbazone antibiotic Perchlozone is a novel thiosemicarbazone used for the treatment of multidrug-resistant tuberculosis. It is similar to thiacetazone with only a different side chain attached to the thiosemicarbazone moiety. Perchlozone is a prodrug that is activated by ethA and inhibits the HadABC complex. http://purl.obolibrary.org/obo/ARO_3005176 CMY-158 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-158 is a beta-lactamase found in Escherichia coli. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3005177 CMY-173 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-173 is a beta-lactamase found in Escherichia coli. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3005178 Mycobacterium tuberculosis ethA mutations conferring resistance to perchlozone http://purl.obolibrary.org/obo/ARO_3005205 perchlozone resistant ethA Mutations in ethA conferring resistance to perchlozone, a novel thiosemicarbazone. http://purl.obolibrary.org/obo/ARO_3005180 CMY-147 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-147 is a beta-lactamase found in Escherichia coli. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3005181 CMY-146 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-146 is a beta-lactamase found in Escherichia coli. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3005182 CMY-156 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-156 is a beta-lactamase found in Escherichia coli. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3005183 CMY-160 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-160 is a beta-lactamase found in Escherichia coli. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3005184 CMY-162 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-162 is a beta-lactamase found in Escherichia coli. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3005185 CMY-140 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-140 is a beta-lactamase found in Escherichia coli. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3005186 CMY-164 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-164 is a beta-lactamase found in Escherichia coli. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3005187 CMY-161 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-161 is a beta-lactamase found in Escherichia coli. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3005188 CMY-165 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-165 is a beta-lactamase found in Escherichia coli. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3005189 CMY-166 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-166 is a beta-lactamase found in Escherichia coli. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3005190 CMY-149 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-149 is a beta-lactamase found in Proteus mirabilis. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3005191 CMY-139 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-139 is a beta-lactamase found in Escherichia coli. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3005192 CMY-148 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-148 is a beta-lactamase found in Escherichia coli. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3005193 CMY-163 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-163 is a beta-lactamase found in Escherichia coli. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3005194 CMY-154 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-154 is a beta-lactamase found in Escherichia coli. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3005195 CMY-142 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-142 is a beta-lactamase found in Escherichia coli. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3005196 CMY-141 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-141 is a beta-lactamase found in Escherichia coli. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3005197 CMY-145 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-145 is a beta-lactamase found in Escherichia coli. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3005198 CMY-157 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-96 is a beta-lactamase found in Citrobacter sp. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3005199 CMY-171 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-171 is a beta-lactamase found in Escherichia coli. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3005200 CMY-155 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-155 is a beta-lactamase found in Klebsiella sp. KF07. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3005201 bispicen http://purl.obolibrary.org/obo/ARO_3007133 polypyridine metallo-beta-lactamase inhibitor An experimental polypyridine ligand used as a metallo-beta-lactamase inhibitor. http://purl.obolibrary.org/obo/ARO_3005202 trispicen http://purl.obolibrary.org/obo/ARO_3007133 polypyridine metallo-beta-lactamase inhibitor An experimental polypyridine ligand used as a metallo-beta-lactamase inhibitor. http://purl.obolibrary.org/obo/ARO_3005204 CMY-143 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-143 is a beta-lactamase found in Escherichia coli. It confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3005205 perchlozone resistant ethA http://purl.obolibrary.org/obo/ARO_3003456 antibiotic resistant ethA Genetic variants of ethA from Mycobacterium spp. including tuberculosis, which confer resistance to the antibiotic perchlozone. http://purl.obolibrary.org/obo/ARO_3004726 cefpirome http://purl.obolibrary.org/obo/ARO_3009108 fourth-generation cephalosporin Cefpirome is a fourth generation cephalosporin with activity against methicillin-susceptible Staphylococcus aureus, coagulase-negative staphylococci and viridans group streptococci, and in vitro activity towards Streptococcus pneumoniae. http://purl.obolibrary.org/obo/ARO_3004727 cefsulodin http://purl.obolibrary.org/obo/ARO_3009107 third-generation cephalosporin Cefsulodin is a third generation cephalosporin with with activity against Pseudomonas spp., but little activity against other Gram-negative bacteria. http://purl.obolibrary.org/obo/ARO_3004728 carumonam http://purl.obolibrary.org/obo/ARO_0000004 monobactam Carumonam is a monobactam antibiotic. It has activity towards Gram-negative bacteria with negligible activity towards Gram-postitive bacteria. http://purl.obolibrary.org/obo/ARO_3004729 LYS228 http://purl.obolibrary.org/obo/ARO_0000004 monobactam A monobactam with potent activity against Enterobacteriaceae. Stable to metallo-B-lactamases and serine carbapenemases resulting in potency against the majority of extended-spectrum B-lactamase-producing and carbapenem-resistant Enterobacteriaceae strains tested. http://purl.obolibrary.org/obo/ARO_3004730 tva(A) http://purl.obolibrary.org/obo/ARO_3007068 Miscellaneous ABC-F subfamily ATP-binding cassette ribosomal protection proteins A pleuromutilin resistance gene encoding a predicted ABC-F transporter. The presence of inhibitory or sub-inhibitory concentrations of tiamulin showed that tva(A) confers reduced pleuromutilin susceptibility that does not lead to clinical resistance but facilitates the development of higher-level resistance via mutations in genes encoding ribosome-associated functions. http://purl.obolibrary.org/obo/ARO_3004731 Zabofloxacin http://purl.obolibrary.org/obo/ARO_0000001 fluoroquinolone antibiotic A fluoroquinolone with potent activity against Gram-positive pathogens. Showed the most potent in vitro and in vivo activities against drug-resistant Streptococcus pneumoniae. One of the most potent antibacterial agent against penicillin-resistant S. pneumoniae in a murine systemic infection model. http://purl.obolibrary.org/obo/ARO_3004732 Finafloxacin http://purl.obolibrary.org/obo/ARO_0000001 fluoroquinolone antibiotic An 8-cyano-substituted fluoroquinolone with increased antibacterial activity in acidic conditions in contrast to other fluoroquinolones which demonstrate reduced activity in lower pH. Finafloxacin showed increased bactericidal activity at pH 5 in comparison to pH 7 and ciprofloxacin at pH 5 in vitro. http://purl.obolibrary.org/obo/ARO_3004733 Nemonoxacin http://purl.obolibrary.org/obo/ARO_0000001 fluoroquinolone antibiotic A C-8-methoxy non-fluorinated quinolone exhibiting potent antibacterial activities against Gram-positive, including MRSA and fluoroquinolone-resistant MRSA, Gram-negative, and atypical pathogens, especially methicillin-resistant Staphylococcus aureus. http://purl.obolibrary.org/obo/ARO_3004734 ARL-1 http://purl.obolibrary.org/obo/ARO_3004742 ARL Beta-lactamase ARL-1 is a beta-lactamase gene found in Staphylococcus Arlettae. http://purl.obolibrary.org/obo/ARO_3004735 ARL-2 http://purl.obolibrary.org/obo/ARO_3004742 ARL Beta-lactamase ARL-2 is a beta-lactamase gene found in Staphylococcus Arlettae. http://purl.obolibrary.org/obo/ARO_3004736 ARL-3 http://purl.obolibrary.org/obo/ARO_3004742 ARL Beta-lactamase ARL-3 is a beta-lactamase gene found in Staphylococcus arlettae. http://purl.obolibrary.org/obo/ARO_3004737 ARL-4 http://purl.obolibrary.org/obo/ARO_3004742 ARL Beta-lactamase ARL-4 is a beta-lactamase gene found in Staphylococcus arlettae. http://purl.obolibrary.org/obo/ARO_3004738 ARL-5 http://purl.obolibrary.org/obo/ARO_3004742 ARL Beta-lactamase ARL-5 is a beta-lactamase gene found in Staphylococcus arlettae. http://purl.obolibrary.org/obo/ARO_3004739 ARL-6 http://purl.obolibrary.org/obo/ARO_3004742 ARL Beta-lactamase ARL-6 is a beta-lactamase gene found in Staphylococcus arlettae. http://purl.obolibrary.org/obo/ARO_3004740 AST-1 http://purl.obolibrary.org/obo/ARO_3004741 AST Beta-lactamase AST-1 is a broad-spectrum beta-lactamase gene found in Nocardia asteroides. http://purl.obolibrary.org/obo/ARO_3004741 AST Beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase A family of beta-lactamase known for their broad spectrum resistance profile. http://purl.obolibrary.org/obo/ARO_3004742 ARL Beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase ARL beta-lactamase is an AMR Gene Family associated with Staphylococcus arlettae. http://purl.obolibrary.org/obo/ARO_3004745 MIR-23 http://purl.obolibrary.org/obo/ARO_3000058 MIR beta-lactamase MIR-23, originally described as AZECL-25, is a class C beta-lactamase that is found in Enterobacter cloacae. http://purl.obolibrary.org/obo/ARO_3004746 BAT Beta-lactamase http://purl.obolibrary.org/obo/ARO_3000075 class D beta-lactamase BAT is a class D beta-lactamase. http://purl.obolibrary.org/obo/ARO_3004747 BAT-1 http://purl.obolibrary.org/obo/ARO_3004746 BAT Beta-lactamase BAT-1 is a class D beta-lactamase found in Bacillus atrophaeus. http://purl.obolibrary.org/obo/ARO_3004748 BCL Beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase BCL beta-lactamase is a class A beta-lactamase. http://purl.obolibrary.org/obo/ARO_3004749 BCL-1 http://purl.obolibrary.org/obo/ARO_3004748 BCL Beta-lactamase BCL-1 is a class A beta-lactamase found in Alkalihalobacillus clausii. http://purl.obolibrary.org/obo/ARO_3004750 BES Beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase BES beta-lactamase is a class A beta-lactamase family. http://purl.obolibrary.org/obo/ARO_3004751 BES-1 http://purl.obolibrary.org/obo/ARO_3004750 BES Beta-lactamase BES-1 is a class A beta-lactamase that is found in Serratia marcescens. http://purl.obolibrary.org/obo/ARO_3004752 BIC Beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase BIC is a class A beta-lactamase conferring resistance to carbapenem. http://purl.obolibrary.org/obo/ARO_3004753 BIC-1 http://purl.obolibrary.org/obo/ARO_3004752 BIC Beta-lactamase BIC-1 is a beta-lactamase conferring resistance to carbapenems that is found in Pseudomonas fluorescens. http://purl.obolibrary.org/obo/ARO_3004754 BIL Beta-lactamase http://purl.obolibrary.org/obo/ARO_3000076 class C beta-lactamase BIL beta-lactamase is plasmid-borne and is a class C beta-lactamase. http://purl.obolibrary.org/obo/ARO_3004755 BIL-1 http://purl.obolibrary.org/obo/ARO_3004754 BIL Beta-lactamase BIL-1 is a plasmid-borne beta-lactamase that is also a class C beta-lactamase. http://purl.obolibrary.org/obo/ARO_3004756 BKC Beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase BKC beta-lactamase is a class A beta-lactamase. http://purl.obolibrary.org/obo/ARO_3004757 BKC-1 http://purl.obolibrary.org/obo/ARO_3004756 BKC Beta-lactamase BKC-1 is a beta-lactamase conferring resistance to carbapenem and is found in Brazilian Klebsiella. http://purl.obolibrary.org/obo/ARO_3004758 BPU Beta-lactamase http://purl.obolibrary.org/obo/ARO_3000075 class D beta-lactamase BPU is a class D beta lactamase gene family. http://purl.obolibrary.org/obo/ARO_3004759 BPU-1 http://purl.obolibrary.org/obo/ARO_3004758 BPU Beta-lactamase BPU-1 is a class D beta-lactamase found in Bacillus pumilus. http://purl.obolibrary.org/obo/ARO_3004760 BRO Beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase BRO is a class A beta-lactamase that is found in M.catarrhalis. http://purl.obolibrary.org/obo/ARO_3004761 BRO-1 http://purl.obolibrary.org/obo/ARO_3004760 BRO Beta-lactamase BRO-1 is a class A beta-lactamase found in M.catarrhalis. http://purl.obolibrary.org/obo/ARO_3004762 BRO-2 http://purl.obolibrary.org/obo/ARO_3004760 BRO Beta-lactamase BRO-2 is a class A beta-lactamase found in M.catarrhalis. http://purl.obolibrary.org/obo/ARO_3004763 CBP beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase CBP is a