BDBC_BACSU
ID BDBC_BACSU Reviewed; 138 AA.
AC O32217;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Disulfide bond formation protein C;
DE AltName: Full=Disulfide oxidoreductase C;
DE AltName: Full=Thiol-disulfide oxidoreductase C;
GN Name=bdbC; Synonyms=yvgU; OrderedLocusNames=BSU33470;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
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 [2]
RP IDENTIFICATION OF FUNCTION.
RC STRAIN=168;
RX PubMed=10455116; DOI=10.1074/jbc.274.35.24531;
RA Bolhuis A., Venema G., Quax W.J., Bron S., van Dijl J.M.;
RT "Functional analysis of paralogous thiol-disulfide oxidoreductases in
RT Bacillus subtilis.";
RL J. Biol. Chem. 274:24531-24538(1999).
RN [3]
RP DISRUPTION PHENOTYPE.
RC STRAIN=168 / BGSC1A1;
RX PubMed=11844773; DOI=10.1128/jb.184.5.1423-1429.2002;
RA Erlendsson L.S., Hederstedt L.;
RT "Mutations in the thiol-disulfide oxidoreductases BdbC and BdbD can
RT suppress cytochrome c deficiency of CcdA-defective Bacillus subtilis
RT cells.";
RL J. Bacteriol. 184:1423-1429(2002).
RN [4]
RP FUNCTION IN PRODUCTION OF COMGC.
RC STRAIN=168;
RX PubMed=11744713; DOI=10.1074/jbc.m111380200;
RA Meima R., Eschevins C., Fillinger S., Bolhuis A., Hamoen L.W., Dorenbos R.,
RA Quax W.J., van Dijl J.M., Provvedi R., Chen I., Dubnau D., Bron S.;
RT "The bdbDC operon of Bacillus subtilis encodes thiol-disulfide
RT oxidoreductases required for competence development.";
RL J. Biol. Chem. 277:6994-7001(2002).
RN [5]
RP FUNCTION IN PRODUCTION OF SUBLANCIN 168.
RC STRAIN=168;
RX PubMed=11872755; DOI=10.1074/jbc.m201158200;
RA Dorenbos R., Stein T., Kabel J., Bruand C., Bolhuis A., Bron S., Quax W.J.,
RA Van Dijl J.M.;
RT "Thiol-disulfide oxidoreductases are essential for the production of the
RT lantibiotic sublancin 168.";
RL J. Biol. Chem. 277:16682-16688(2002).
RN [6]
RP SUBCELLULAR LOCATION.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=20713508; DOI=10.1101/gad.1945010;
RA Lopez D., Kolter R.;
RT "Functional microdomains in bacterial membranes.";
RL Genes Dev. 24:1893-1902(2010).
CC -!- FUNCTION: Required for the stabilization, possibly via formation of a
CC disulfide bond, of the obligatory competence protein ComGC. Not
CC normally required for production of the secreted lantibiotic sublancin
CC 168, although it can partially substitute for BdbB when the latter is
CC absent. It may also be required for the stability of other secreted
CC proteins. Not required for sporulation. {ECO:0000269|PubMed:11744713,
CC ECO:0000269|PubMed:11872755}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20713508};
CC Multi-pass membrane protein {ECO:0000305}. Membrane raft
CC {ECO:0000269|PubMed:20713508}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Present in detergent-resistant membrane (DRM)
CC fractions that may be equivalent to eukaryotic membrane rafts; these
CC rafts include proteins involved in signaling, molecule trafficking and
CC protein secretion. {ECO:0000269|PubMed:20713508}.
CC -!- DEVELOPMENTAL STAGE: A late competence gene, expression is enhanced in
CC the presence of ComK.
CC -!- DISRUPTION PHENOTYPE: Cells partially restore cytochrome c oxidase
CC activity in a CcdA-deficient mutant, possibly because the bacteria can
CC no longer oxidize the two heme-binding thiol groups in apocytochrome c.
CC {ECO:0000269|PubMed:11844773}.
CC -!- SIMILARITY: Belongs to the DsbB family. BdbC subfamily. {ECO:0000305}.
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DR EMBL; AL009126; CAB15352.1; -; Genomic_DNA.
DR PIR; B70041; B70041.
DR RefSeq; NP_391227.1; NC_000964.3.
DR RefSeq; WP_003228417.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O32217; -.
DR SMR; O32217; -.
DR STRING; 224308.BSU33470; -.
DR PaxDb; O32217; -.
DR EnsemblBacteria; CAB15352; CAB15352; BSU_33470.
DR GeneID; 936042; -.
DR KEGG; bsu:BSU33470; -.
DR PATRIC; fig|224308.179.peg.3632; -.
DR eggNOG; COG1495; Bacteria.
DR InParanoid; O32217; -.
DR OMA; INWFGFI; -.
DR PhylomeDB; O32217; -.
DR BioCyc; BSUB:BSU33470-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR Gene3D; 1.20.1550.10; -; 1.
DR HAMAP; MF_00287; BdbC; 1.
DR InterPro; IPR003752; DiS_bond_form_DsbB/BdbC.
DR InterPro; IPR012187; Disulphide_bond_form_BdbC.
DR InterPro; IPR023380; DsbB-like_sf.
DR PANTHER; PTHR43469; PTHR43469; 1.
DR Pfam; PF02600; DsbB; 1.
DR PIRSF; PIRSF036659; BdbC; 1.
DR SUPFAM; SSF158442; SSF158442; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Chaperone; Competence; Disulfide bond; Electron transport;
KW Membrane; Oxidoreductase; Redox-active center; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..138
FT /note="Disulfide bond formation protein C"
FT /id="PRO_0000059376"
FT TRANSMEM 5..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DISULFID 34..37
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT DISULFID 95..101
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 138 AA; 15714 MW; 690A577185F8B6DB CRC64;
MKNRIVFLYA SWVVALIAML GSLYFSEIRK FIPCELCWYQ RILMYPLVLI LGIATFQGDT
RVKKYVLPMA IIGAFISIMH YLEQKVPGFS GIKPCVSGVP CSGQYINWFG FITIPFLALI
AFILIIIFMC LLKGEKSE
