ARDB-Antibiotic Resistance Genes Database

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Your Query:     Database: Resistance Gene(ALL)    Species: Bacillus cereus 95/8201    

12 resistance genes are found

Gene IDGene TypeResistance ProfileDescription
ZP_04251264bl2a_iiipenicillin; Class A beta-lactamase. This enzyme breaks the beta-lactam antibiotic ring open and deactivates the molecule's antibacterial properites.

EEL18054bacabacitracin; Undecaprenyl pyrophosphate phosphatase, which consists in the sequestration of Undecaprenyl pyrophosphate.

ZP_04251927vanrbvancomycin; VanB type vancomycin resistance operon genes, which can synthesize peptidoglycan with modified C-terminal D-Ala-D-Ala to D-alanine--D-lactate.

ZP_04250264bacabacitracin; Undecaprenyl pyrophosphate phosphatase, which consists in the sequestration of Undecaprenyl pyrophosphate.

ZP_04250840fosbfosfomycin; Glutathione transferase, metalloglutathione transferase which confers resistance to fosfomycin by catalyzing the addition of glutathione to fosfomycin

ZP_04252176bl2a_1penicillin; Class A beta-lactamase. This enzyme breaks the beta-lactam antibiotic ring open and deactivates the molecule's antibacterial properites.

EEL16398vanrbvancomycin; VanB type vancomycin resistance operon genes, which can synthesize peptidoglycan with modified C-terminal D-Ala-D-Ala to D-alanine--D-lactate.

EEL19106bacabacitracin; Undecaprenyl pyrophosphate phosphatase, which consists in the sequestration of Undecaprenyl pyrophosphate.

ZP_04249185bacabacitracin; Undecaprenyl pyrophosphate phosphatase, which consists in the sequestration of Undecaprenyl pyrophosphate.

EEL17015bl2a_iiipenicillin; Class A beta-lactamase. This enzyme breaks the beta-lactam antibiotic ring open and deactivates the molecule's antibacterial properites.

EEL17450fosbfosfomycin; Glutathione transferase, metalloglutathione transferase which confers resistance to fosfomycin by catalyzing the addition of glutathione to fosfomycin

EEL16184bl2a_1penicillin; Class A beta-lactamase. This enzyme breaks the beta-lactam antibiotic ring open and deactivates the molecule's antibacterial properites.