The extracellular domain of <i>Sa</i>NSrFP binds bacitracin and allows the identification of new members of the BceAB transporter family.

ABSTRACT: Peptidoglycan serves as the first permeability barrier of Gram-positive bacteria. Intermediates of the peptidoglycan synthesis cycle are typical targets of antimicrobial compounds, including the peptide antibiotics nisin and bacitracin. In human pathogenic bacteria, gene clusters have been identified that are upregulated to confer resistance against these compounds. One such cluster found in Streptococcus agalactiae encodes a Bacitracin efflux (BceAB)-type ATP binding cassette transporter, SaNsrFP, and an associated two-component system, SaNsrRK. SaNsrFP has been shown to confer resistance against multiple antimicrobial peptides in vivo, with highest activity against bacitracin. Like other BceAB-type ABC-transporters, SaNsrFP features a large extra

SUBMITTER: Mammen C 

PROVIDER: S-EPMC12484072 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature