BRXB_BACSU
ID BRXB_BACSU Reviewed; 145 AA.
AC P54534;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Bacilliredoxin BrxB {ECO:0000303|PubMed:24313874};
DE Short=Brx-B {ECO:0000303|PubMed:24313874};
DE AltName: Full=Dithiol bacilliredoxin {ECO:0000303|PubMed:24313874};
DE AltName: Full=UPF0403 protein YqiW;
GN Name=brxB {ECO:0000303|PubMed:24313874};
GN Synonyms=yqiW {ECO:0000303|PubMed:24313874}; OrderedLocusNames=BSU23990;
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 / JH642;
RX PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA Kobayashi Y.;
RT "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT Bacillus subtilis genome containing the skin element and many sporulation
RT genes.";
RL Microbiology 142:3103-3111(1996).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=7961792; DOI=10.1016/s0021-9258(18)46956-6;
RA Ahmed M., Borsch C.M., Taylor S.S., Vazquez-Laslop N., Neyfakh A.A.;
RT "A protein that activates expression of a multidrug efflux transporter upon
RT binding the transporter substrates.";
RL J. Biol. Chem. 269:28506-28513(1994).
RN [4]
RP PROTEIN SEQUENCE OF 42-60, FUNCTION, INDUCTION, PTM, IDENTIFICATION BY MASS
RP SPECTROMETRY, DISRUPTION PHENOTYPE, MOTIF, ACTIVE SITE, POST-TRANSLATIONAL
RP MODIFICATION AT CYS-52, DISULFIDE BOND, AND MUTAGENESIS OF CYS-52 AND
RP CYS-54.
RX PubMed=24313874; DOI=10.1089/ars.2013.5327;
RA Gaballa A., Chi B.K., Roberts A.A., Becher D., Hamilton C.J., Antelmann H.,
RA Helmann J.D.;
RT "Redox regulation in Bacillus subtilis: The bacilliredoxins BrxA(YphP) and
RT BrxB(YqiW) function in de-bacillithiolation of S-bacillithiolated OhrR and
RT MetE.";
RL Antioxid. Redox Signal. 21:357-367(2014).
RN [5]
RP FUNCTION, INTERACTION WITH BRXC, PTM, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
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 dithiol bacilliredoxin, which
CC debacillithiolates (removes BSH) the S-bacillithiolated OhrR (OhrR-SSB)
CC in vitro and in vivo NaOCl-generated S-bacillithiolated MetE (MetE-
CC SSB). Involved in maintaining redox homeostasis in response to
CC disulfide stress conditions. {ECO:0000269|PubMed:24313874,
CC ECO:0000269|PubMed:33722570}.
CC -!- SUBUNIT: Interacts with BrxC. {ECO:0000269|PubMed:33722570}.
CC -!- INDUCTION: Expression is up-regulated by cumene hydroperoxide (CHP).
CC {ECO:0000269|PubMed:24313874}.
CC -!- PTM: N-terminal Cys of the CXC active site motif can react with
CC bacillithiol (BSH) to form mixed disulfides. S-bacillithiolation
CC protects Cys residues against overoxidation by acting as a redox switch
CC in response to oxidative stress. {ECO:0000269|PubMed:24313874,
CC ECO:0000269|PubMed:33722570}.
CC -!- DISRUPTION PHENOTYPE: Sensitive to cumene hydroperoxide (CHP) as
CC indicated by growth inhibition assay. No effect on growth after NaOCl
CC treatment. {ECO:0000269|PubMed:7961792}.
CC -!- SIMILARITY: Belongs to the bacilliredoxin family.
CC {ECO:0000305|PubMed:24313874}.
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DR EMBL; D84432; BAA12603.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14330.1; -; Genomic_DNA.
DR EMBL; L25604; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; E69962; E69962.
DR RefSeq; NP_390279.1; NC_000964.3.
DR RefSeq; WP_003226477.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P54534; -.
DR SMR; P54534; -.
DR STRING; 224308.BSU23990; -.
DR jPOST; P54534; -.
DR PaxDb; P54534; -.
DR PRIDE; P54534; -.
DR EnsemblBacteria; CAB14330; CAB14330; BSU_23990.
DR GeneID; 64304188; -.
DR GeneID; 938683; -.
DR KEGG; bsu:BSU23990; -.
DR PATRIC; fig|224308.179.peg.2613; -.
DR eggNOG; ENOG502ZBVN; Bacteria.
DR OMA; HHIEGRP; -.
DR PhylomeDB; P54534; -.
DR BioCyc; BSUB:BSU23990-MON; -.
DR PRO; PR:P54534; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR009474; YphP/YqiW.
DR PANTHER; PTHR40052; PTHR40052; 1.
DR Pfam; PF06491; Disulph_isomer; 1.
DR TIGRFAMs; TIGR04191; YphP_YqiW; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Oxidoreductase;
KW Redox-active center; Reference proteome.
FT CHAIN 1..145
FT /note="Bacilliredoxin BrxB"
FT /id="PRO_0000049827"
FT MOTIF 52..54
FT /note="CXC active site motif"
FT /evidence="ECO:0000269|PubMed:24313874"
FT ACT_SITE 52
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:24313874"
FT ACT_SITE 54
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:24313874"
FT MOD_RES 52
FT /note="S-bacillithiol cysteine disulfide"
FT /evidence="ECO:0000269|PubMed:24313874"
FT DISULFID 52..54
FT /note="Redox-active"
FT /evidence="ECO:0000269|PubMed:24313874"
FT MUTAGEN 52
FT /note="C->A: Loss of debacillithiolation of the S-
FT bacillithiolated OhrR (OhrR-SSB) by the NaBH(4)-reduced
FT form of this protein in vitro. Loss of regeneration of
FT active OhrR with DNA-binding activity in vitro. Loss of
FT debacillithiolation of in vivo NaOCl-generated S-
FT bacillithiolated MetE (MetE-SSB)."
FT /evidence="ECO:0000269|PubMed:24313874"
FT MUTAGEN 54
FT /note="C->A: Accumulation of S-bacillithiolated form due to
FT lack of this resolving cysteine residue.
FT Debacillithiolation of the S-bacillithiolated OhrR (OhrR-
FT SSB) without the prior NaBH(4) reduction of this protein in
FT vitro. Regenerates active OhrR with DNA-binding activity,
FT but unable to activate the S-cysteinyl cysteine modified
FT form of OhrR (OhrR-SSCys) in vitro. Debacillithiolation of
FT in vivo NaOCl-generated S-bacillithiolated MetE (MetE-
FT SSB)."
FT /evidence="ECO:0000269|PubMed:24313874"
SQ SEQUENCE 145 AA; 16196 MW; 612994D34B9237A9 CRC64;
MNMDFNLFMN DIVRQARQEI TAAGYTELKT AEEVDEALTK KGTTLVMVNS VCGCAGGIAR
PAAYHSVHYD KRPDQLVTVF AGQDKEATAR ARDYFEGYPP SSPSFAILKD GKIMKMVERH
EIEGHEPMAV VAKLQEAFEE YCEEV
