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BSH is an equivalent of glutathione (GSH) in Firmicutes. This protein is a dithiol bacilliredoxin, which debacillithiolates (removes BSH) the S-bacillithiolated OhrR (OhrR-SSB) in vitro and in vivo NaOCl-generated S-bacillithiolated MetE (MetE-SSB). Involved in maintaining redox homeostasis in response to disulfide stress conditions"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33722570"}],"value":"Interacts with BrxC"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24313874"}],"value":"Expression is up-regulated by cumene hydroperoxide (CHP)"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24313874"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33722570"}],"value":"N-terminal Cys of the CXC active site motif can react with bacillithiol (BSH) to form mixed disulfides. S-bacillithiolation protects Cys residues against overoxidation by acting as a redox switch in response to oxidative stress"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7961792"}],"value":"Sensitive to cumene hydroperoxide (CHP) as indicated by growth inhibition assay. No effect on growth after NaOCl treatment"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"24313874"}],"value":"Belongs to the bacilliredoxin family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":145,"modifier":"EXACT"}},"description":"Bacilliredoxin BrxB","featureId":"PRO_0000049827"},{"type":"Motif","location":{"start":{"value":52,"modifier":"EXACT"},"end":{"value":54,"modifier":"EXACT"}},"description":"CXC active site motif","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24313874"}]},{"type":"Active site","location":{"start":{"value":52,"modifier":"EXACT"},"end":{"value":52,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24313874"}]},{"type":"Active site","location":{"start":{"value":54,"modifier":"EXACT"},"end":{"value":54,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24313874"}]},{"type":"Modified residue","location":{"start":{"value":52,"modifier":"EXACT"},"end":{"value":52,"modifier":"EXACT"}},"description":"S-bacillithiol cysteine disulfide","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24313874"}]},{"type":"Disulfide bond","location":{"start":{"value":52,"modifier":"EXACT"},"end":{"value":54,"modifier":"EXACT"}},"description":"Redox-active","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24313874"}]},{"type":"Mutagenesis","location":{"start":{"value":52,"modifier":"EXACT"},"end":{"value":52,"modifier":"EXACT"}},"description":"Loss of debacillithiolation of the S-bacillithiolated OhrR (OhrR-SSB) by the NaBH(4)-reduced form of this protein in vitro. Loss of regeneration of active OhrR with DNA-binding activity in vitro. Loss of debacillithiolation of in vivo NaOCl-generated S-bacillithiolated MetE (MetE-SSB).","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24313874"}],"alternativeSequence":{"originalSequence":"C","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":54,"modifier":"EXACT"},"end":{"value":54,"modifier":"EXACT"}},"description":"Accumulation of S-bacillithiolated form due to lack of this resolving cysteine residue. Debacillithiolation of the S-bacillithiolated OhrR (OhrR-SSB) without the prior NaBH(4) reduction of this protein in vitro. Regenerates active OhrR with DNA-binding activity, but unable to activate the S-cysteinyl cysteine modified form of OhrR (OhrR-SSCys) in vitro. 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