ID   BDBC2_BACC1             Reviewed;         139 AA.
AC   P61777;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Probable disulfide formation protein C 2;
DE   AltName: Full=Disulfide oxidoreductase C 2;
DE   AltName: Full=Thiol-disulfide oxidoreductase C 2;
GN   Name=bdbC2; OrderedLocusNames=BCE_A0144;
OS   Bacillus cereus (strain ATCC 10987 / NRS 248).
OG   Plasmid pBc10987.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE017195; AAS44994.1; -; Genomic_DNA.
DR   RefSeq; WP_000454806.1; NC_005707.1.
DR   AlphaFoldDB; P61777; -.
DR   EnsemblBacteria; AAS44994; AAS44994; BCE_A0144.
DR   KEGG; bca:BCE_A0144; -.
DR   HOGENOM; CLU_128688_0_0_9; -.
DR   OMA; WVNYFGF; -.
DR   Proteomes; UP000002527; Plasmid pBc10987.
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; Plasmid; Redox-active center; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..139
FT                   /note="Probable disulfide formation protein C 2"
FT                   /id="PRO_0000059373"
FT   TRANSMEM        6..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        40..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        66..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        110..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DISULFID        35..38
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
FT   DISULFID        95..101
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   139 AA;  16208 MW;  99C4186B81644EAE CRC64;
     MEWIRKYHIA IAWMIATSAM LISLFFSEWM KLPPCDLCWY QRMAMYPLVL ILGIGMYRKD
     PRVSMYAFPF TCIGLILSVY QITIQAFPIN EMKICSVGVS CTEDYLNLFG FISIPMLSFI
     GFLVIIILIY IESDRETKE