BDR_BACSU
ID BDR_BACSU Reviewed; 324 AA.
AC P50736; A0A6M3ZIP2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Bacilliredoxin reductase Bdr {ECO:0000303|PubMed:33722570};
DE EC=1.8.1.- {ECO:0000269|PubMed:33722570};
DE AltName: Full=Bacillithiol-disulfide reductase {ECO:0000303|PubMed:33722570};
DE Short=BSSB reductase {ECO:0000303|PubMed:33722570};
DE AltName: Full=NADPH-dependent disulfide oxidoreductase {ECO:0000303|PubMed:33722570};
DE AltName: Full=Thioredoxin reductase-like flavoprotein {ECO:0000303|PubMed:33722570};
DE AltName: Full=YpdA family putative bacillithiol disulfide reductase {ECO:0000312|EMBL:QJP89022.1};
GN Name=bdr {ECO:0000303|PubMed:33722570};
GN Synonyms=ypdA {ECO:0000303|PubMed:33722570, ECO:0000312|EMBL:QJP89022.1};
GN OrderedLocusNames=BSU22950;
GN ORFNames=HIR78_13750 {ECO:0000312|EMBL:QJP89022.1};
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 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=8760912; DOI=10.1099/13500872-142-8-2005;
RA Sorokin A.V., Azevedo V., Zumstein E., Galleron N., Ehrlich S.D.,
RA Serror P.;
RT "Sequence analysis of the Bacillus subtilis chromosome region between the
RT serA and kdg loci cloned in a yeast artificial chromosome.";
RL Microbiology 142:2005-2016(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 SEQUENCE REVISION TO 4.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4] {ECO:0000312|EMBL:QJP89022.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168 {ECO:0000312|EMBL:QJP89022.1};
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 FUNCTION, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH BRXC, PTM,
RP IDENTIFICATION BY MASS SPECTROMETRY, POST-TRANSLATIONAL MODIFICATION AT
RP CYS-220, MUTAGENESIS OF CYS-14; CYS-122 AND CYS-220, AND 3D-STRUCTURE
RP 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 NADPH-dependent bacilliredoxin
CC reductase, which debacillithiolates (removes BSH) the S-
CC bacillithiolated BrxB (BrxB-SSB), and to a lesser extent BrxC (BrxC-
CC SSB). Involved in a redox cascade increasing the efficacy of BrxB
CC function by reducing BrxB-SSB and thus reactivating it. Has NADPH-
CC dependent oxidase activity under aerobic conditions producing hydrogen
CC peroxide (H(2)O(2)). {ECO:0000269|PubMed:33722570}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:33722570};
CC -!- SUBUNIT: Interacts with BrxC. {ECO:0000269|PubMed:33722570}.
CC -!- PTM: C-terminal Cys can react with bacillithiol (BSH) to form mixed
CC disulfides. S-bacillithiolation protects Cys residues against
CC overoxidation by acting as a redox switch in response to oxidative
CC stress. {ECO:0000269|PubMed:33722570}.
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DR EMBL; L47648; AAC83954.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14211.2; -; Genomic_DNA.
DR EMBL; CP052842; QJP89022.1; -; Genomic_DNA.
DR PIR; A69934; A69934.
DR RefSeq; NP_390176.2; NC_000964.3.
DR RefSeq; WP_004399008.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P50736; -.
DR SMR; P50736; -.
DR STRING; 224308.BSU22950; -.
DR jPOST; P50736; -.
DR PaxDb; P50736; -.
DR PRIDE; P50736; -.
DR EnsemblBacteria; CAB14211; CAB14211; BSU_22950.
DR GeneID; 938977; -.
DR KEGG; bsu:BSU22950; -.
DR PATRIC; fig|224308.179.peg.2502; -.
DR eggNOG; COG0492; Bacteria.
DR InParanoid; P50736; -.
DR OMA; KMGQPNR; -.
DR PhylomeDB; P50736; -.
DR BioCyc; BSUB:BSU22950-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0004497; F:monooxygenase activity; IBA:GO_Central.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR023856; Bacillithiol_biosynth_YpdA.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR04018; Bthiol_YpdA; 1.
PE 1: Evidence at protein level;
KW Flavoprotein; Oxidoreductase; Redox-active center; Reference proteome.
FT CHAIN 1..324
FT /note="Bacilliredoxin reductase Bdr"
FT /id="PRO_0000049684"
FT MOD_RES 220
FT /note="S-bacillithiol cysteine disulfide"
FT /evidence="ECO:0000269|PubMed:33722570"
FT MUTAGEN 14
FT /note="C->A: Retains NADPH-dependent oxidase activity under
FT aerobic conditions, but at a lower level. No effect on S-
FT bacillithiolation. Decreased bacilliredoxin reductase
FT activity. Decreased NADPH-dependent oxidase activity under
FT aerobic conditions; when associated with A-122 or with A-
FT 122 and A-220. Loss of bacilliredoxin reductase activity;
FT when associated with A-122 and A-220."
FT /evidence="ECO:0000269|PubMed:33722570"
FT MUTAGEN 122
FT /note="C->A: Retains NADPH-dependent oxidase activity under
FT aerobic conditions. No effect on S-bacillithiolation.
FT Decreased bacilliredoxin reductase activity. Decreased
FT NADPH-dependent oxidase activity under aerobic conditions;
FT when associated with A-14 or with A-14 and A-220. Loss of
FT bacilliredoxin reductase activity; when associated with A-
FT 14 and A-220."
FT /evidence="ECO:0000269|PubMed:33722570"
FT MUTAGEN 220
FT /note="C->A: Retains NADPH-dependent oxidase activity under
FT aerobic conditions. Loss of S-bacillithiolation. Decreased
FT bacilliredoxin reductase activity. Decreased NADPH-
FT dependent oxidase activity under aerobic conditions; when
FT associated with A-14 or with A-14 and A-122. Loss of
FT bacilliredoxin reductase activity; when associated with A-
FT 14 and A-122."
FT /evidence="ECO:0000269|PubMed:33722570"
FT CONFLICT 4
FT /note="E -> G (in Ref. 1; AAC83954)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 324 AA; 36409 MW; 290D0C9BB8369171 CRC64;
MIQEKAIIIG GGPCGLSAAI HLKQIGIDAL VIEKGNVVNS IYNYPTHQTF FSSSEKLEIG
DVAFITENRK PVRIQALSYY REVVKRKNIR VNAFEMVRKV TKTQNNTFVI ETSKETYTTP
YCIIATGYYD HPNYMGVPGE DLPKVFHYFK EGHPYFDKDV VVIGGKNSSV DAALELVKSG
ARVTVLYRGN EYSPSIKPWI LPEFEALVRN GTIRMEFGAC VEKITENEVV FRSGEKELIT
IKNDFVFAMT GYHPDHQFLE KIGVEIDKET GRPFFNEETM ETNVEGVFIA GVIAAGNNAN
EIFIENGRFH GGHIAAEIAK RENH