class A beta-lactamase family found in C. botulinum. http://purl.obolibrary.org/obo/ARO_3004764 CBP-1 http://purl.obolibrary.org/obo/ARO_3004763 CBP beta-lactamase CBP-1 is a class A beta-lactamase gene found in C. botulinum. http://purl.obolibrary.org/obo/ARO_3004765 CGA beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase CGA is a class A beta-lactamase family that is found in Chryseobacterium gleum. http://purl.obolibrary.org/obo/ARO_3004766 CGA-1 http://purl.obolibrary.org/obo/ARO_3004765 CGA beta-lactamase CGA-1 is a class A beta-lactamase gene found in Chryseobacterium gleum. http://purl.obolibrary.org/obo/ARO_3004767 CIA beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase CIA is a class A beta-lactamase gene family found in Chryseobacterium indologenes. http://purl.obolibrary.org/obo/ARO_3004768 CIA-1 http://purl.obolibrary.org/obo/ARO_3004767 CIA beta-lactamase CIA-1 is a class A beta-lactamase gene found in Chryseobacterium indologenes. http://purl.obolibrary.org/obo/ARO_3004769 CIA-2 http://purl.obolibrary.org/obo/ARO_3004767 CIA beta-lactamase CIA-2 is a class A beta-lactamase gene found in Chryseobacterium indologenes. http://purl.obolibrary.org/obo/ARO_3004770 CIA-3 http://purl.obolibrary.org/obo/ARO_3004767 CIA beta-lactamase CIA-3 is a class A beta-lactamase gene found in Chryseobacterium indologenes. http://purl.obolibrary.org/obo/ARO_3004771 CIA-4 http://purl.obolibrary.org/obo/ARO_3004767 CIA beta-lactamase CIA-4 is a class A beta-lactamase gene found in Chryseobacterium indologenes. http://purl.obolibrary.org/obo/ARO_3004772 CKO beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase CKO is a class A beta-lactamase gene family found in Citrobacter koseri. http://purl.obolibrary.org/obo/ARO_3004773 CKO-1 http://purl.obolibrary.org/obo/ARO_3004772 CKO beta-lactamase CKO-1 is a class A beta-lactamase gene found in Citrobacter koseri. http://purl.obolibrary.org/obo/ARO_3004774 CME beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase CME is a class A beta-lactamase gene family belonging to Chryseobacterium meningosepticum. http://purl.obolibrary.org/obo/ARO_3004775 CME-1 http://purl.obolibrary.org/obo/ARO_3004774 CME beta-lactamase CME-1 is a class A beta-lactamase gene belonging to Chryseobacterium meningosepticum. http://purl.obolibrary.org/obo/ARO_3004776 CMH beta-lactamase http://purl.obolibrary.org/obo/ARO_3000076 class C beta-lactamase CMH is a class C beta-lactamase gene family belonging to Enterobacter cloacae. http://purl.obolibrary.org/obo/ARO_3004777 CMH-1 http://purl.obolibrary.org/obo/ARO_3004776 CMH beta-lactamase CMH-1 is a class C beta-lactamase gene found in Enterobacter cloacae. http://purl.obolibrary.org/obo/ARO_3004778 CMY-135 http://purl.obolibrary.org/obo/ARO_3000069 CMY beta-lactamase CMY-135 is a class C beta-lactamase that confers resistance to cephamycin. http://purl.obolibrary.org/obo/ARO_3004779 DES beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase DES is a class A beta-lactamase gene family found in Desulfovibrio desulfuricans. http://purl.obolibrary.org/obo/ARO_3004780 DES-1 http://purl.obolibrary.org/obo/ARO_3004779 DES beta-lactamase DES-1 is a class A beta-lactamase gene found in Desulfovibrio desulfuricans. http://purl.obolibrary.org/obo/ARO_3004781 ERP beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase ERP is a class A beta-lactamase gene family found in Erwinia persicina. http://purl.obolibrary.org/obo/ARO_3004782 ERP-1 http://purl.obolibrary.org/obo/ARO_3004781 ERP beta-lactamase ERP-1 is a class A beta-lactamase gene found in Erwinia persicina. http://purl.obolibrary.org/obo/ARO_3004783 FAR beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase FAR is a class A extended spectrum beta-lactamase gene family found in Nocardia farcinica. http://purl.obolibrary.org/obo/ARO_3004784 FAR-1 http://purl.obolibrary.org/obo/ARO_3004783 FAR beta-lactamase FAR-1 is a class A beta-lactamase gene found in Nocardia farcinica. http://purl.obolibrary.org/obo/ARO_3004785 FIM beta-lactamase http://purl.obolibrary.org/obo/ARO_3000004 class B (metallo-) beta-lactamase FIM is a metallo-beta-lactamase gene family found in Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3004786 FIM-1 http://purl.obolibrary.org/obo/ARO_3004785 FIM beta-lactamase FIM-1 is a metallo-beta-lactamase gene found in Pseudomonas aeruginosa from isolates in Italy. http://purl.obolibrary.org/obo/ARO_3004787 FONA beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase FONA is a class A beta-lactamase gene family found in Serratia fonticola. http://purl.obolibrary.org/obo/ARO_3004788 FONA-1 http://purl.obolibrary.org/obo/ARO_3004787 FONA beta-lactamase FONA-1 is a class A beta-lactamase gene found in Serratia fonticola. http://purl.obolibrary.org/obo/ARO_3004789 FONA-2 http://purl.obolibrary.org/obo/ARO_3004787 FONA beta-lactamase FONA-2 is a class A beta-lactamase gene found in Serratia fonticola. http://purl.obolibrary.org/obo/ARO_3004790 FONA-3 http://purl.obolibrary.org/obo/ARO_3004787 FONA beta-lactamase FONA-3 is a class A beta-lactamase gene found in Serratia fonticola. http://purl.obolibrary.org/obo/ARO_3004791 FONA-4 http://purl.obolibrary.org/obo/ARO_3004787 FONA beta-lactamase FONA-4 is a class A beta-lactamase gene found in Serratia fonticola. http://purl.obolibrary.org/obo/ARO_3004792 FONA-5 http://purl.obolibrary.org/obo/ARO_3004787 FONA beta-lactamase FONA-5 is a class A beta-lactamase gene found in Serratia fonticola. http://purl.obolibrary.org/obo/ARO_3004793 FONA-6 http://purl.obolibrary.org/obo/ARO_3004787 FONA beta-lactamase FONA-6 is a class A beta-lactamase gene found in Serratia fonticola. http://purl.obolibrary.org/obo/ARO_3004794 FPH beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase FPH is a carbapenem-hydrolyzing class A beta-lactamase found in Francisella philomiragia. http://purl.obolibrary.org/obo/ARO_3004795 FPH-1 http://purl.obolibrary.org/obo/ARO_3004794 FPH beta-lactamase FPH-1 is a carbapenem-hydrolyzing class A beta-lactamase gene found in Francisella philomiragia. http://purl.obolibrary.org/obo/ARO_3004796 FRI beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase FRI is a carbapenem-Hydrolyzing Class A beta-Lactamase from Enterobacter cloacae. http://purl.obolibrary.org/obo/ARO_3004797 FRI-1 http://purl.obolibrary.org/obo/ARO_3004796 FRI beta-lactamase FRI-1 is a carbapenem-hydrolyzing Class A beta-lactamase found in Enterobacter cloacae. http://purl.obolibrary.org/obo/ARO_3004798 FRI-2 http://purl.obolibrary.org/obo/ARO_3004796 FRI beta-lactamase FRI-2 is a carbapenem-hydrolyzing Class A beta-lactamase gene found in Enterobacter asburiae. http://purl.obolibrary.org/obo/ARO_3004799 FRI-3 http://purl.obolibrary.org/obo/ARO_3004796 FRI beta-lactamase FRI-3 is a carbapenem-hydrolyzing Class A beta-lactamase gene found in Enterobacter cloacae. http://purl.obolibrary.org/obo/ARO_3004800 FTU beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase FTU is a class A beta-lactamase gene family found in Francisella tularensis. http://purl.obolibrary.org/obo/ARO_3004801 FTU-1 http://purl.obolibrary.org/obo/ARO_3004800 FTU beta-lactamase FTU-1 is a class A beta-lactamase gene found in Francisella tularensis. It causes Tularemia. http://purl.obolibrary.org/obo/ARO_3004802 GOB-10 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-10 is a class B beta-lactamase gene found in Chryseobacterium meningosepticum. http://purl.obolibrary.org/obo/ARO_3004803 GOB-11 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-11 is a class B beta-lactamase gene found in Chryseobacterium meningosepticum. http://purl.obolibrary.org/obo/ARO_3004804 GOB-12 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-12 is a class B beta-lactamase gene found in Elizabethkingia meningoseptica. http://purl.obolibrary.org/obo/ARO_3004805 GOB-13 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-13 is a class B beta-lactamase gene found in Elizabethkingia meningoseptica. http://purl.obolibrary.org/obo/ARO_3004806 GOB-14 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-14 is a class B beta-lactamase gene found in Elizabethkingia meningoseptica. http://purl.obolibrary.org/obo/ARO_3004807 GOB-15 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-15 is a class B beta-lactamase gene found in Elizabethkingia meningoseptica. http://purl.obolibrary.org/obo/ARO_3004808 GOB-16 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-16 is a class B beta-lactamase gene found in Elizabethkingia meningoseptica. http://purl.obolibrary.org/obo/ARO_3004809 GOB-2 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-2 is class B beta-lactamase gene found in Elizabethkingia meningoseptica. http://purl.obolibrary.org/obo/ARO_3004810 GOB-3 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-3 is a class B beta-lactamase gene found in Elizabethkingia meningoseptica. http://purl.obolibrary.org/obo/ARO_3004811 GOB-4 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-4 is a class B beta-lactamase gene found in Elizabethkingia meningoseptica. http://purl.obolibrary.org/obo/ARO_3004812 GOB-5 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-5 is a class B beta-lactamase gene found in Elizabethkingia meningoseptica. http://purl.obolibrary.org/obo/ARO_3004813 GOB-6 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-6 is a class B beta-lactamase gene found in Elizabethkingia meningoseptica. http://purl.obolibrary.org/obo/ARO_3004814 GOB-7 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-7 is a class B beta-lactamase gene found in Elizabethkingia meningoseptica. http://purl.obolibrary.org/obo/ARO_3004815 GOB-8 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-8 is a class B beta-lactamase gene found in Elizabethkingia meningoseptica. http://purl.obolibrary.org/obo/ARO_3004816 GOB-9 http://purl.obolibrary.org/obo/ARO_3004212 GOB beta-lactamase GOB-9 is a class B beta-lactamase gene found in Elizabethkingia meningoseptica. http://purl.obolibrary.org/obo/ARO_3004476 vmlR http://purl.obolibrary.org/obo/ARO_3007068 Miscellaneous ABC-F subfamily ATP-binding cassette ribosomal protection proteins vmlR is an ABC-F ATPase ribosomal protection protein identified in Bacillus subtilus. Shown to confer resistance to lincomycin and streptogramin A virginiamycin. Described by Crowe-McAuliffe et al. 2018. http://purl.obolibrary.org/obo/ARO_3004477 eremomycin pyrrolidide http://purl.obolibrary.org/obo/ARO_3000081 glycopeptide antibiotic Eremomycin pyrrolidide 3, 4, 5, and 6 are semisynthetic glycopeptide derived from vancomycin or eremomycin. There have high activity against staphylococci and enterococci, including vancomycin-resistant strains. http://purl.obolibrary.org/obo/ARO_3004478 OXA-665 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase Beta-lactamase found in Acinetobacter rudis efficiently inactivating carbapenems and amoxicillin conferring resistance to cephalosporins. http://purl.obolibrary.org/obo/ARO_3004479 OXA-664 http://purl.obolibrary.org/obo/ARO_3000017 OXA beta-lactamase Beta-lactamase found in Acinetobacter spp. efficiently inactivating carbapenems and amoxicillin conferring resistance to cephalosporins. http://purl.obolibrary.org/obo/ARO_3004480 Bifidobacterium adolescentis rpoB mutants conferring resistance to rifampicin http://purl.obolibrary.org/obo/ARO_3000210 rifamycin-resistant beta-subunit of RNA polymerase (rpoB) Bifidobacterium are antibiotic resistant probiotics are prescribed to upkeep the population beneficial bacteria in the gut microbiome. However, horizontal gene transfer among gut microbes could create harmful antibiotic-resistant pathogenic bacteria, such as Mycobacterium tuberculosis. Lokesh et al. analyzed Bifidobacterium antitubercular drug resistance and mutations in rpoB. They found that B. animalis, B. longum and B. adolescentis showed considerable resistance to pyrazinamide, isoniazid, and streptomycin, while B. adolescentis had mutations both in the rifampicin (RIF) pocket and in regions outside the pockets, and also showed considerable resistance to RIF. http://purl.obolibrary.org/obo/ARO_3004489 OXA-663 http://purl.obolibrary.org/obo/ARO_3007697 OXA-10-like beta-lactamase An OXA-10 family class beta-lactamase identified from a Klebsiella pneumoniae BIDMC 35 isolate. http://purl.obolibrary.org/obo/ARO_3004490 delamanid http://purl.obolibrary.org/obo/ARO_3004115 nitroimidazole antibiotic A novel nitroimidazole antibiotic for treating Mycobacterium tuberculosis infection. Delamanid inhibits bacterial cell wall growth by mycolic acid synthesis disruption and is particularly effective in combination therapies against multidrug-resistant tuberculosis. http://purl.obolibrary.org/obo/ARO_3004491 diarylquinoline antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule A class of antibiotics used to treat specifically Mycobacterium tuberculosis infection; therefore, referred to as an antimycobacterial. Diarylquinoline antibiotics inhibit ATP synthesis in tuberculosis cells by disruption of mycobacterial ATP synthase. http://purl.obolibrary.org/obo/ARO_3004492 bedaquiline http://purl.obolibrary.org/obo/ARO_3004491 diarylquinoline antibiotic A diarylquinoline antibiotic drug sold under the brand name Sirturo, used to treat infection from Mycobacterium spp., particularly multidrug-resistant tuberculosis. Bedaquiline disrupts ATP synthase by proton pump blockage, inhibiting ATP synthesis. http://purl.obolibrary.org/obo/ARO_3004493 