ID   BDBC1_BACC1             Reviewed;         139 AA.
AC   P61776;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Probable disulfide formation protein C 1;
DE   AltName: Full=Disulfide oxidoreductase C 1;
DE   AltName: Full=Thiol-disulfide oxidoreductase C 1;
GN   Name=bdbC1; OrderedLocusNames=BCE_0823;
OS   Bacillus cereus (strain ATCC 10987 / NRS 248).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=222523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10987 / NRS 248;
RX   PubMed=14960714; DOI=10.1093/nar/gkh258;
RA   Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA   Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA   Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT   "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT   adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL   Nucleic Acids Res. 32:977-988(2004).
CC   -!- FUNCTION: Required for disulfide bond formation in some proteins.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the DsbB family. BdbC subfamily. {ECO:0000305}.
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DR   EMBL; AE017194; AAS39755.1; -; Genomic_DNA.
DR   RefSeq; WP_000532254.1; NC_003909.8.
DR   AlphaFoldDB; P61776; -.
DR   EnsemblBacteria; AAS39755; AAS39755; BCE_0823.
DR   GeneID; 59158581; -.
DR   KEGG; bca:BCE_0823; -.
DR   HOGENOM; CLU_128688_0_0_9; -.
DR   OMA; INWFGFI; -.
DR   Proteomes; UP000002527; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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: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   3: Inferred from homology;
KW   Cell membrane; Chaperone; Disulfide bond; Electron transport; Membrane;
KW   Oxidoreductase; Redox-active center; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..139
FT                   /note="Probable disulfide formation protein C 1"
FT                   /id="PRO_0000059372"
FT   TRANSMEM        8..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        42..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        68..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        113..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DISULFID        37..40
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
FT   DISULFID        99..104
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   139 AA;  15600 MW;  ECC27153C7A90D2A CRC64;
     MGREKKQEYA LFTAWGASFI ATLGSLYFSE IMKFEPCVLC WYQRIFMYPF VLWLGIAVVK
     KDYRIANYSL PIASIGACIS LYHYAIQKIA AFSAAGAACG RVPCTGEYIN WFGFVTIPFL
     ALIGFITIAV CSFIVIKNK