ID BRXC_BACSU Reviewed; 108 AA. AC P39914; A0A6M4JNQ9; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 22-FEB-2023, entry version 115. DE RecName: Full=Monothiol bacilliredoxin BrxC {ECO:0000303|PubMed:33722570}; DE Short=Monothiol Brx-C {ECO:0000305}; DE AltName: Full=Bacillithiol system redox-active protein YtxJ {ECO:0000312|EMBL:QJP89694.1}; DE AltName: Full=ORF2; DE AltName: Full=ORF3; GN Name=brxC {ECO:0000303|PubMed:33722570}; GN Synonyms=ytxJ {ECO:0000303|PubMed:33722570, ECO:0000312|EMBL:QJP89694.1}; GN OrderedLocusNames=BSU29760; GN ORFNames=HIR78_17325 {ECO:0000312|EMBL:QJP89694.1}; OS Bacillus subtilis (strain 168). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=224308; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168; RA Bolotin A.P., Khazak V.E., Ratmanova K.I., Yomantas Y.I., Kozlov Y.I.; RL Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168; RX PubMed=9387221; DOI=10.1099/00221287-143-11-3431; RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.; RT "Sequencing and functional annotation of the Bacillus subtilis genes in the RT 200 kb rrnB-dnaB region."; RL Microbiology 143:3431-3441(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K., RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., RA Yoshikawa H., Danchin A.; RT "The complete genome sequence of the Gram-positive bacterium Bacillus RT subtilis."; RL Nature 390:249-256(1997). RN [4] {ECO:0000312|EMBL:QJP89694.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168 {ECO:0000312|EMBL:QJP89694.1}; RA Dragos A., Kovacs A.T.; RT "Phage recombination drives evolution of spore-forming Bacilli."; RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56. RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB RC 3610 / NRRL NRS-744 / VKM B-501; RX PubMed=8733232; DOI=10.1111/j.1365-2958.1996.tb02621.x; RA Varon D., Brody M.S., Price C.W.; RT "Bacillus subtilis operon under the dual control of the general stress RT transcription factor sigma B and the sporulation transcription factor sigma RT H."; RL Mol. Microbiol. 20:339-350(1996). RN [6] RP FUNCTION, INTERACTION WITH ABRB; BDHA; BDR; BRXB; FOLD; GAPA; GAPB; GATA; RP PFKA; PYRAA; PYRAB; PYRE; PYRG; PYRH; RPSB; RPSK; RPSL; SALA; SUCC; TUF AND RP YTSJ, PTM, DISRUPTION PHENOTYPE, POST-TRANSLATIONAL MODIFICATION AT CYS-31, RP MUTAGENESIS OF CYS-31, AND 3D-STRUCTURE MODELING. RC STRAIN=168 / CU1065 {ECO:0000303|PubMed:33722570}; RX PubMed=33722570; DOI=10.1016/j.redox.2021.101935; RA Gaballa A., Su T.T., Helmann J.D.; RT "The Bacillus subtilis monothiol bacilliredoxin BrxC (YtxJ) and the Bdr RT (YpdA) disulfide reductase reduce S-bacillithiolated proteins."; RL Redox Biol. 42:101935-101935(2021). CC -!- FUNCTION: S-bacillithiolation is the formation of mixed disulfide bonds CC between protein thiols and the general thiol reductant bacillithiol CC (BSH) under oxidative stress. BSH is an equivalent of glutathione (GSH) CC in Firmicutes. This protein is a monothiol bacilliredoxin, which CC debacillithiolates (removes BSH) the S-bacillithiolated glyceraldehyde- CC 3-phosphate dehydrogenases (GAPDHs) GapA and GapB in vivo and probably CC a number of other oxidized cytosolic proteins. Debacillithiolates the CC S-bacillithiolated Bdr (Bdr-SSB) and BrxB (BrxB-SSB) in vitro. Involved CC in maintaining redox homeostasis in response to disulfide stress CC conditions. {ECO:0000269|PubMed:33722570}. CC -!- SUBUNIT: Interacts with AbrB, BdhA, Bdr, BrxB, FolD, GapA, GapB, GatA, CC PfkA, PyrAA, PyrAB, PyrE, PyrG, PyrH, RpsB, RpsK, RpsL, SalA, SucC, Tuf CC and YtsJ. {ECO:0000269|PubMed:33722570}. CC -!- PTM: Cys can react with bacillithiol (BSH) to form mixed disulfides. S- CC bacillithiolation protects Cys residues against overoxidation by acting CC as a redox switch in response to oxidative stress. CC {ECO:0000269|PubMed:33722570}. CC -!- DISRUPTION PHENOTYPE: Cells lacking the operon including this gene CC (ytxGH-brxC) have increased S-bacillithiolation of glyceraldehyde-3- CC phosphate dehydrogenases (GAPDHs) GapA and GapB in cells with increased CC basal levels of oxidative stress due to concomitant deletion of genes CC encoding for catalase (katA) and alkyl hydroperoxide reductase (ahpCF). CC {ECO:0000269|PubMed:33722570}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X65945; CAA46762.1; -; Genomic_DNA. DR EMBL; AF008220; AAC00297.1; -; Genomic_DNA. DR EMBL; AL009126; CAB14954.1; -; Genomic_DNA. DR EMBL; CP052842; QJP89694.1; -; Genomic_DNA. DR EMBL; L31845; AAB40046.1; -; Genomic_DNA. DR PIR; S21420; S21420. DR RefSeq; NP_390854.1; NC_000964.3. DR RefSeq; WP_003229280.1; NZ_JNCM01000036.1. DR AlphaFoldDB; P39914; -. DR SMR; P39914; -. DR STRING; 224308.BSU29760; -. DR PaxDb; P39914; -. DR EnsemblBacteria; CAB14954; CAB14954; BSU_29760. DR GeneID; 937308; -. DR KEGG; bsu:BSU29760; -. DR PATRIC; fig|224308.179.peg.3234; -. DR eggNOG; COG3118; Bacteria. DR OMA; KHSTRCS; -. DR OrthoDB; 677051at2; -. DR BioCyc; BSUB:BSU29760-MON; -. DR Proteomes; UP000001570; Chromosome. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0061770; F:translation elongation factor binding; IPI:UniProtKB. DR Gene3D; 3.40.30.10; Glutaredoxin; 1. DR InterPro; IPR022551; BrxC. DR InterPro; IPR036249; Thioredoxin-like_sf. DR Pfam; PF11009; DUF2847; 1. DR SUPFAM; SSF52833; Thioredoxin-like; 1. DR TIGRFAMs; TIGR04019; B_thiol_YtxJ; 1. PE 1: Evidence at protein level; KW Oxidoreductase; Redox-active center; Reference proteome. FT CHAIN 1..108 FT /note="Monothiol bacilliredoxin BrxC" FT /id="PRO_0000049906" FT MOD_RES 31 FT /note="S-bacillithiol cysteine disulfide" FT /evidence="ECO:0000269|PubMed:33722570" FT MUTAGEN 31 FT /note="C->A: Loss of debacillithiolation of S- FT bacillithiolated Bdr (Bdr-SSB)." FT /evidence="ECO:0000269|PubMed:33722570" SQ SEQUENCE 108 AA; 12402 MW; D8F03DD68E79AF38 CRC64; MAKQLIQSEE EFKRIAEQEG VFVFLKHSTT CPISQAAFHE FDAFANQHED VPAYYLQVQE ARPLSNFIAE TYGVKHESPQ IFIIQNGEVK WHTSHSQITE AAIEQHLS //