ADC-68 http://purl.obolibrary.org/obo/ARO_3004545 ADC beta-lactamase with carbapenemase activity A class C carbapenemase and extended-spectrum beta-lactamase identified from Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3004494 IMP-55 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase An IMP class B metallo-beta-lactamase enzyme identified from Acinetobacter baumannii. http://purl.obolibrary.org/obo/ARO_3004495 IMP-56 http://purl.obolibrary.org/obo/ARO_3000020 IMP beta-lactamase An IMP class B metallo-beta-lactamase enzyme identified from carbapenem-resistant Pseudomonas aeruginosa. http://purl.obolibrary.org/obo/ARO_3004496 KPC-24 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase A KPC class A beta-lactamase and carbapenemase identified from Chilean isolates of Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3004498 dfrB4 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr A trimethoprim-resistant dihydrofolate reductase characterized on a class I integron from an E. coli isolate. http://purl.obolibrary.org/obo/ARO_3004499 Tosufloxacin http://purl.obolibrary.org/obo/ARO_0000001 fluoroquinolone antibiotic Tosufloxacin is a fluoroquinolone antibiotic with an extended spectrum of activity. http://purl.obolibrary.org/obo/ARO_3004500 MCR-3.11 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-3 phosphoethanolamine transferase and polymyxin resistance gene variant differing by 2 amino acid substitutions, identified from an Escherichia coli isolate. http://purl.obolibrary.org/obo/ARO_3004501 MCR-6.1 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-2 phosphoethanolamine transferase and polymyxin resistance gene variant identified in Moraxella isolated from pigs in the United Kingdom. http://purl.obolibrary.org/obo/ARO_3004502 MCR-2.2 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-2 phosphoethanolamine transferase and polymyxin resistance gene variant identified in Moraxella isolated from pigs in Great Britain. http://purl.obolibrary.org/obo/ARO_3004503 MCR-3.6 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-3 phosphoethanolamine transferase and polymyxin resistance gene variant identified in Aeromonas. http://purl.obolibrary.org/obo/ARO_3004504 MCR-3.10 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-3 phosphoethanolamine transferase and polymyxin (colistin) resistance gene variant identified from Aeromonas, Proteus and Escherichia coli. http://purl.obolibrary.org/obo/ARO_3004505 MCR-3.5 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-3 phosphoethanolamine transferase and polymyxin (colistin) resistance gene variant identified from an extensively-resistant Escherichia coli clinical isolate. http://purl.obolibrary.org/obo/ARO_3004506 MCR-1.10 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-1 phosphoethanolamine transferase and polymyxin (colistin) resistance gene variant identified from an Escherichia porcine isolate in Great Britain. http://purl.obolibrary.org/obo/ARO_3004507 MCR-1.9 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-1 phosphoethanolamine transferase and polymyxin resistance gene variant identified from an enterotoxigenic Escherichia coli clinical isolate. http://purl.obolibrary.org/obo/ARO_3004508 MCR-3.9 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-3 polymyxin (incl. colistin) resistance gene variant isolated from an Aeromonas isolate. http://purl.obolibrary.org/obo/ARO_3004509 MCR-3.8 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-3 polymyxin (incl. colistin) resistance gene variant identified from an Aeromonas isolate. http://purl.obolibrary.org/obo/ARO_3004510 MCR-3.7 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR polymyxin (colistin) resistance gene variant identified in Aeromonas. http://purl.obolibrary.org/obo/ARO_3004511 MCR-3.2 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-3 polymyxin resistance gene variant identified in a colistin-resistant Salmonella isolate from Canada, located on an IncHI-2 plasmid. http://purl.obolibrary.org/obo/ARO_3004513 MCR-1.6 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-1 polymyxin resistance gene variant identified from colistin-resistant Salmonella enterica (serovar typhimurium) isolate, carried by an IncP plasmid. http://purl.obolibrary.org/obo/ARO_3004514 MCR-1.3 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-1 polymyxin resistance gene variant identified from a poultry Raoultella planticola isolate. http://purl.obolibrary.org/obo/ARO_3004515 MCR-1.4 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-1 polymyxin resistance gene variant identified from a colistin-resistant Escherichia coli isolate. http://purl.obolibrary.org/obo/ARO_3004516 MCR-8.1 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase A novel phosphoethanolamine transferase and mobile colistin resistance gene identified from carbapenem-resistant NDM-1-producing Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3004517 MCR-7.1 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase A novel plasmid-mediated colistin-resistant phosphoethanolamine transferase identified from a poultry isolate of Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3004519 MIC sign http://purl.obolibrary.org/obo/ARO_3004439 component of AMR phenotype measurement MIC sign (>, <, =) of the MIC value. http://purl.obolibrary.org/obo/ARO_3004520 > http://purl.obolibrary.org/obo/ARO_3004519 MIC sign Greater than MIC value. http://purl.obolibrary.org/obo/ARO_3004521 < http://purl.obolibrary.org/obo/ARO_3004519 MIC sign Less than MIC value. http://purl.obolibrary.org/obo/ARO_3004522 = http://purl.obolibrary.org/obo/ARO_3004519 MIC sign Equal to MIC value. http://purl.obolibrary.org/obo/ARO_3004523 MIC range http://purl.obolibrary.org/obo/ARO_3004519 MIC sign MIC is a range of two MIC values (e.g., given 10 clinical isolates with a resistance determinant, there are 5 that have an MIC of 25ug/mL and 5 that have an MIC of 100ug/mL agaisnt tobramycin). http://purl.obolibrary.org/obo/ARO_3004524 strain type http://purl.obolibrary.org/obo/ARO_3004389 reagent or protocol used for testing AMR Strain type used for antibiotic susceptibility testing. http://purl.obolibrary.org/obo/ARO_3004525 resistance determinant in strain http://purl.obolibrary.org/obo/ARO_3004524 strain type Resistant determinant is identified in strain without any experimental methods. http://purl.obolibrary.org/obo/ARO_3004526 deletion of resistance determinant http://purl.obolibrary.org/obo/ARO_3004524 strain type Experimental deletion of resistance determinant in the chromosome of the strain initially with this resistance determinant. http://purl.obolibrary.org/obo/ARO_3004527 deletion of resistance determinant with plasmid harbouring resistance determinant http://purl.obolibrary.org/obo/ARO_3004524 strain type Experimental protocol where there is a deletion of resistance determinant and the transformation of a plasmid harbouring resistance determinant into the same strain. http://purl.obolibrary.org/obo/ARO_3004528 plasmid harbouring resistance determinant http://purl.obolibrary.org/obo/ARO_3004524 strain type Experimental procedure where plasmid harbouring a resistance determinant is transformed into a strain. http://purl.obolibrary.org/obo/ARO_3004529 resistance determinant not in strain http://purl.obolibrary.org/obo/ARO_3004524 strain type Without any experimental protocol, the resistance determinant is absent from the strain. http://purl.obolibrary.org/obo/ARO_3004530 insertion of resistance determinant http://purl.obolibrary.org/obo/ARO_3004524 strain type Experimental insertion of resistance determinant in the chromosome of the strain initially without this resistance determinant. http://purl.obolibrary.org/obo/ARO_3004531 strain http://purl.obolibrary.org/obo/ARO_3004389 reagent or protocol used for testing AMR Specific strain of bacteria that was used to perform the antibiotic susceptibility test. http://purl.obolibrary.org/obo/ARO_3004532 strain source http://purl.obolibrary.org/obo/ARO_3004389 reagent or protocol used for testing AMR Source of the strain used in the antibiotic susceptibility test (e.g., clinical, environmental, agriculture). http://purl.obolibrary.org/obo/ARO_3004533 clinical source http://purl.obolibrary.org/obo/ARO_3004532 strain source Strain isolated in a clinical setting (e.g., from a patient). http://purl.obolibrary.org/obo/ARO_3004534 environmental source http://purl.obolibrary.org/obo/ARO_3004532 strain source Strain collected from environment (e.g., soil, water). http://purl.obolibrary.org/obo/ARO_3004535 agricultural source http://purl.obolibrary.org/obo/ARO_3004532 strain source Strain collected from agricultural setting (e.g., chicken, pig). http://purl.obolibrary.org/obo/ARO_3004536 antimicrobial susceptibility test control http://purl.obolibrary.org/obo/ARO_3004389 reagent or protocol used for testing AMR The control of the antibiotic susceptibility testing, whether there was an experimental control (same strain, with and without resistance determinant) or if there was a group of clinical isolates found to have a resistance determinant compared against a strain without that resistance determinant. http://purl.obolibrary.org/obo/ARO_3004537 experimental control http://purl.obolibrary.org/obo/ARO_3004536 antimicrobial susceptibility test control Antimicrobial susceptibility testing was performed on the same strain with and without a resistance determinant. http://purl.obolibrary.org/obo/ARO_3004538 correlative control http://purl.obolibrary.org/obo/ARO_3004536 antimicrobial susceptibility test control Antibiotic susceptibility testing is performed on a group of clinical isolates with a resistance determinant compared to different strains that do not have this resistance determinant. No experiment was performed to delete / insert the resistance determinant to determine antibiotic susceptibility using the same genetic background. http://purl.obolibrary.org/obo/ARO_3004539 mphH http://purl.obolibrary.org/obo/ARO_3000333 macrolide phosphotransferase (MPH) A chromosomal macrolide 2'-phosphotransferase and resistance gene identified from a Brachybacterium faecium cave isolate. http://purl.obolibrary.org/obo/ARO_3004540 experimental source http://purl.obolibrary.org/obo/ARO_3004532 strain source Source is an experimental, commonly used lab strain (e.g., P. aeruginosa PAO1). http://purl.obolibrary.org/obo/ARO_3004541 mphK http://purl.obolibrary.org/obo/ARO_3000333 macrolide phosphotransferase (MPH) A chromosomal macrolide phosphotransferase identified from Bacillus subtilis. http://purl.obolibrary.org/obo/ARO_3004542 mphN http://purl.obolibrary.org/obo/ARO_3000333 macrolide phosphotransferase (MPH) A macrolide phosphotransferase identified on a plasmid in Exiguobacterium. http://purl.obolibrary.org/obo/ARO_3004543 mphO http://purl.obolibrary.org/obo/ARO_3000333 macrolide phosphotransferase (MPH) A chromosomal macrolide phosphostransferase identified in Brachybacterium paraconglomeratum. http://purl.obolibrary.org/obo/ARO_3004544 mphJ http://purl.obolibrary.org/obo/ARO_3000333 macrolide phosphotransferase (MPH) A chromosomal macrolide phosphotransferase identified in Brevibacillus brevis VM4. http://purl.obolibrary.org/obo/ARO_3004545 ADC beta-lactamase with carbapenemase activity http://purl.obolibrary.org/obo/ARO_3005459 ADC beta-lactamase ADC beta-lactamase enzymes with demonstrable carbapenemase activity, an exception amongst these enzymes. http://purl.obolibrary.org/obo/ARO_3004546 Campylobacter jejuni 23S rRNA with mutation conferring resistance to erythromycin http://purl.obolibrary.org/obo/ARO_3004125 23S rRNA with mutation conferring resistance to macrolide antibiotics Point mutations in the 23S ribosomal RNA domain of Campylobacter jejuni which confer resistance to macrolide antibiotics, including erythromycin. http://purl.obolibrary.org/obo/NCIT_85595 disk-diffusion method http://purl.obolibrary.org/obo/ARO_3004391 diffusion method A method to determine microbial susceptibility to antibiotics wherein bacteria are inoculated onto agar plates and the antimicrobial agent diffused onto the agar plate from a filter paper disk. An approximate, but not exact, MIC is determined by the diameter of growth inhibition zones. This method has been found to have good correlation between in-vivo data and in-vitro data. http://purl.obolibrary.org/obo/NCIT_85596 antimicrobial gradient method (E-test) http://purl.obolibrary.org/obo/ARO_3004391 diffusion method A method to determine microbial susceptibility to antibiotics in which a plastic strip impregnated with the antibiotic of interest is placed on an agar plate that has been inoculated with bacteria. The antibiotic diffuses from the strip producing a concentration gradient of drug on the agar. The point at which the elliptical shaped area of growth inhibition meets the strip is the minimum inhibitory concentration of the drug of interest. http://purl.obolibrary.org/obo/NCIT_85701 macro broth dilution method http://purl.obolibrary.org/obo/ARO_3004397 broth dilution method A method to determine the minimum inhibitory concentration (MIC) of antibiotics in which growth media is pipetted into a multi-well plate. Each well contains a known concentration of drug which is inoculated with a known quantity of bacteria. The plate is incubated for a specified period of time and each well is assessed for bacterial cell growth. The drug concentration