A conserved residue in the histidine kinase BceS tunes bacitracin stress responses in Bacillus subtilis
Abstract
Two-component systems regulate bacterial responses through histidine kinases, where the majority act as both a kinase and a phosphatase. In Bacillus subtilis, the BceRS-BceAB system mediates bacitracin resistance, but it is unknown whether its histidine kinase, BceS, also functions as a phosphatase. Here, we identify the conserved motif within the BceS DHp domain and show that Thr-128 contributes to maintaining kinase-phosphatase balance. Substitutions at this site impaired BceS signalling and bacitracin resistance. Our findings demonstrate that in BceS, Thr-128 is important for proper BceAB regulation.
Fields of Study & Subjects
Bacterial Genetics and Biotechnology
Bacterial biofilms and quorum sensing
Enzyme Structure and Function
Publication details
- Journal / source
- Access Microbiology
- Publisher
- Microbiology Society
- Volume
- 8
- Issue
- 8
- Publication date
- 1 August 2026
- Language
- EN