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Updated: Aug 16, 2026

Recombinant Protein Expression, Crystallization, and Biophysical Studies of a Bacillus-conserved Nucleotide Pyrophosphorylase, BcMazG
Published on: May 16, 2017
A conserved residue in the histidine kinase BceS tunes bacitracin stress responses in Bacillus subtilis
Kate Gridley1,2, Alan Koh1,2
1Department of Life Sciences, University of Bath, Bath, UK.
Abstract:
Two-component systems regulate bacterial responses through histidine kinases (HKs), 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 HK, 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.
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