in the first well showing no growth is known as the MIC for that antibiotic. Minimum 2 mL total broth dilution volume. http://purl.obolibrary.org/obo/ARO_3007474 contezolid http://purl.obolibrary.org/obo/ARO_3000079 oxazolidinone antibiotic Contezolid is an oxazolidinone antimicrobial agent newly approved for treatment of multidrug-resistant (MDR) Gram-positive bacterial infections, including methicillin-resistant Staphylococcus aureus (MRSA) and vancomycin-resistant enterococci. http://purl.obolibrary.org/obo/ARO_3007475 cefcapene http://purl.obolibrary.org/obo/ARO_3009107 third-generation cephalosporin Cefcapene is a third-generation cephalosporin in the beta-lactam class of antibiotics used to manage and treat gram-negative and gram-positive bacterial infections. http://purl.obolibrary.org/obo/ARO_3007476 Mycobacterium abscessus atpE with mutation conferring resistance to bedaquiline http://purl.obolibrary.org/obo/ARO_3007477 antibiotic resistant ATP synthase Mutations to the ATPase subunit C atpE gene, which is involved with the production of ATP, confer resistance to bedaquiline by altering the antibiotic's target. http://purl.obolibrary.org/obo/ARO_3007477 antibiotic resistant ATP synthase http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant ATP synthase enzymes, specifically subunit C, resistant to diarylquinolone antibiotics including Bedaquiline. Mutations in ATP synthase confer antibiotic resistance by disrupting binding and blocking of ATP synthase reactions by Bedaquiline. http://purl.obolibrary.org/obo/ARO_3007478 darobactin A http://purl.obolibrary.org/obo/ARO_3000053 peptide antibiotic Darobactin A, isolated from Photorhabdus bacteria, contains a macrocyclic peptide-based ring system and exhibits selective antibiotic activity against Gram-negative pathogens in both in vitro and animal infection models and functions. http://purl.obolibrary.org/obo/ARO_3007479 caprazamycin http://purl.obolibrary.org/obo/ARO_3000034 nucleoside antibiotic Caprazamycin is a potent anti-mycobacterial liponucleoside antibiotics isolated from Streptomyces sp. http://purl.obolibrary.org/obo/ARO_3007480 TBI-223 http://purl.obolibrary.org/obo/ARO_3000079 oxazolidinone antibiotic TBI-223 is a novel oxazolidinone with potentially reduced myelosuppression, compared to linezolid. TBI-223 may be considered an additional treatment against MRSA infections and potentially other Gram-positive bacteria in humans. http://purl.obolibrary.org/obo/ARO_3007481 pseudouridimycin http://purl.obolibrary.org/obo/ARO_3000034 nucleoside antibiotic Pseudouridimycin is a nucleoside analogue inhibitor discovered from the soil bacterium Streptomyces sp. which has proven to be effective against multidrug-resistant S. pyogenes. http://purl.obolibrary.org/obo/ARO_3007482 RAD beta-lactamase http://purl.obolibrary.org/obo/ARO_3000075 class D beta-lactamase RAD beta-lactamases are a class D beta-lactamase first identified in Riemerella anatipestifer. http://purl.obolibrary.org/obo/ARO_3007483 RAD-1 http://purl.obolibrary.org/obo/ARO_3007482 RAD beta-lactamase RAD-1 is a class D RAD beta-lactamase found in Riemerella anatipestifer. http://purl.obolibrary.org/obo/ARO_3007484 monensin http://purl.obolibrary.org/obo/ARO_3005163 ionophore with antibiotic activity Monensin is an ionophore antibiotic isolated from Streptomyces cinnamonensis with very strong antibacterial and antiparasitic effects. http://purl.obolibrary.org/obo/ARO_3007485 nigericin http://purl.obolibrary.org/obo/ARO_3005163 ionophore with antibiotic activity Nigericin is an antibiotic derived from Streptomyces hygroscopicus. It is described as a potassium ionophore, which facilitates H+/K+ anti-port across cell membranes, thereby activating NLRP3 by causing potassium efflux. http://purl.obolibrary.org/obo/ARO_3007486 wychimicin http://purl.obolibrary.org/obo/ARO_3005171 polyketide with antibiotic activity Wychimicins are spirotetronates with activity against methicillin-resistant Staphylococcus aureus. http://purl.obolibrary.org/obo/ARO_3007487 wychimicin A http://purl.obolibrary.org/obo/ARO_3007486 wychimicin Wychimicin A is a spirotetronate polyketides from Actinocrispum wychmicini MI503-A4. http://purl.obolibrary.org/obo/ARO_3007488 wychimicin C http://purl.obolibrary.org/obo/ARO_3007486 wychimicin Wychimicin C is a spirotetronate polyketides from Actinocrispum wychmicini MI503-A4. http://purl.obolibrary.org/obo/ARO_3007489 dfrB10 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr A dihydrofolate reductase and trimethoprim resistance gene found on a mega-plasmid (0.4 Mb) from a Pseudomonas putida strain. http://purl.obolibrary.org/obo/ARO_3007490 dfrB11 http://purl.obolibrary.org/obo/ARO_3001218 trimethoprim resistant dihydrofolate reductase dfr A dihydrofolate reductase and trimethoprim resistance gene found in a groundwater sample at the Horonobe Underground Research laboratory in Japan in 2017, in a Betaproteobacteria sequence. http://purl.obolibrary.org/obo/ARO_3007491 Pseudomonas aeruginosa ampR with mutation conferring resistance to aztreonam http://purl.obolibrary.org/obo/ARO_3007797 ampR transcriptional regulator with mutation conferring resistance to monobactam antibiotics ampR is a regulatory gene that plays an essential role in regulating antibiotic resistance in P. aeruginosa. Mutation in ampR leads to its loss of control over blaPDC-16, allowing overexpression of blaPDC-16 and further resistance to aztreonam. http://purl.obolibrary.org/obo/ARO_3007492 tet(62) http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump A novel tetA-type efflux pump. http://purl.obolibrary.org/obo/ARO_3007493 tet(63) http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump A tetracycline efflux MFS Transporter from Staphylococcus aureus. http://purl.obolibrary.org/obo/ARO_3007494 tet(64) http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump A tetracycline efflux MFS Transporter from Burkholderia ubonensis. http://purl.obolibrary.org/obo/ARO_3007495 azole antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule Azoles are a group of antibiotics, particularly antifungals, that target the cytochrome P450 enzyme sterol 14alpha-demethylase, which converts lanosterol to ergosterol. They are typically fungistatic in yeasts and fungicidal in molds. The two main groups of azoles are imidazoles and triazoles. http://purl.obolibrary.org/obo/ARO_3007496 echinocandin antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule Echinocandins are a group of antibiotics, particularly antifungals, that target the target glucan synthase, an enzyme involved in the cell wall biosynthesis of fungi. They typically induce adaptive mechanisms that promote resistance such as heat shock protein 90, cell wall integrity pathway, high osmolarity glycerol pathway, and chitin biosynthesis. The three main echinocandins are caspofungin, micafungin and anidulafungin. http://purl.obolibrary.org/obo/ARO_3007497 polyene antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule Polyenes are a group of antibiotics, particularly antifungals, that bind ergosterol, a fungal-specific sterol in the plasma membrane of fungi, causing the efflux of potassium and cell death. They were discovered in the 1930s by Richard Kuhn. They are primarily used for therapy for invasive fungal infections like invasive aspergillosis, cryptococcosis blastomycosis, etc. The two main polyenes are amphotericin B and nystatin. http://purl.obolibrary.org/obo/ARO_3007498 allylamine antibiotic http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule Allylamines are a group of antibiotics, particularly antifungals, that act as squalene epoxidase and ergosterol inhibitors. They have broad-spectrum activity against pathogenic fungi, especially dermatophytes. The two main allylamines are naftifine and terbinafine. http://purl.obolibrary.org/obo/ARO_3007499 triazole antibiotic http://purl.obolibrary.org/obo/ARO_3007495 azole antibiotic Triazoles are a group of antibiotics, particularly antifungals, derived from azoles. Triazoles include fluconazole, itraconazole, voriconazole, posaconazole, and isavuconazole. http://purl.obolibrary.org/obo/ARO_3007500 imidazole antibiotic http://purl.obolibrary.org/obo/ARO_3007495 azole antibiotic Imidazoles are a group of antibiotics, particularly antifungals, derived from azoles. Imidazoles include imidazole derivatives clotrimazole, ketoconazole, miconazole, econazole and oxiconazole. http://purl.obolibrary.org/obo/ARO_3007501 caspofungin http://purl.obolibrary.org/obo/ARO_3007496 echinocandin antibiotic Caspofungin is an antibiotic, particularly antifungal, derived from echinocandins. It has a wide range of activity against fungi and yeasts. http://purl.obolibrary.org/obo/ARO_3007502 micafungin http://purl.obolibrary.org/obo/ARO_3007496 echinocandin antibiotic Micafungin is an antibiotic, particularly antifungal, derived from echinocandins. It was discovered at Fujisawa Pharmaceutical Co., Ltd. It is active against most Candida species. http://purl.obolibrary.org/obo/ARO_3007503 anidulafungin http://purl.obolibrary.org/obo/ARO_3007496 echinocandin antibiotic Anidulafungin is an antibiotic, particularly antifungal, derived from echinocandins. It exhibits strong antifungal action against a variety of Candida spp. and Aspergillus spp., including those that are resistant to amphotericin B and triazole. http://purl.obolibrary.org/obo/ARO_3007504 amphotericin B http://purl.obolibrary.org/obo/ARO_3007497 polyene antibiotic Amphotericin B is an antibiotic, particularly antifungal, derived from polyene. It exhibits strong antifungal action against a variety of fungi species and is typically considered the gold standard of antifungals. http://purl.obolibrary.org/obo/ARO_3007505 nystatin http://purl.obolibrary.org/obo/ARO_3007497 polyene antibiotic Nystatin is an antibiotic, particularly antifungal, derived from polyene. Nystatin is fungistatic in vitro against Candida albicans and certain other yeast-like fungi. http://purl.obolibrary.org/obo/ARO_3007506 naftifine http://purl.obolibrary.org/obo/ARO_3007498 allylamine antibiotic Naftifine is an antibiotic, particularly antifungal, derived from Allylamine. It was discovered in 19742 at the Sandoz Research Institute in Vienna, Austria. Naftifine is fungicidal against a broad spectrum of dermatophyte fungi and provides good against Candida and Aspergillus species. http://purl.obolibrary.org/obo/ARO_3007507 terbinafine http://purl.obolibrary.org/obo/ARO_3007498 allylamine antibiotic Terbinafine is an antibiotic, particularly antifungal, derived from allylamine. Terbinafine is active against a broad range of fungi and yeast. It was discovered in 1983. http://purl.obolibrary.org/obo/ARO_3007508 fluconazole http://purl.obolibrary.org/obo/ARO_3007499 triazole antibiotic Fluconazole is a type of triazole antibiotic, particularly antifungal. It is used for the treatment of superficial and systemic fungal infections. http://purl.obolibrary.org/obo/ARO_3007509 Shigella flexneri acrA http://purl.obolibrary.org/obo/ARO_3000207 acrA AcrA is a subunit of the AcrAB multidrug efflux system found in Shigella flexneri, which is encoded by the acrRAB operon. http://purl.obolibrary.org/obo/ARO_3007511 itraconazole http://purl.obolibrary.org/obo/ARO_3007499 triazole antibiotic Itraconazole is a type of triazole antibiotic, particularly antifungal. It has broad spectrum activity against Candida and Malassezia species and Dermatophytes. http://purl.obolibrary.org/obo/ARO_3007512 voriconazole http://purl.obolibrary.org/obo/ARO_3007499 triazole antibiotic Voriconazole is a type of triazole antibiotic, particularly antifungal. It is used for the treatment of invasive aspergillosis, candidaemia, and infections caused by Candida spp. http://purl.obolibrary.org/obo/ARO_3007513 posaconazole http://purl.obolibrary.org/obo/ARO_3007499 triazole antibiotic Posaconazole is a type of triazole antibiotic, particularly antifungal. It has broad spectrum activity against Candida albicans and Aspergillus fumigatus. http://purl.obolibrary.org/obo/ARO_3007514 isavuconazole http://purl.obolibrary.org/obo/ARO_3007499 triazole antibiotic Isavuconazole is a type of triazole antibiotic, particularly antifungal. It has activity against yeasts, dimorphic fungi, and molds. http://purl.obolibrary.org/obo/ARO_3007515 ANT(9)-Ic http://purl.obolibrary.org/obo/ARO_3007400 ANT(9)-I ANT(9)-Ic encodes an intrinsic, chromosomal aminoglycoside nucleotidyltransferase in Brucella intermedia. http://purl.obolibrary.org/obo/ARO_3007516 clotrimazole http://purl.obolibrary.org/obo/ARO_3007500 imidazole antibiotic Clotrimazole is a type of imidazole antibiotic, particularly antifungal. It is mostly used for the treatment of tinea pedis, vulvovaginal and oropharyngeal candidiasis. It has broad activity against Candida albicans and other fungal infections. http://purl.obolibrary.org/obo/ARO_3007517 ketoconazole http://purl.obolibrary.org/obo/ARO_3007500 imidazole antibiotic Ketoconazole is a type of imidazole antibiotic, particularly antifungal. It was one of the first available oral broad-spectrum antifungals for the treatment of systemic and superficial mycoses. http://purl.obolibrary.org/obo/ARO_3007518 miconazole http://purl.obolibrary.org/obo/ARO_3007500 imidazole antibiotic Miconazole is a type of imidazole antibiotic, particularly antifungal. It is used to treat oral and vaginal yeast infections, as well as mucosal