ARDB-Antibiotic Resistance Genes Database

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Your Query:     Database: Resistance Gene(ALL)    Species: Bacillus cereus m1550    

12 resistance genes are found

Gene IDGene TypeResistance ProfileDescription
EEK88495bl2a_1penicillin; Class A beta-lactamase. This enzyme breaks the beta-lactam antibiotic ring open and deactivates the molecule's antibacterial properites.

ZP_04276921bacabacitracin; Undecaprenyl pyrophosphate phosphatase, which consists in the sequestration of Undecaprenyl pyrophosphate.

EEK89432bl2a_iiipenicillin; Class A beta-lactamase. This enzyme breaks the beta-lactam antibiotic ring open and deactivates the molecule's antibacterial properites.

EEK90314bacabacitracin; Undecaprenyl pyrophosphate phosphatase, which consists in the sequestration of Undecaprenyl pyrophosphate.

ZP_04281833aph3iagentamincin_b; kanamycin; lividomycin; neomycin; paromomycin; ribostamycin; Aminoglycoside O-phosphotransferase, which modifies aminoglycosides by phosphorylation.

EEK89799fosbfosfomycin; Glutathione transferase, metalloglutathione transferase which confers resistance to fosfomycin by catalyzing the addition of glutathione to fosfomycin

ZP_04277914bacabacitracin; Undecaprenyl pyrophosphate phosphatase, which consists in the sequestration of Undecaprenyl pyrophosphate.

ZP_04279826bl2a_1penicillin; Class A beta-lactamase. This enzyme breaks the beta-lactam antibiotic ring open and deactivates the molecule's antibacterial properites.

EEK91370bacabacitracin; Undecaprenyl pyrophosphate phosphatase, which consists in the sequestration of Undecaprenyl pyrophosphate.

ZP_04278512fosbfosfomycin; Glutathione transferase, metalloglutathione transferase which confers resistance to fosfomycin by catalyzing the addition of glutathione to fosfomycin

EEK86461aph3iagentamincin_b; kanamycin; lividomycin; neomycin; paromomycin; ribostamycin; Aminoglycoside O-phosphotransferase, which modifies aminoglycosides by phosphorylation.

ZP_04278944bl2a_iiipenicillin; Class A beta-lactamase. This enzyme breaks the beta-lactam antibiotic ring open and deactivates the molecule's antibacterial properites.