ARDB-Antibiotic Resistance Genes Database

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Your Query:     Database: Resistance Gene(ALL)    Species: Bacillus anthracis str. 'Ames Ancestor'    

12 resistance genes are found

Gene IDGene TypeResistance ProfileDescription
YP_018024bacabacitracin; Undecaprenyl pyrophosphate phosphatase, which consists in the sequestration of Undecaprenyl pyrophosphate.

AAT31156fosbfosfomycin; Glutathione transferase, metalloglutathione transferase which confers resistance to fosfomycin by catalyzing the addition of glutathione to fosfomycin

AAT32609bl2a_1penicillin; Class A beta-lactamase. This enzyme breaks the beta-lactam antibiotic ring open and deactivates the molecule's antibacterial properites.

YP_018681fosbfosfomycin; Glutathione transferase, metalloglutathione transferase which confers resistance to fosfomycin by catalyzing the addition of glutathione to fosfomycin

YP_020134bl2a_1penicillin; Class A beta-lactamase. This enzyme breaks the beta-lactam antibiotic ring open and deactivates the molecule's antibacterial properites.

AAT30499bacabacitracin; Undecaprenyl pyrophosphate phosphatase, which consists in the sequestration of Undecaprenyl pyrophosphate.

YP_016893bacabacitracin; Undecaprenyl pyrophosphate phosphatase, which consists in the sequestration of Undecaprenyl pyrophosphate.

AAT29368bacabacitracin; Undecaprenyl pyrophosphate phosphatase, which consists in the sequestration of Undecaprenyl pyrophosphate.

AAT33228fosbfosfomycin; Glutathione transferase, metalloglutathione transferase which confers resistance to fosfomycin by catalyzing the addition of glutathione to fosfomycin

YP_020753fosbfosfomycin; Glutathione transferase, metalloglutathione transferase which confers resistance to fosfomycin by catalyzing the addition of glutathione to fosfomycin

YP_019143bl2a_iiipenicillin; Class A beta-lactamase. This enzyme breaks the beta-lactam antibiotic ring open and deactivates the molecule's antibacterial properites.

AAT31618bl2a_iiipenicillin; Class A beta-lactamase. This enzyme breaks the beta-lactam antibiotic ring open and deactivates the molecule's antibacterial properites.