thrush. http://purl.obolibrary.org/obo/ARO_3007519 econazole http://purl.obolibrary.org/obo/ARO_3007500 imidazole antibiotic Econazole is a type of imidazole antibiotic, particularly antifungal. It is often used to treat tinea cruris, tinea pedis, and tinea corporis. http://purl.obolibrary.org/obo/ARO_3007520 oxiconazole http://purl.obolibrary.org/obo/ARO_3007500 imidazole antibiotic Oxiconazole is a type of imidazole antibiotic, particularly antifungal. It is primarily used to treat tinea pedis, tinea cruris, tinea corporis, and tinea versicolor. http://purl.obolibrary.org/obo/ARO_3007521 flumequine http://purl.obolibrary.org/obo/ARO_0000001 fluoroquinolone antibiotic Flumequine is a first generation fluoroquinolone antibiotic. It is used primarily for the treatment of enteric infections in domestic species. It has been removed from clinical use and is no longer being marketed. http://purl.obolibrary.org/obo/ARO_3007522 antifungal-resistant cytochrome P450 enzyme http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Fungal cytochrome P450 enzymes which include mutations or other modifications to confer resistance to antifungal drug compounds. http://purl.obolibrary.org/obo/ARO_3007523 triazole-resistant fungal cytochrome P450 enzyme http://purl.obolibrary.org/obo/ARO_3007522 antifungal-resistant cytochrome P450 enzyme Fungal cytochrome P450 enzymes which include mutations to confer resistance to triazole-class antibiotics. http://purl.obolibrary.org/obo/ARO_3007524 Candida spp. ERG11 with mutations conferring resistance to azole antibiotics http://purl.obolibrary.org/obo/ARO_3007523 triazole-resistant fungal cytochrome P450 enzyme ERG11 is a cytochrome P450 enzyme in Candida spp. Mutations in ERG11 have been shown to confer resistance to azole antibiotics including fluconazole and itraconazole. http://purl.obolibrary.org/obo/ARO_3007525 norvancomycin http://purl.obolibrary.org/obo/ARO_3000081 glycopeptide antibiotic Norvancomycin differs from vancomycin by a single methyl group and is typically used to treat methicillin-resistant Staphylococcus aureus (MRSA) ventriculitis in patients. http://purl.obolibrary.org/obo/ARO_3007526 spectinomycin resistant rpsE http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Amino acid substitutions in ribosomal protein S5, the product of the rpsE gene, is associated with resistance to spectinomycin (SpcR). This protein is located on the 30S subunit and interacts with 16S rRNA and other proteins. http://purl.obolibrary.org/obo/ARO_3007527 Bacillus subtilis rpsE mutations conferring resistance to spectinomycin http://purl.obolibrary.org/obo/ARO_3007526 spectinomycin resistant rpsE Amino acid substitutions in ribosomal protein S5, rpsE, is associated with resistance to spectinomycin (SpcR). http://purl.obolibrary.org/obo/ARO_3007528 gallic acid http://purl.obolibrary.org/obo/ARO_3007223 adjuvants enhancing antibiotic entry Gallic acid was found to enhance sulfonamides against multidrug-resistant S. suis. Gallic acid effectively disrupts the integrity and function of the cytoplasmic membrane by dissipating the proton motive force of bacteria. It regulates the expression of dihydrofolate reductase, which then inhibits tetrahydrofolate synthesis. As a result of polypharmacology, gallic acid can fully restore sulfadiazine sodium activity in the animal infection model without any drug resistances. http://purl.obolibrary.org/obo/ARO_3007529 pivmecillinam http://purl.obolibrary.org/obo/ARO_3009123 penicillin with extended spectrum Pivmecillinam, the oral prodrug of the antimicrobial active agent mecillinam, is a bona fide agent for uncomplicated lower urinary tract infections (UTIs), because of its selectivity and effect against several species of Enterobacteriaceae. http://purl.obolibrary.org/obo/ARO_3007530 Streptococcus pyogenes PBP2x with mutation conferring resistance to beta-lactam antibiotics http://purl.obolibrary.org/obo/ARO_3003938 Penicillin-binding protein mutations conferring resistance to beta-lactam antibiotics PBP2x is a penicillin-binding protein and beta-lactam resistance enzyme. Mutations can cause resistance to some beta-lactam antibiotics. http://purl.obolibrary.org/obo/ARO_3007531 Streptococcus pyogenes PBP2x conferring resistance to beta-lactam antibiotics http://purl.obolibrary.org/obo/ARO_3003938 Penicillin-binding protein mutations conferring resistance to beta-lactam antibiotics PBP2x is a penicillin-binding protein and beta-lactam resistance enzyme. Mutations can cause resistance to some beta-lactam antibiotics. http://purl.obolibrary.org/obo/ARO_3007532 proflavine http://purl.obolibrary.org/obo/ARO_3005386 disinfecting agents and antiseptics Proflavine, also called proflavin and diaminoacridine, is an acriflavine derivative, a disinfectant bacteriostatic against many gram-positive bacteria. http://purl.obolibrary.org/obo/ARO_3007533 MCR-4.7 http://purl.obolibrary.org/obo/ARO_3004268 MCR phosphoethanolamine transferase An MCR-4-type colistin resistance gene variant. http://purl.obolibrary.org/obo/ARO_3007534 arsinothricin http://purl.obolibrary.org/obo/ARO_3000551 organoarsenic antibiotic Arsinothricin is a natural product synthesized by the rhizosphere bacterium Burkholderia gladioli GSRB05 and is a broad-spectrum antibiotic effective against human pathogens such as carbapenem-resistant Enterobacter cloacae. It is a non-proteogenic amino acid and glutamate mimetic that inhibits bacterial glutamine synthetase. http://purl.obolibrary.org/obo/ARO_3007535 pretomanid http://purl.obolibrary.org/obo/ARO_3004115 nitroimidazole antibiotic Pretomanid is an antibiotic medication used for the treatment of multi-drug-resistant tuberculosis affecting the lungs. http://purl.obolibrary.org/obo/ARO_3007536 Mycobacterium tuberculosis 16S rRNA (rrnS) mutation conferring resistance to amikacin http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutation in M. tuberculosis rrnS conferring resistance to amikacin antibiotic. http://purl.obolibrary.org/obo/ARO_3007537 Mycobacterium tuberculosis 16S rRNA (rrnS) mutation conferring resistance to kanamycin http://purl.obolibrary.org/obo/ARO_3003666 16s rRNA with mutation conferring resistance to aminoglycoside antibiotics Point mutation in M. tuberculosis rrnS conferring resistance to kanamycin antibiotic. http://purl.obolibrary.org/obo/ARO_3007538 chenodeoxycholic acid http://purl.obolibrary.org/obo/ARO_3007223 adjuvants enhancing antibiotic entry A cholic acid derivative of the traditional Chinese medicine (TCM) Tanreqing (TRQ), synergizes with amikacin against Staphylococcus aureus in vitro, and this synergistic killing was effective against diverse methicillin-resistant S. aureus (MRSA) variants. Mechanistically, chenodeoxycholic acid increases the uptake of aminoglycosides in a proton motive force-dependent manner by dissipating the chemical potential and potentiates reactive oxygen species (ROS) generation by inhibiting superoxide dismutase activity. http://purl.obolibrary.org/obo/ARO_3007539 APH(9)-Ic http://purl.obolibrary.org/obo/ARO_3000153 APH(9) APH(9)-Ic is a chromosomal-encoded aminoglycoside phosphotransferase in S. maltophilia. http://purl.obolibrary.org/obo/ARO_3007540 cyclomarin antibiotics http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule Cyclomarins are cyclic heptapeptides containing four unusual amino acids. Cyclomarins target two different targets: Clp C1, a subunit of the caseinolytic protease of Mycobacterium tuberculosis (MTB), and PfAp3Ase of Plasmodium falciparum. Therefore, cyclomarins are interesting lead structures for the development of drugs against tuberculosis and malaria. http://purl.obolibrary.org/obo/ARO_3007541 cyclomarin A http://purl.obolibrary.org/obo/ARO_3007540 cyclomarin antibiotics Cyclomarin A was found to be bacteriocidal against bacteria replicating in culture broth and in human-derived macrophages and a series of multidrug resistant clinical isolates. It was identified as a potent antitubercular compound in a natural product whole cell screen. Importantly it kills both growing and dormant, non-replicating mycobacteria. http://purl.obolibrary.org/obo/ARO_3007542 cyclomarin B http://purl.obolibrary.org/obo/ARO_3007540 cyclomarin antibiotics Cyclomarin B is a cyclomarin antibiotic. http://purl.obolibrary.org/obo/ARO_3007543 cyclomarin C http://purl.obolibrary.org/obo/ARO_3007540 cyclomarin antibiotics Cyclomarin C is a cyclomarin antibiotic. http://purl.obolibrary.org/obo/ARO_3007544 Erysipelothrix rhusiopathiae gyrA with mutation conferring resistance to enrofloxacin http://purl.obolibrary.org/obo/ARO_3003292 fluoroquinolone resistant gyrA Sequence analysis of the gyrA gene showed that resistance of E. rhusiopathiae strains to enrofloxacin is due to a mutation at position 257. http://purl.obolibrary.org/obo/ARO_3007545 antifungal-resistant beta-1,3-D-glucan synthase http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Fungal beta-1,3-D-glucan synthase enzymes which include mutations to confer resistance to antifungal drug compounds. http://purl.obolibrary.org/obo/ARO_3007546 echinocandin antibiotic-resistant beta-1,3-D-glucan synthase http://purl.obolibrary.org/obo/ARO_3007545 antifungal-resistant beta-1,3-D-glucan synthase Fungal beta-1,3-D-glucan synthases which include mutations to confer resistance to echinocandin-class antibiotics. http://purl.obolibrary.org/obo/ARO_3007547 salinomycin http://purl.obolibrary.org/obo/ARO_3005163 ionophore with antibiotic activity Salinomycin is an antibacterial and coccidiostat ionophore therapeutic drug. http://purl.obolibrary.org/obo/ARO_3007548 Candida spp. FKS2 with mutations conferring resistance to echinocandin antibiotics http://purl.obolibrary.org/obo/ARO_3007546 echinocandin antibiotic-resistant beta-1,3-D-glucan synthase Glucan synthase FKS2 is involved in the production of the fungal cell wall by the synthesis of the core component beta-1,3-glucan in Candida spp. Mutations in FKS2 have been shown to confer resistance to echinocandin antibiotic micafungin. http://purl.obolibrary.org/obo/ARO_3007549 antibiotic resistant ergosterol biosynthesis pathway transcription factor http://purl.obolibrary.org/obo/ARO_3007610 gene modulating azole resistance Fungal sterol regulatory element binding proteins are transcription factors that modulate antibiotic-susceptible genes. Mutations in these proteins confer resistance to antifungal drug compounds through differential gene regulation. http://purl.obolibrary.org/obo/ARO_3007551 Candida spp. Upc2 with mutations conferring resistance to azole antibiotics http://purl.obolibrary.org/obo/ARO_3007549 antibiotic resistant ergosterol biosynthesis pathway transcription factor Upc2 is a sterol synthesis regulatory element binding protein in Candida spp. Mutations in Upc2 have been shown to confer resistance to azole antibiotics including fluconazole by upregulating ERG11 expression. http://purl.obolibrary.org/obo/ARO_3007552 pleiotropic drug resistance transcription factors http://purl.obolibrary.org/obo/ARO_3000451 protein(s) and two-component regulatory system modulating antibiotic efflux Pleiotropic Drug Resistance factors (PDR) are transcription factors in fungi that regulate the expression of genes encoding for efflux pumps causing multidrug resistance. http://purl.obolibrary.org/obo/ARO_3007553 Candida spp. CDR1 http://purl.obolibrary.org/obo/ARO_0010001 ATP-binding cassette (ABC) antibiotic efflux pump CDR1 is a pleiotropic drug resistance gene encoding ABC transporters that contributes to multidrug antifungal resistance in Candida spp. http://purl.obolibrary.org/obo/ARO_3007554 Candida spp. CDR2 http://purl.obolibrary.org/obo/ARO_0010001 ATP-binding cassette (ABC) antibiotic efflux pump CDR2 is a Pleiotropic drug resistance gene encoding ABC transporters that contributes to multidrug antifungal resistance in Candida spp. http://purl.obolibrary.org/obo/ARO_3007555 Zn2Cys6 transcription factors http://purl.obolibrary.org/obo/ARO_3000219 mutant efflux regulatory protein conferring antibiotic resistance Zn2Cys6 is a transcription factor family that includes mutations to confer resistance to azole-class antibiotics. http://purl.obolibrary.org/obo/ARO_3007556 fungal uracil phosphoribosyltransferase http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Fungal uracil phosphoribosyltransferases which include mutations to confer resistance to 5-flucytosine antibiotic. http://purl.obolibrary.org/obo/ARO_3007557 Candida spp. FUR1 with mutations conferring resistance to 5-flucytosine http://purl.obolibrary.org/obo/ARO_3007556 fungal uracil phosphoribosyltransferase FUR1 is a fungal uracil phosphoribosyltransferase in Candida spp. It encodes the UPRT protein, also known as uracil pyrophosphorylase, which is a key regulating enzyme in pyrimidine salvage. Mutations in FUR1 have been shown to confer resistance to 5-flucytosine. http://purl.obolibrary.org/obo/ARO_3007558 5-flucytosine http://purl.obolibrary.org/obo/ARO_3007560 pyrimidine antifungal drug 5-Flucytosine is an antibiotic, particularly antifungal. It inhibits fungal RNA and DNA synthesis by changing the amino-acylation of tRNA, causing the amino acid pool to be altered and protein synthesis to be inhibited. http://purl.obolibrary.org/obo/ARO_3007559 Saccharomyces spp. FUR1 with mutations conferring resistance to 5-flucytosine http://purl.obolibrary.org/obo/ARO_3007556 fungal uracil phosphoribosyltransferase FUR1 is