| Gene name | Length | Location | Length of alignment | Identity (%) | Coverage (%) | E-value |
|---|---|---|---|---|---|---|
| repA | 1007 | 5168572 - 5169572 (-) | 1007 | 70 | 91 | 3.595E-121 |
| Type match | Model name | Model type | Location | E-value | Identity | ||||
|---|---|---|---|---|---|---|---|---|---|
| Strict | TRU-1 | protein homolog model | 1204909 - 1206057(+) | 0 | 71.7 % | ||||
|
AMR Gene Family
A class C beta-lactamase endogenous to Aeromonas enteropelogenes (tructi)
Drug Class
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.
Drug Class
Penams, often referred to as penicillins, are a group of antibiotics derived from Penicillium fungi. Penicillin 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.
Resistance Mechanism
Enzymatic inactivation of antibiotic to confer drug resistance.
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| Strict | adeF | protein homolog model | 1427656 - 1430784(-) | 0 | 49.23 % | ||||
|
AMR Gene Family
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.
Antibiotic
Tetracycline is a broad-spectrum polyketide antibiotic produced by many Streptomyces. It works by inhibiting action of the prokaryotic 30S ribosome.
Drug Class
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.
Drug Class
These antibiotics are derived from tetracycline, a polyketide antibiotic that inhibits the 30S subunit of bacterial ribosomes.
Efflux Component
Efflux proteins that pump antibiotic out of a cell to confer resistance.
Resistance Mechanism
Antibiotic resistance via the transport of antibiotics out of the cell.
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| Strict | adeF | protein homolog model | 1483842 - 1486991(+) | 0 | 43.61 % | ||||
|
AMR Gene Family
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.
Antibiotic
Tetracycline is a broad-spectrum polyketide antibiotic produced by many Streptomyces. It works by inhibiting action of the prokaryotic 30S ribosome.
Drug Class
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.
Drug Class
These antibiotics are derived from tetracycline, a polyketide antibiotic that inhibits the 30S subunit of bacterial ribosomes.
Efflux Component
Efflux proteins that pump antibiotic out of a cell to confer resistance.
Resistance Mechanism
Antibiotic resistance via the transport of antibiotics out of the cell.
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| Strict | CEPH-A3 | protein homolog model | 4360347 - 4361108(-) | 0 | 98.81 % | ||||
|
AMR Gene Family
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.
Drug Class
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.
Resistance Mechanism
Enzymatic inactivation of antibiotic to confer drug resistance.
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| Strict | OXA-724 | protein homolog model | 5249156 - 5249950(+) | 0 | 97.73 % | ||||
|
AMR Gene Family
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.
Drug Class
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.
Drug Class
Penams, often referred to as penicillins, are a group of antibiotics derived from Penicillium fungi. Penicillin 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.
Resistance Mechanism
Enzymatic inactivation of antibiotic to confer drug resistance.
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| Strict | Escherichia coli EF-Tu mutants conferring resistance to Pulvomycin | protein variant model | 274318 - 275502(+) | 0 | 90.61 % | ||||
|
AMR Gene Family
Sequence variants of elongation factor Tu that confer resistance to elfamycin antibiotics.
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.
Drug Class
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.
Resistance Mechanism
Mutational alteration or enzymatic modification of antibiotic target which results in antibiotic resistance.
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| Strict | Escherichia coli EF-Tu mutants conferring resistance to Pulvomycin | protein variant model | 294566 - 295750(+) | 0 | 90.61 % | ||||
|
AMR Gene Family
Sequence variants of elongation factor Tu that confer resistance to elfamycin antibiotics.
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.
Drug Class
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.
Resistance Mechanism
Mutational alteration or enzymatic modification of antibiotic target which results in antibiotic resistance.
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