bearer of at some time only_in_taxon Brucella virulence factor disposition Brucella suis 1330 lon protein ATP-dependent protease La LocusTag: BR1106 NCBIGene: 1166782 Molecule Role Annotation: FUNCTION: Degrades short-lived regulatory and abnormal proteins in presence of ATP. Hydrolyzes two ATPs for each peptide bond cleaved in the protein substrate (By similarity)(Swiss-Prot: Q8G0I7). CATALYTIC ACTIVITY: Hydrolysis of proteins in presence of ATP(Swiss-Prot: Q8G0I7). SUBUNIT: Homotetramer (By similarity)(Swiss-Prot: Q8G0I7). SUBCELLULAR LOCATION: Cytoplasm (By similarity)(Swiss-Prot: Q8G0I7). SIMILARITY: Belongs to the peptidase S16 family(Swiss-Prot: Q8G0I7). SIMILARITY: Contains 1 Lon domain(Swiss-Prot: Q8G0I7). MUTATION: In contrast to the parent strain, the Brucella abortus lon mutant, was impaired in its capacity to form isolated colonies on solid medium at 41 degrees C and displayed an increased sensitivity to killing by puromycin and H2O2. Brucella abortus Lon homologue functions as a stress response protease that is required for wild-type virulence during the initial stages of infection in the mouse model, but is not essential for the establishment and maintenance of chronic infection in this host [Ref6494:Robertson et al., 2000]. Both single lon or clpA mutations had comparable effects on growth inhibition, suggesting that the concerned proteases Lon and ClpAP both degrade a number of specific proteins, but are also both involved in general degradation of abnormal proteins. Compared to the single mutants, the double mutant lon clpA was highly sensitive to canavanine. One possible explanation for this observation is that both proteases can substitute for each other to a large extent during bacterial growth. Hence, simultaneous inactivation or decrease in activation of both proteases, either by direct mutation or by elimination of the regulatory component ClpA, strongly increased growth inhibition [Ref6494:Robertson et al., 2000]. NCBIProteinAccess:NP_698111.1 Gene name: lon PMID: 10672180 NCBIProteinGI: 23501984 This protein is a Brucella virulence factor. FUNCTION: Degrades short-lived regulatory and abnormal proteins in presence of ATP. Hydrolyzes two ATPs for each peptide bond cleaved in the protein substrate (By similarity)(Swiss-Prot: Q8G0I7). CATALYTIC ACTIVITY: Hydrolysis of proteins in presence of ATP(Swiss-Prot: Q8G0I7). SUBUNIT: Homotetramer (By similarity)(Swiss-Prot: Q8G0I7). SUBCELLULAR LOCATION: Cytoplasm (By similarity)(Swiss-Prot: Q8G0I7). SIMILARITY: Belongs to the peptidase S16 family(Swiss-Prot: Q8G0I7). SIMILARITY: Contains 1 Lon domain(Swiss-Prot: Q8G0I7). MUTATION: In contrast to the parent strain, the Brucella abortus lon mutant, was impaired in its capacity to form isolated colonies on solid medium at 41 degrees C and displayed an increased sensitivity to killing by puromycin and H2O2. Brucella abortus Lon homologue functions as a stress response protease that is required for wild-type virulence during the initial stages of infection in the mouse model, but is not essential for the establishment and maintenance of chronic infection in this host [Ref6494:Robertson et al., 2000]. Both single lon or clpA mutations had comparable effects on growth inhibition, suggesting that the concerned proteases Lon and ClpAP both degrade a number of specific proteins, but are also both involved in general degradation of abnormal proteins. Compared to the single mutants, the double mutant lon clpA was highly sensitive to canavanine. One possible explanation for this observation is that both proteases can substitute for each other to a large extent during bacterial growth. Hence, simultaneous inactivation or decrease in activation of both proteases, either by direct mutation or by elimination of the regulatory component ClpA, strongly increased growth inhibition [Ref6494:Robertson et al., 2000]. UniProtKB: PR:Q8G0I7