a fungal uracil phosphoribosyltransferase in Saccharomyces spp. It encodes the UPRT protein, also known as uracil pyrophosphorylase, which is a key regulating enzyme in pyrimidine salvage. Mutations in FUR1 have been shown to confer resistance to 5-flucytosine. http://purl.obolibrary.org/obo/ARO_3007560 pyrimidine antifungal drug http://purl.obolibrary.org/obo/ARO_1000003 antibiotic molecule Any pyrimidine antifungal agent that has been used for the treatment of fungal infections in humans or animals. http://purl.obolibrary.org/obo/ARO_3007561 OXA-1038 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase The blaOXA-48-like enzyme demonstrated significant hydrolysis activity against meropenem, and the classical beta-lactamase inhibitor had no significant inhibitory effect. This is a novel OXA carbapenemases in S. xiamenensis. http://purl.obolibrary.org/obo/ARO_3007562 OXA-1039 http://purl.obolibrary.org/obo/ARO_3007721 OXA-48-like beta-lactamase The blaOXA-48-like enzyme demonstrated significant hydrolysis activity against meropenem, and the classical beta-lactamase inhibitor had no significant inhibitory effect. This is a novel OXA carbapenemases in S. xiamenensis. http://purl.obolibrary.org/obo/ARO_3007563 Candida spp. TAC1 with mutations conferring resistance to azole antibiotics http://purl.obolibrary.org/obo/ARO_3007555 Zn2Cys6 transcription factors TAC1 is a Zn2Cys6 transcription factor that transcriptionally activates efflux units CDR1 and CDR2. Mutations in TAC1 upregulate CDR1 and CDR2 causing increased resistance. http://purl.obolibrary.org/obo/ARO_3007564 pH-responsive transcription factors http://purl.obolibrary.org/obo/ARO_3000270 protein modulating permeability to antibiotic The pH-dependant transcription factors regulate the expression of antifungal resistance-conferring genes based on the pH of the environment. http://purl.obolibrary.org/obo/ARO_3007565 Aspergillus spp. cyp51A with mutations conferring resistance to triazoles antibiotics http://purl.obolibrary.org/obo/ARO_3007523 triazole-resistant fungal cytochrome P450 enzyme Aspergillus spp. cyp51A is a fungal cytochrome P450 enzyme with mutations in the gene causing triazole resistance. http://purl.obolibrary.org/obo/ARO_3007566 Cryptococcus spp. AFR1 http://purl.obolibrary.org/obo/ARO_0010001 ATP-binding cassette (ABC) antibiotic efflux pump Cryptococcus spp. AFR1 gene is an ABC transporter gene that contributes to antifungal resistance through antibiotic efflux. http://purl.obolibrary.org/obo/ARO_3007567 UDP-glucuronic acid decarboxylase http://purl.obolibrary.org/obo/ARO_3003768 gene conferring resistance via absence UDP-glucuronic acid decarboxylase catalyzes the decarboxylation of UDP-glucuronic acid. Accumulation of UDP-glucuronic acid mediates resistance to 5-flucytosine. http://purl.obolibrary.org/obo/ARO_3007568 Cryptococcus spp. UXS1 conferring resistance to 5-flucytosine via absence http://purl.obolibrary.org/obo/ARO_3007567 UDP-glucuronic acid decarboxylase UXS1 is a UDP-glucuronic acid decarboxylase. Deletion of UXS1 confers resistance to 5-flucytosine by accumulation of UDP-glucoronic acid, thereby suppressing the cellular toxicity of 5-flucytosine. http://purl.obolibrary.org/obo/ARO_3007569 BIOMIC Microbiology System http://purl.obolibrary.org/obo/ARO_3004398 automated testing platform Specific automated system of analysis for determining antimicrobial susceptibility developed by Giles Scientific. http://purl.obolibrary.org/obo/ARO_3007570 Mycaminosyltylonolide http://purl.obolibrary.org/obo/ARO_0000000 macrolide antibiotic Mycaminosyltylonolide is a tylosin derivative with promising anti- P. aeruginosa activity, especially when combined with other antibiotics such as polymixin B. http://purl.obolibrary.org/obo/ARO_3007571 cefquinome http://purl.obolibrary.org/obo/ARO_3009108 fourth-generation cephalosporin Cefquinome is a fourth-generation cephalosporin with pharmacological and antibacterial properties valuable in the treatment of coliform mastitis and other infections. http://purl.obolibrary.org/obo/ARO_3007572 cinnamaldehyde http://purl.obolibrary.org/obo/ARO_3007223 adjuvants enhancing antibiotic entry Cinnamaldehyde was found to enhance the antibacterial activity of ceftriaxone sodium against MDR Salmonella in vitro by significantly reducing the expression of extended-spectrum beta-lactamase, inhibiting the development of drug resistance under ceftriaxone selective pressure in vitro, damaging the cell membrane, and affecting its basic metabolism. http://purl.obolibrary.org/obo/ARO_3007573 fasamycin http://purl.obolibrary.org/obo/ARO_3005171 polyketide with antibiotic activity Fasamycins and congeners are a class of rare aromatic polyketides possessing a partially reduced 1-phenyltetracene pentacyclic core. http://purl.obolibrary.org/obo/ARO_3007574 formicamycin http://purl.obolibrary.org/obo/ARO_3005171 polyketide with antibiotic activity The formicamycins are promising antibiotics first identified in Streptomyces formicae KY5, which produces the compounds at low levels. http://purl.obolibrary.org/obo/ARO_3007575 fasamycin A http://purl.obolibrary.org/obo/ARO_3007573 fasamycin Fasamycin congeners were named as such after they were shown to be inhibitors of the bacterial fatty acid synthase (FAS) condensing enzyme FabF. http://purl.obolibrary.org/obo/ARO_3007576 fasamycin B http://purl.obolibrary.org/obo/ARO_3007573 fasamycin Fasamycin congeners were named as such after they were shown to be inhibitors of the bacterial fatty acid synthase (FAS) condensing enzyme FabF. http://purl.obolibrary.org/obo/ARO_3007577 fasamycin G http://purl.obolibrary.org/obo/ARO_3007573 fasamycin Fasamycin congeners were named as such after they were shown to be inhibitors of the bacterial fatty acid synthase (FAS) condensing enzyme FabF. http://purl.obolibrary.org/obo/ARO_3007578 fasamycin H http://purl.obolibrary.org/obo/ARO_3007573 fasamycin Fasamycin congeners were named as such after they were shown to be inhibitors of the bacterial fatty acid synthase (FAS) condensing enzyme FabF. http://purl.obolibrary.org/obo/ARO_3007579 fasamycin I http://purl.obolibrary.org/obo/ARO_3007573 fasamycin Fasamycin congeners were named as such after they were shown to be inhibitors of the bacterial fatty acid synthase (FAS) condensing enzyme FabF. http://purl.obolibrary.org/obo/ARO_3007580 fasamycin J http://purl.obolibrary.org/obo/ARO_3007573 fasamycin Fasamycin congeners were named as such after they were shown to be inhibitors of the bacterial fatty acid synthase (FAS) condensing enzyme FabF. http://purl.obolibrary.org/obo/ARO_3007581 fasamycin K http://purl.obolibrary.org/obo/ARO_3007573 fasamycin Fasamycin congeners were named as such after they were shown to be inhibitors of the bacterial fatty acid synthase (FAS) condensing enzyme FabF. http://purl.obolibrary.org/obo/ARO_3007582 formicamycin A http://purl.obolibrary.org/obo/ARO_3007574 formicamycin Formicamycin congeners are promising antibiotics with potent activity against Gram-positive pathogens including VRE and MRSA and display a high barrier to selection of resistant isolates. http://purl.obolibrary.org/obo/ARO_3007583 formicamycin B http://purl.obolibrary.org/obo/ARO_3007574 formicamycin Formicamycin congeners are promising antibiotics with potent activity against Gram-positive pathogens including VRE and MRSA and display a high barrier to selection of resistant isolates. http://purl.obolibrary.org/obo/ARO_3007584 formicamycin C http://purl.obolibrary.org/obo/ARO_3007574 formicamycin Formicamycin congeners are promising antibiotics with potent activity against Gram-positive pathogens including VRE and MRSA and display a high barrier to selection of resistant isolates. http://purl.obolibrary.org/obo/ARO_3007585 formicamycin E http://purl.obolibrary.org/obo/ARO_3007574 formicamycin Formicamycin congeners are promising antibiotics with potent activity against Gram-positive pathogens including VRE and MRSA and display a high barrier to selection of resistant isolates. http://purl.obolibrary.org/obo/ARO_3007586 formicamycin M http://purl.obolibrary.org/obo/ARO_3007574 formicamycin Formicamycin congeners are promising antibiotics with potent activity against Gram-positive pathogens including VRE and MRSA and display a high barrier to selection of resistant isolates. http://purl.obolibrary.org/obo/ARO_3007587 formicamycin O http://purl.obolibrary.org/obo/ARO_3007574 formicamycin Formicamycin congeners are promising antibiotics with potent activity against Gram-positive pathogens including VRE and MRSA and display a high barrier to selection of resistant isolates. http://purl.obolibrary.org/obo/ARO_3007588 formicamycin L http://purl.obolibrary.org/obo/ARO_3007574 formicamycin Formicamycin congeners are promising antibiotics with potent activity against Gram-positive pathogens including VRE and MRSA and display a high barrier to selection of resistant isolates. http://purl.obolibrary.org/obo/ARO_3007589 formicamycin F http://purl.obolibrary.org/obo/ARO_3007574 formicamycin Formicamycin congeners are promising antibiotics with potent activity against Gram-positive pathogens including VRE and MRSA and display a high barrier to selection of resistant isolates. http://purl.obolibrary.org/obo/ARO_3007590 formicamycin P http://purl.obolibrary.org/obo/ARO_3007574 formicamycin Formicamycin congeners are promising antibiotics with potent activity against Gram-positive pathogens including VRE and MRSA and display a high barrier to selection of resistant isolates. http://purl.obolibrary.org/obo/ARO_3007591 formicamycin G http://purl.obolibrary.org/obo/ARO_3007574 formicamycin Formicamycin congeners are promising antibiotics with potent activity against Gram-positive pathogens including VRE and MRSA and display a high barrier to selection of resistant isolates. http://purl.obolibrary.org/obo/ARO_3007592 formicamycin D http://purl.obolibrary.org/obo/ARO_3007574 formicamycin Formicamycin congeners are promising antibiotics with potent activity against Gram-positive pathogens including VRE and MRSA and display a high barrier to selection of resistant isolates. http://purl.obolibrary.org/obo/ARO_3007593 formicamycin N http://purl.obolibrary.org/obo/ARO_3007574 formicamycin Formicamycin congeners are promising antibiotics with potent activity against Gram-positive pathogens including VRE and MRSA and display a high barrier to selection of resistant isolates. http://purl.obolibrary.org/obo/ARO_3007594 formicamycin H http://purl.obolibrary.org/obo/ARO_3007574 formicamycin Formicamycin congeners are promising antibiotics with potent activity against Gram-positive pathogens including VRE and MRSA and display a high barrier to selection of resistant isolates. http://purl.obolibrary.org/obo/ARO_3007595 formicamycin Q http://purl.obolibrary.org/obo/ARO_3007574 formicamycin Formicamycin congeners are promising antibiotics with potent activity against Gram-positive pathogens including VRE and MRSA and display a high barrier to selection of resistant isolates. http://purl.obolibrary.org/obo/ARO_3007596 formicamycin I http://purl.obolibrary.org/obo/ARO_3007574 formicamycin Formicamycin congeners are promising antibiotics with potent activity against Gram-positive pathogens including VRE and MRSA and display a high barrier to selection of resistant isolates. http://purl.obolibrary.org/obo/ARO_3007597 formicamycin J http://purl.obolibrary.org/obo/ARO_3007574 formicamycin Formicamycin congeners are promising antibiotics with potent activity against Gram-positive pathogens including VRE and MRSA and display a high barrier to selection of resistant isolates. http://purl.obolibrary.org/obo/ARO_3007598 formicamycin K http://purl.obolibrary.org/obo/ARO_3007574 formicamycin Formicamycin congeners are promising antibiotics with potent activity against Gram-positive pathogens including VRE and MRSA and display a high barrier to selection of resistant isolates. http://purl.obolibrary.org/obo/ARO_3007599 propolis http://purl.obolibrary.org/obo/ARO_3007224 adjuvants inhibiting antibiotic removal Propolis has a significant synergistic effect in combination with ciprofloxacin, erythromycin, and gentamycin. It has a potent inhibitory activity toward the S. aureus (MRS USA300) pump system. http://purl.obolibrary.org/obo/ARO_3007600 cervimycin http://purl.obolibrary.org/obo/ARO_3005171 polyketide with antibiotic activity The polyketide antibiotics cervimycins are natural products of Streptomyces tendae HKI 0179 with promising activity against multidrug-resistant staphylococci and vancomycin-resistant enterococci. http://purl.obolibrary.org/obo/ARO_3007601 cervimycin A http://purl.obolibrary.org/obo/ARO_3007600 cervimycin Cervimycins are polyketide antibiotics. http://purl.obolibrary.org/obo/ARO_3007602 cervimycin B http://purl.obolibrary.org/obo/ARO_3007600 cervimycin Cervimycins are polyketide antibiotics. http://purl.obolibrary.org/obo/ARO_3007603 cervimycin C http://purl.obolibrary.org/obo/ARO_3007600 cervimycin Cervimycins are polyketide antibiotics. http://purl.obolibrary.org/obo/ARO_3007604 cervimycin D http://purl.obolibrary.org/obo/ARO_3007600 cervimycin Cervimycins are polyketide antibiotics. http://purl.obolibrary.org/obo/ARO_3007605 cervimycin K1 http://purl.obolibrary.org/obo/ARO_3007600 cervimycin Cervimycins are polyketide antibiotics. http://purl.obolibrary.org/obo/ARO_3007606 cervimycin K2 http://purl.obolibrary.org/obo/ARO_3007600 