Bacillithiol (BSH) functions as a general thiol reductant, analogous to glutathione, in a wide range of bacterial species. Bacilliredoxins reduce those proteins that are modified by disulfide bond formation with BSH (S-bacillithiolation) [[cite:PUB00100073]]. This entry represents BrxC from Bacillus subtilis (formerly known as YtxJ) and similar bacterial proteins related to BSH. BrxC is a monothiol bacilliredoxin responsible for the removal of BSH from oxidized cytosolic proteins. It can also debacillithiolate the mixed disulfide form of the bacilliredoxin BrxB [[cite:PUB00055031],[cite:PUB00100075]]. It has a similar fold to thioredoxin. The homologue in Deinococcus radiodurans, named AbxC, plays a role in the response to oxidative stress [[cite:PUB00100126]].
","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00100126":{"PMID":34356381,"ISBN":null,"volume":"10","issue":"7","year":2021,"title":"Atypical Bacilliredoxin AbxC Plays a Role in Responding to Oxidative Stress in Radiation-Resistant Bacterium Deinococcus radiodurans.","URL":null,"raw_pages":null,"medline_journal":"Antioxidants (Basel)","ISO_journal":"Antioxidants (Basel)","authors":["Jeong S","Jung JH","Kim MK","de Groot A","Blanchard L","Ryu S","Bahn YS","Lim S."],"DOI_URL":null},"PUB00100075":{"PMID":33722570,"ISBN":null,"volume":"42","issue":null,"year":2021,"title":"The Bacillus subtilis monothiol bacilliredoxin BrxC (YtxJ) and the Bdr (YpdA) disulfide reductase reduce S-bacillithiolated proteins.","URL":null,"raw_pages":"101935","medline_journal":"Redox Biol","ISO_journal":"Redox Biol","authors":["Gaballa A","Su TT","Helmann JD."],"DOI_URL":null},"PUB00055031":{"PMID":20308541,"ISBN":null,"volume":"107","issue":"14","year":2010,"title":"Biosynthesis and functions of bacillithiol, a major low-molecular-weight thiol in Bacilli.","URL":null,"raw_pages":"6482-6","medline_journal":"Proc Natl Acad Sci U S A","ISO_journal":"Proc. Natl. Acad. Sci. U.S.A.","authors":["Gaballa A","Newton GL","Antelmann H","Parsonage D","Upton H","Rawat M","Claiborne A","Fahey RC","Helmann JD."],"DOI_URL":"http://dx.doi.org/10.1073/pnas.1000928107"},"PUB00100073":{"PMID":28301954,"ISBN":null,"volume":"28","issue":"6","year":2018,"title":"The Role of Bacillithiol in Gram-Positive Firmicutes.","URL":null,"raw_pages":"445-462","medline_journal":"Antioxid Redox Signal","ISO_journal":"Antioxid Redox Signal","authors":["Chandrangsu P","Loi VV","Antelmann H","Helmann JD."],"DOI_URL":null}},"set_info":{"accession":"CL0172","name":"Thioredoxin"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":6,"interactions":0,"matches":3076,"pathways":0,"proteins":3076,"proteomes":2928,"sets":1,"structural_models":{"alphafold":1910},"structures":1,"taxa":3744},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":60,"alignment:full":1375},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"3iv4","name":"A putative oxidoreductase with a thioredoxin fold"}}}