|CARD Short Name
|The almEFG operon is responsible for glycylation of lipid A as a mechanism of colistin resistance in Vibrio cholerae. Its mechanism involves transfer of a glycyl molecule to the carrier protein almF by almE followed by glycylation of lipid A by almG.
|AMR Gene Family
|polymyxin resistance operon
|antibiotic target alteration
|11 ontology terms | Show
+ process or component of antibiotic biology or chemistry
+ antibiotic molecule
+ peptide antibiotic [Drug Class]
+ lipopeptide antibiotic
+ mechanism of antibiotic resistance
+ determinant of antibiotic resistance
+ polymyxin antibiotic
+ antibiotic target alteration [Resistance Mechanism]
+ antibiotic resistance gene cluster, cassette, or operon
+ charge alteration conferring antibiotic resistance
|4 ontology terms | Show
|3 ontology terms | Show
Henderson JC, et al. 2014. ACS Chem Biol 9(10):2382-92 Antimicrobial peptide resistance of Vibrio cholerae results from an LPS modification pathway related to nonribosomal peptide synthetases. (PMID 25068415)
Prevalence of almEFG among the sequenced genomes, plasmids, and whole-genome shotgun assemblies available at NCBI or IslandViewer for 413 important pathogens (see methodological details and complete list of analyzed pathogens). Values reflect percentage of genomes, plasmids, genome islands, or whole-genome shotgun assemblies that have at least one hit to the AMR detection model. Default view includes percentages calculated based on Perfect plus Strict RGI hits. Select the checkbox to view percentages based on only Perfect matches to AMR reference sequences curated in CARD (note: this excludes resistance via mutation as references in protein variant models are often wild-type, sensitive sequences).
|No prevalence data
Model Name: almEFG
Model Description: The almEFG operon is responsible for glycylation of lipid A as a mechanism of colistin resistance in Vibrio cholerae. Its mechanism involves transfer of a glycyl molecule to the carrier protein almF by almE followed by glycylation of lipid A by almG.