ARDB-Antibiotic Resistance Genes Database

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Your Query:     Database: Resistance Gene(ALL)    Species: Bacillus anthracis Tsiankovskii-I    

12 resistance genes are found

Gene IDGene TypeResistance ProfileDescription
ZP_03020988bacabacitracin; Undecaprenyl pyrophosphate phosphatase, which consists in the sequestration of Undecaprenyl pyrophosphate.

ZP_03020873fosbfosfomycin; Glutathione transferase, metalloglutathione transferase which confers resistance to fosfomycin by catalyzing the addition of glutathione to fosfomycin

EDV18181bl2a_1penicillin; Class A beta-lactamase. This enzyme breaks the beta-lactam antibiotic ring open and deactivates the molecule's antibacterial properites.

ZP_03018958fosbfosfomycin; Glutathione transferase, metalloglutathione transferase which confers resistance to fosfomycin by catalyzing the addition of glutathione to fosfomycin

ZP_03020269bacabacitracin; Undecaprenyl pyrophosphate phosphatase, which consists in the sequestration of Undecaprenyl pyrophosphate.

EDV15453bacabacitracin; Undecaprenyl pyrophosphate phosphatase, which consists in the sequestration of Undecaprenyl pyrophosphate.

EDV14991fosbfosfomycin; Glutathione transferase, metalloglutathione transferase which confers resistance to fosfomycin by catalyzing the addition of glutathione to fosfomycin

EDV17212bl2a_iiipenicillin; Class A beta-lactamase. This enzyme breaks the beta-lactam antibiotic ring open and deactivates the molecule's antibacterial properites.

ZP_03018140bl2a_iiipenicillin; Class A beta-lactamase. This enzyme breaks the beta-lactam antibiotic ring open and deactivates the molecule's antibacterial properites.

EDV14787bacabacitracin; Undecaprenyl pyrophosphate phosphatase, which consists in the sequestration of Undecaprenyl pyrophosphate.

ZP_03017821bl2a_1penicillin; Class A beta-lactamase. This enzyme breaks the beta-lactam antibiotic ring open and deactivates the molecule's antibacterial properites.

EDV16924fosbfosfomycin; Glutathione transferase, metalloglutathione transferase which confers resistance to fosfomycin by catalyzing the addition of glutathione to fosfomycin