cervimycin Cervimycins are polyketide antibiotics. http://purl.obolibrary.org/obo/ARO_3007607 cervimycin N http://purl.obolibrary.org/obo/ARO_3007600 cervimycin Cervimycins are polyketide antibiotics. http://purl.obolibrary.org/obo/ARO_3007608 antibiotic susceptible ERG11 http://purl.obolibrary.org/obo/ARO_3000709 cell wall synthesis enzyme targeted by antibiotic ERG11 is a cytochrome P450 enzyme in Candida species that is not functional when bound by azole antibiotics including fluconazole and itraconazole. However, high levels of ERG11 expression can overcome effective azole doses. http://purl.obolibrary.org/obo/ARO_3007609 antibiotic target overexpression http://purl.obolibrary.org/obo/ARO_1000002 mechanism of antibiotic resistance Increased expression of an antibiotic target protein can overcome effective dose of an antibiotic, leading to reduced susceptibility. http://purl.obolibrary.org/obo/ARO_3007610 gene modulating azole resistance http://purl.obolibrary.org/obo/ARO_3000000 determinant of antibiotic resistance Genes that directly or indirectly modulate azole resistance. http://purl.obolibrary.org/obo/ARO_3007611 sarafloxacin http://purl.obolibrary.org/obo/ARO_0000001 fluoroquinolone antibiotic Sarafloxacin is used for treatment and control of bacterial infections in poultry caused by Escherichia coli and Salmonella spp. It was removed from the market by manufacturers in 2001. http://purl.obolibrary.org/obo/ARO_3007612 hinokitiol http://purl.obolibrary.org/obo/ARO_3007224 adjuvants inhibiting antibiotic removal Hinokitiol (beta-thujaplicin), a natural tropolone derivative found in the heartwood of cupressaceous plants, has been widely used in oral and skin care products as an antimicrobial agent, specifically to enhance tetracyclines against Staphylococcus aureus. http://purl.obolibrary.org/obo/ARO_3007613 totarol http://purl.obolibrary.org/obo/ARO_3007224 adjuvants inhibiting antibiotic removal The phenolic diterpene totarol had good antimicrobial activity against effluxing strains of Staphylococcus aureus. Totoral acts as a NorA efflux pump inhibitor as well as an antistaphylococcal antimicrobial agent. http://purl.obolibrary.org/obo/ARO_3007614 resveratrol http://purl.obolibrary.org/obo/ARO_3005025 ATP synthase inhibitor Resveratrol is a naturally occurring polyphenolic compound that is produced by many different plants, displays antioxidant properties, and protects macromolecules against damage by reactive oxygen species. ATP synthase inhibition with resveratrol can enhance the activity of aminoglycosides against S. aureus and potentially against other bacterial pathogens. http://purl.obolibrary.org/obo/ARO_3007615 pyrrolomycin antibiotic http://purl.obolibrary.org/obo/ARO_3005163 ionophore with antibiotic activity Pyrrolomycins are protonophore antibiotics produced by Actinosporangium and Streptomyces. The mechanism of their antimicrobial activity consists in depolarization of bacterial membrane, leading to the suppression of bacterial bioenergetics through the uncoupling of oxidative phosphorylation. http://purl.obolibrary.org/obo/ARO_3007616 pyrrolomycin A http://purl.obolibrary.org/obo/ARO_3007615 pyrrolomycin antibiotic Pyrrolomycins are protonophores with antibiotic activity. http://purl.obolibrary.org/obo/ARO_3007617 pyrrolomycin B http://purl.obolibrary.org/obo/ARO_3007615 pyrrolomycin antibiotic Pyrrolomycins are protonophores with antibiotic activity. http://purl.obolibrary.org/obo/ARO_3007618 pyrrolomycin C http://purl.obolibrary.org/obo/ARO_3007615 pyrrolomycin antibiotic Pyrrolomycins are protonophores with antibiotic activity. http://purl.obolibrary.org/obo/ARO_3007619 pyrrolomycin D http://purl.obolibrary.org/obo/ARO_3007615 pyrrolomycin antibiotic Pyrrolomycins are protonophores with antibiotic activity. http://purl.obolibrary.org/obo/ARO_3007620 pyrrolomycin E http://purl.obolibrary.org/obo/ARO_3007615 pyrrolomycin antibiotic Pyrrolomycins are protonophores with antibiotic activity. http://purl.obolibrary.org/obo/ARO_3007621 pyrrolomycin F http://purl.obolibrary.org/obo/ARO_3007615 pyrrolomycin antibiotic Pyrrolomycins are protonophores with antibiotic activity. http://purl.obolibrary.org/obo/ARO_3007622 pyrrolomycin F2a http://purl.obolibrary.org/obo/ARO_3007615 pyrrolomycin antibiotic Pyrrolomycins are protonophores with antibiotic activity. http://purl.obolibrary.org/obo/ARO_3007623 pyrrolomycin F2b http://purl.obolibrary.org/obo/ARO_3007615 pyrrolomycin antibiotic Pyrrolomycins are protonophores with antibiotic activity. http://purl.obolibrary.org/obo/ARO_3007624 pyrrolomycin G http://purl.obolibrary.org/obo/ARO_3007615 pyrrolomycin antibiotic Pyrrolomycins are protonophores with antibiotic activity. http://purl.obolibrary.org/obo/ARO_3007625 pyrrolomycin H http://purl.obolibrary.org/obo/ARO_3007615 pyrrolomycin antibiotic Pyrrolomycins are protonophores with antibiotic activity. http://purl.obolibrary.org/obo/ARO_3007626 pyrrolomycin F3 http://purl.obolibrary.org/obo/ARO_3007615 pyrrolomycin antibiotic Pyrrolomycins are protonophores with antibiotic activity. http://purl.obolibrary.org/obo/ARO_3007627 pyrrolomycin I http://purl.obolibrary.org/obo/ARO_3007615 pyrrolomycin antibiotic Pyrrolomycins are protonophores with antibiotic activity. http://purl.obolibrary.org/obo/ARO_3007628 pyrrolomycin J http://purl.obolibrary.org/obo/ARO_3007615 pyrrolomycin antibiotic Pyrrolomycins are protonophores with antibiotic activity. http://purl.obolibrary.org/obo/ARO_3007629 cadaside antibiotic http://purl.obolibrary.org/obo/ARO_3000035 lipopeptide antibiotic The cadasides are calcium-dependent cyclic acidic lipopeptide antibiotics that disrupt cell wall biosynthesis and show activity against multiple drug-resistant Gram-positive pathogens. http://purl.obolibrary.org/obo/ARO_3007630 cadaside A http://purl.obolibrary.org/obo/ARO_3007629 cadaside antibiotic Cadasides are lipopeptides with antibiotic activity. http://purl.obolibrary.org/obo/ARO_3007631 cadaside B http://purl.obolibrary.org/obo/ARO_3007629 cadaside antibiotic Cadasides are lipopeptides with antibiotic activity. http://purl.obolibrary.org/obo/ARO_3007632 FRI-11 http://purl.obolibrary.org/obo/ARO_3004796 FRI beta-lactamase FRI-11 is a FRI-type carbapenem-hydrolyzing class A beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007633 KPC-125 http://purl.obolibrary.org/obo/ARO_3000059 KPC beta-lactamase KPC-125 is a KPC-type class A beta-lactamase. KPC-125 is a variant of KPC-3, differing by a D179A polymorphism within the omega-loop region. http://purl.obolibrary.org/obo/ARO_3007634 CAE beta-lactamase http://purl.obolibrary.org/obo/ARO_3000078 class A beta-lactamase CAE beta-lactamases are a novel class A serine beta-lactamase family first isolated from Comamonas aquatica. http://purl.obolibrary.org/obo/ARO_3007635 CAE-1 http://purl.obolibrary.org/obo/ARO_3007634 CAE beta-lactamase CAE-1 is a CAE beta-lactamase and confers resistance to ampicillin, piperacillin, cefazolin, cefuroxime, and ceftriaxone, and elevates the MIC of ampicillin-sulbactam two-fold in Escherichia coli DH5alpha, suggesting that CAE-1 functions as a broad-spectrum beta-lactamase. http://purl.obolibrary.org/obo/ARO_3007636 iboxamycin http://purl.obolibrary.org/obo/ARO_0000017 lincosamide antibiotic Iboxamycin is a fully synthetic lincosamide antibiotic. Like other lincosamides, it selectively targets the bacterial ribosome and prevents elongation of the peptide chain. Iboxamycin has been shown to be effective against bacterial strains otherwise resistant to licosamide antibiotics. http://purl.obolibrary.org/obo/ARO_3007637 Clostridioides difficile cplR http://purl.obolibrary.org/obo/ARO_3007068 Miscellaneous ABC-F subfamily ATP-binding cassette ribosomal protection proteins CplR is an ABC-F ATPase ribosomal protection protein from Clostridioides difficile which confers resistance to pleuromutilins and lincosamides. Its resistance to these antibiotics increases in synergy with erythromcyin resistance methylases (e.g., ermB). http://purl.obolibrary.org/obo/ARO_3007638 hygromycin A http://purl.obolibrary.org/obo/ARO_3000003 antibiotic without defined classification Hygromycin A is an antibiotic produced by Streptomyces hygroscopicus. It inhibits translation by binding to the peptidyl transferase center on the large ribosomal subunit. This prevents the binding of aminoacyl-tRNA to the A-site. Not to confused with Hygromycin B, which is structurally distinct. http://purl.obolibrary.org/obo/ARO_3007639 A201A http://purl.obolibrary.org/obo/ARO_3000080 aminonucleoside antibiotic A201A is a nucleoside antibiotic. It inhibits translation by binding to the peptidyl transferase center on the large ribosomal subunit. This prevents the binding of aminoacyl-tRNA to the A-site. http://purl.obolibrary.org/obo/ARO_3007640 Candida spp. pleiotropic drug resistance factor 1 http://purl.obolibrary.org/obo/ARO_3007552 pleiotropic drug resistance transcription factors PDR1 is a transcription factor that regulates the expression of several genes encoding ABC transporters, contributing to multidrug resistance. http://purl.obolibrary.org/obo/ARO_3007641 fungal nucleobase transporters http://purl.obolibrary.org/obo/ARO_3000270 protein modulating permeability to antibiotic Fungal nucleobase transporters facilitate the movement of nucleobases across the fungal cell membrane. The absence confers resistance to antibiotics by preventing antibiotic entry into the cell. http://purl.obolibrary.org/obo/ARO_3007642 Aspergillus spp. fcyB conferring resistance to 5-flucytosine via reduced permeability http://purl.obolibrary.org/obo/ARO_3007641 fungal nucleobase transporters FcyB encodes for purine-cytosine permease in fungal cells. Downregulation or absence of fcyB confers resistance to antibiotics by preventing entry into the cell. http://purl.obolibrary.org/obo/ARO_3007643 Aspergillus spp. transcription factor pacC http://purl.obolibrary.org/obo/ARO_3007564 pH-responsive transcription factors PacC is a pH-responsive transcription factor. It regulates the expression of antibiotic susceptible genes whose absence confers resistance to antibiotics. http://purl.obolibrary.org/obo/ARO_3007644 Clostridium perfringes cplR http://purl.obolibrary.org/obo/ARO_3007068 Miscellaneous ABC-F subfamily ATP-binding cassette ribosomal protection proteins CplR is an ABC-F ATPase ribosomal protection protein from Clostridium perfringes which confers resistance to pleuromutilins and lincosamides. http://purl.obolibrary.org/obo/ARO_3007645 Clostridium sporogenes cplR http://purl.obolibrary.org/obo/ARO_3007068 Miscellaneous ABC-F subfamily ATP-binding cassette ribosomal protection proteins CplR is an ABC-F ATPase ribosomal protection protein from Clostridium sporogenes which confers resistance to pleuromutilins and lincosamides. http://purl.obolibrary.org/obo/ARO_3007646 Neobacillus vireti vmlR2 http://purl.obolibrary.org/obo/ARO_3007068 Miscellaneous ABC-F subfamily ATP-binding cassette ribosomal protection proteins vmlR2 is an ABC-F ATPase ribosomal protection protein from Neobacillus vireti (formerly known as Bacillus vireti). This representative of the ARE2 subfamily has an unusually long linker domain. Confers resistance to some lincosamide and nucleoside antibiotics. http://purl.obolibrary.org/obo/ARO_3007647 PSZ beta-lactamase http://purl.obolibrary.org/obo/ARO_3000076 class C beta-lactamase PSZ beta-lactamases are a novel AmpC enzyme gene family, which was found on a strain of Pantoea endophytica isolated from a rabbit in a livestock farm in China. It shows resistance to penicillins and several cephalosporins, and shares the highest amino acid similarity with the function-characterized AmpC enzyme ERH-1. http://purl.obolibrary.org/obo/ARO_3007648 PSZ-1 http://purl.obolibrary.org/obo/ARO_3007647 PSZ beta-lactamase PSZ-1 is a PSZ beta-lactamase found in Pantoea endophytica. The gene showed resistance to penicillins and several first-, second-and third-generation cephalosporins as well as aztreonam. http://purl.obolibrary.org/obo/ARO_3007649 CDA beta-lactamase http://purl.obolibrary.org/obo/ARO_3000076 class C beta-lactamase A CDA beta-lactamase was identified as a novel class C enzyme that was phylogenetically and biochemically close to the chromosome-borne beta-lactamases of the genera Enterobacter and Citrobacter. http://purl.obolibrary.org/obo/ARO_3007650 CDA-1 http://purl.obolibrary.org/obo/ARO_3007649 CDA beta-lactamase CDA-1 was recovered from a urine sample and is intermediate or resistant to third-generation cephalosporins and carbapenems. Susceptibility testing, isoelectric focusing, and analysis of outer membrane proteins showed that AmpC beta-lactamase expression combined with porin deficiency accounted for the carbapenem resistance. http://purl.obolibrary.org/obo/ARO_3007651 carmoisine http://purl.obolibrary.org/obo/ARO_3007225 adjuvants which alter physiology Carmoisine is widely used as a food coloring agent. Carmoisine-mediated reduction of biofilm in Pseudomonas aeruginosa is due to its interaction with LasR and interference with the QS system. http://purl.obolibrary.org/obo/ARO_3007652 lipoxin A4 http://purl.obolibrary.org/obo/ARO_3007225 adjuvants which alter physiology Lipoxin A4 is a Specialized Pro-resolving Mediator and has direct effects on P. aeruginosa where it reduced biofilm formation and promoted ciprofloxacin antibiotic efficacy in a static biofilm-forming