BRXC_BACSU
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 03-AUG-2022, entry version 113.
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}.
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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 PRIDE; 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 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 InterPro; IPR022551; BrxC.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF11009; DUF2847; 1.
DR SUPFAM; SSF52833; SSF52833; 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
