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    <AnnotationProperty rdf:about="http://purl.obolibrary.org/obo/IAO_0000115"/>
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    <!-- http://purl.obolibrary.org/obo/ARO_2000000 -->

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        <rdfs:label>confers_resistance_to_antibiotic</rdfs:label>
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        <rdfs:label>confers_resistance_to_drug_class</rdfs:label>
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    <!-- http://purl.obolibrary.org/obo/ARO_0000004 -->

    <Class rdf:about="http://purl.obolibrary.org/obo/ARO_0000004">
        <rdfs:label>monobactam</rdfs:label>
    </Class>
    


    <!-- http://purl.obolibrary.org/obo/ARO_0000032 -->

    <Class rdf:about="http://purl.obolibrary.org/obo/ARO_0000032">
        <rdfs:label>cephalosporin</rdfs:label>
    </Class>
    


    <!-- http://purl.obolibrary.org/obo/ARO_2000000 -->

    <Class rdf:about="http://purl.obolibrary.org/obo/ARO_2000000">
        <rdfs:label>confers_resistance_to_antibiotic</rdfs:label>
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    <!-- http://purl.obolibrary.org/obo/ARO_2000001 -->

    <Class rdf:about="http://purl.obolibrary.org/obo/ARO_2000001">
        <rdfs:label>confers_resistance_to_drug_class</rdfs:label>
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    <!-- http://purl.obolibrary.org/obo/ARO_3000008 -->

    <Class rdf:about="http://purl.obolibrary.org/obo/ARO_3000008">
        <rdfs:label>penicillin beta-lactam</rdfs:label>
    </Class>
    


    <!-- http://purl.obolibrary.org/obo/ARO_3000014 -->

    <Class rdf:about="http://purl.obolibrary.org/obo/ARO_3000014">
        <rdfs:label>TEM beta-lactamase</rdfs:label>
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        <ns4:IAO_0000115>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.</ns4:IAO_0000115>
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    <!-- http://purl.obolibrary.org/obo/ARO_3000078 -->

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        <rdfs:label>class A beta-lactamase</rdfs:label>
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    <!-- http://purl.obolibrary.org/obo/ARO_3000637 -->

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        <rdfs:label>ampicillin</rdfs:label>
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