system. Further studies show lipoxin A4 can help antibiotic efficacy and promote monocyte activity against established P. aeruginosa biofilm formed under hydrodynamic conditions. http://purl.obolibrary.org/obo/ARO_3007653 ascorbic acid http://purl.obolibrary.org/obo/ARO_3007225 adjuvants which alter physiology The production of pyocyanin by Pseudomonas aeruginosa increases its virulence, fitness and biofilm formation. Ascorbic acid combined with furanone-30 elevated quorum-sensing inhibition in P. aeruginosa, which was directly associated with significantly reduced virulence, adhesion, aggregation and biofilm formation and enhanced antibiotic-mediated bacterial killing. http://purl.obolibrary.org/obo/ARO_3007654 erm(56) http://purl.obolibrary.org/obo/ARO_3000560 Erm 23S ribosomal RNA methyltransferase Erm(56) is an Erm ribosomal RNA methyltransferase. Expression of the cloned erm(56) confers resistance to MLSB in T. pyogenes and Escherichia coli. http://purl.obolibrary.org/obo/ARO_3007655 nifuroxazide http://purl.obolibrary.org/obo/ARO_3004116 nitrofuran antibiotic Nifuroxazide is an oral nitrofuran antibiotic used to treat colitis and diarrhea in humans and non-humans. It has recently been explored to be repurposed for parasitic diseases. http://purl.obolibrary.org/obo/ARO_3007656 antibiotic resistant Mycobacterium tuberculosis nitroreductase http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Inactivation of the F420-dependent anti-oxidant mechanism that protects M.tuberculosis against oxidative stress and bactericidal agents plays a role in antibiotic resistance. http://purl.obolibrary.org/obo/ARO_3007657 metal transporters with antibiotic efflux http://purl.obolibrary.org/obo/ARO_3000159 efflux pump complex or subunit conferring antibiotic resistance Efflux pumps also regulate the level of metal ions in the cytoplasm but are toxic when in excess. Metals often act as a facilitator in the proliferation and persistence of antibiotic resistance. Therefore, metal contamination in natural environments could have an important role in maintaining and promoting antibiotic resistance. The presence of metals co-selects for antibiotic resistance and leads to the development of cross-resistance. Micro-organisms adopt various mechanisms that may confer resistance against more than one antimicrobial, of which multidrug efflux systems are the most common. http://purl.obolibrary.org/obo/ARO_3007658 albicidin http://purl.obolibrary.org/obo/ARO_3000053 peptide antibiotic Albicidin phytotoxins produced by the sugarcane pathogen Xanthomonas albilineans is a potent DNA gyrase inhibitor with inhibitory effects significantly better than most DNA gyrase inhibitors. Albicidin acts primarily by inhibiting the religation of the cleaved DNA intermediate during the gyrase catalytic sequence similar to quinolones. http://purl.obolibrary.org/obo/ARO_3007659 putative nickel/cobalt transporter http://purl.obolibrary.org/obo/ARO_3007657 metal transporters with antibiotic efflux Ectopic expression of NiCoT in Escherichia coli CS109 resulted in the increase of intracellular nickel uptake with enhanced tolerance towards several antibiotics when NiCoT was overexpressed in E. coli and Mycobacterium smegmatis. The presence of a sub-inhibitory dose of nickel resulted in the manifestation of low-level tolerance towards these drugs. http://purl.obolibrary.org/obo/ARO_3007660 clerocidin http://purl.obolibrary.org/obo/ARO_3005172 terpene with antibiotic activity Clerocidin is a terpenoid antibiotic that inhibits bacterial DNA gyrase. It is a natural diterpenoid which has been shown to selectively react with single-stranded bases without targeting the double helix. http://purl.obolibrary.org/obo/ARO_3007661 Mycobacterium tuberculosis ddn mutation conferring resistance to nitroimidazole antibiotics http://purl.obolibrary.org/obo/ARO_3007656 antibiotic resistant Mycobacterium tuberculosis nitroreductase ddn is a protein-coding gene involved in the bioreductive activation of bicyclic 4-nitroimidazole prodrugs such as PA-824 and delamanid developed for anti-tuberculosis therapy against both replicating and persistent bacteria. http://purl.obolibrary.org/obo/ARO_3007662 Rv1877 http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump Rv1877, a putative Major Facilitator Superfamily efflux pump from M. tuberculosis actively effluxes fluoroquinolones ofloxacin and levofloxacin. http://purl.obolibrary.org/obo/ARO_3007663 stress-activated protein kinases http://purl.obolibrary.org/obo/ARO_3003768 gene conferring resistance via absence Stress-activated protein kinases (SAPK) are kinases involved in cellular response to stress whose absence confers resistance to antifungal drug compounds. http://purl.obolibrary.org/obo/ARO_3007664 Candida spp. High Osmolarity Glycerol 1 conferring resistance to caspofungin via absence http://purl.obolibrary.org/obo/ARO_3007663 stress-activated protein kinases Hog1 is a stress-activated protein kinase. Deletion of Hog1 confers resistance to caspofungin through increase in exposed chitin levels in the cell wall. http://purl.obolibrary.org/obo/ARO_3007665 Candida spp. FCY2 conferring resistance to 5-flucytosine via reduced permeability http://purl.obolibrary.org/obo/ARO_3007641 fungal nucleobase transporters FCY2 encodes for purine-cytosine permease in fungal cells. Downregulation or absence of FCY2 confers resistance to antibiotics by preventing entry into the cell. http://purl.obolibrary.org/obo/ARO_3007666 Candida spp. cyp51A1 with mutations conferring resistance to triazoles and imidazole antibiotics http://purl.obolibrary.org/obo/ARO_3007667 imidazole-resistant fungal cytochrome P450 enzyme Candida spp. cyp51A1 is a fungal cytochrome P450 enzyme with mutations in the gene causing triazole and imidazole resistance. http://purl.obolibrary.org/obo/ARO_3007667 imidazole-resistant fungal cytochrome P450 enzyme http://purl.obolibrary.org/obo/ARO_3007522 antifungal-resistant cytochrome P450 enzyme Fungal cytochrome P450 enzymes which include mutations to confer resistance to imidazole-class antibiotics. http://purl.obolibrary.org/obo/ARO_3007668 HMG-CoA reductase-encoding genes http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant HMG-CoA reductase-encoding genes which include mutations to confer resistance to antifungal drug compounds. http://purl.obolibrary.org/obo/ARO_3007669 aadT http://purl.obolibrary.org/obo/ARO_0010002 major facilitator superfamily (MFS) antibiotic efflux pump The AadT pump is a novel multidrug efflux pump from the proton antiporter 2 (DHA2) family and was discovered in Acinetobacter multidrug resistance plasmids. The presence of AadT decreased bacterial susceptibility to antibiotics (erythromycin and tetracycline), biocides (chlorhexidine), and dyes (ethidium bromide and DAPI) and was able to mediate ethidium transport. http://purl.obolibrary.org/obo/ARO_3007670 Aspergillus spp. Hmg1 with mutations conferring resistance to triazoles antibiotics http://purl.obolibrary.org/obo/ARO_3007668 HMG-CoA reductase-encoding genes Hmg1 is an HMG-CoA reductase-encoding gene with mutations in the gene causing triazole resistance. http://purl.obolibrary.org/obo/ARO_3007671 Clostridioides difficile nimB http://purl.obolibrary.org/obo/ARO_3007103 nitroimidazole reductase Clostridioides difficile nimB is a heme-dependent flavin enzyme that degrades nitroimidazoles to amines lacking antimicrobial activity. NimB expression alone is not sufficient for nitroimidazole resistance. Constitutive transcription of nimB, which is driven by a mutation in the promoter PnimBG, is a mechanism of clinically-relevant heme-dependent metronidazole resistance in C. difficile. http://purl.obolibrary.org/obo/ARO_3007672 antibiotic resistant Rv0678 http://purl.obolibrary.org/obo/ARO_0000031 antibiotic resistant gene variant or mutant Rv0678 encodes a transcription factor which negatively regulates the expression of the mmpS5/L5 efflux pump. http://purl.obolibrary.org/obo/ARO_3007673 bedaquiline resistant Rv0678 http://purl.obolibrary.org/obo/ARO_3007672 antibiotic resistant Rv0678 Loss-of-function mutations in the Mycobacterium Rv0678 gene associated with bedaquiline resistance. http://purl.obolibrary.org/obo/ARO_3007674 Mycobacterium tuberculosis Rv0678 with mutation conferring resistance to bedaquiline http://purl.obolibrary.org/obo/ARO_3007673 bedaquiline resistant Rv0678 Rv0678 encodes a transcription factor which negatively regulates the expression of the mmpS5/L5 efflux pump. Loss-of-function mutations in rv0678 are a common mechanism of resistance. http://purl.obolibrary.org/obo/ARO_3007675 famotidine http://purl.obolibrary.org/obo/ARO_3007225 adjuvants which alter physiology Famotidine enhances the antibacterial activity of rifamycin antibiotics, especially rifampicin, against Gram-negative bacteria and reverses drug resistance. Famotidine disrupts the cell membrane of A. baumannii and inhibits the expression of the outer membrane protein ompA gene, while causing a dissipation of the plasma membrane potential which increases the accumulation of reactive oxygen species leading to increased bacterial mortality. Famotidine also inhibited the efflux pump activity and the biofilm formation of A. baumannii. http://purl.obolibrary.org/obo/ARO_3007677 furazidin http://purl.obolibrary.org/obo/ARO_3004116 nitrofuran antibiotic Furazidin is a nitrofuran derivative, acting as an antibacterial medicine with bacteriostatic action. It is active against both gram-positive and gram-negative bacteria. It is used for the treatment of urinary tract, skin, and soft tissues infections. http://purl.obolibrary.org/obo/ARO_3007678 IreK http://purl.obolibrary.org/obo/ARO_3007683 Serine/threonine kinases E. faecalis IreK maintains cell wall integrity, possibly by regulating peptidoglycan biosynthesis and metabolism. Antibiotic-induced cell wall stress leads to activation of IreK-mediated phosphorylation signaling pathways to mitigate and repair the damage. Absence of IreK leads to cell envelope defects and increased susceptibility to a variety of cephalosporins, including ceftriaxone. Increased IreK phosphorylation in response to ceftriaxone treatment has been shown to correlate with antimicrobial resistance. http://purl.obolibrary.org/obo/ARO_3007679 chrysomycin A http://purl.obolibrary.org/obo/ARO_3000103 aminocoumarin antibiotic Chrysomycin A (ChryA) is a benzonaphthopyranone glycoside with rapid bactericidal activity that is highly active against S. aureus persisters, robustly eradicates biofilms in vitro, and shows a sustainable killing efficacy in vivo. Chrysomycin A belongs to the coumarin class of antibiotics which are known to bind gyrase subunit B and inhibit the enzyme function. http://purl.obolibrary.org/obo/ARO_3007680 2,4-diacetylphloroglucinol http://purl.obolibrary.org/obo/ARO_3005171 polyketide with antibiotic activity 2,4-diacetylphloroglucinol (DAPG) is a broad-spectrum antibiotic that was originally isolated from a fluorescent Pseudomonas strain. DAPG is active against numerous organisms, including plants, fungi, viruses, bacteria, and nematodes, and production or increased production of DAPG has been associated with enhanced activity against plant pathogens. http://purl.obolibrary.org/obo/ARO_3007682 MdtQ http://purl.obolibrary.org/obo/ARO_3004278 Outer Membrane Porin (Opr) MdtQ is a putative multidrug resistance outer membrane protein found in carbapenem-resistant Klebsiella pneumoniae. http://purl.obolibrary.org/obo/ARO_3007683 Serine/threonine kinases http://purl.obolibrary.org/obo/ARO_3000270 protein modulating permeability to antibiotic The eukaryotic-type Ser/Thr kinase (STKs) IreK (intrinsic resistance of enterococci kinase) belongs to a family of transmembrane kinases defined by the presence of multiple extracellular PASTA (penicillin-binding protein and serine/threonine kinase associated) domains. In prokaryotes, STKs modulate cellular functions such as growth, differentiation, and secondary metabolism. When the external environment changes, prokaryotes rely on signal transduction systems, including STKs that quickly sense these changes and alter gene expression to induce the appropriate metabolic changes. http://purl.obolibrary.org/obo/ARO_3007684 transmembrane protein conferring colistin resistance http://purl.obolibrary.org/obo/ARO_3003768 gene conferring resistance via absence Mutations in mgrB transmembrane proteins can confer resistance to the antibiotic colistin. http://purl.obolibrary.org/obo/ARO_1000001 process or component of antibiotic biology or chemistry Antibiotic resistance is the ability of a microorganism to withstand the effects of an antibiotic. It is a specific type of drug resistance. http://purl.obolibrary.org/obo/RO_0000056 participates_in http://purl.obolibrary.org/obo/RO_0001000 derives_from http://purl.obolibrary.org/obo/BFO_0000051 has_part http://purl.obolibrary.org/obo/RO_0002409 indirectly_negatively_regulates http://purl.obolibrary.org/obo/RO_0012006 is_small_molecule_inhibitor_of http://purl.obolibrary.org/obo/BFO_0000050 part_of http://purl.obolibrary.org/obo/RO_0002211 regulates http://purl.obolibrary.org/obo/RO_0002212 negatively_regulates http://purl.obolibrary.org/obo/RO_0002213 positively_regulates http://purl.obolibrary.org/obo/RO#_is_a is_a http://purl.obolibrary.org/obo/RO_0002312 evolutionary_variant_of http://purl.obolibrary.org/obo/RO_0002407 indirectly_positively_regulates