ID   BDBC2_BACAN             Reviewed;         140 AA.
AC   Q8KYH8; Q9X395;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 126.
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=pXO1-139, BXA0208, GBAA_pXO1_0208;
OS   Bacillus anthracis.
OG   Plasmid pXO1.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1392;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sterne;
RX   PubMed=10515943; DOI=10.1128/jb.181.20.6509-6515.1999;
RA   Okinaka R.T., Cloud K., Hampton O., Hoffmaster A.R., Hill K.K., Keim P.,
RA   Koehler T.M., Lamke G., Kumano S., Mahillon J., Manter D., Martinez Y.,
RA   Ricke D., Svensson R., Jackson P.J.;
RT   "Sequence and organization of pXO1, the large Bacillus anthracis plasmid
RT   harboring the anthrax toxin genes.";
RL   J. Bacteriol. 181:6509-6515(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Ames / isolate Florida / A2012;
RX   PubMed=12004073; DOI=10.1126/science.1071837;
RA   Read T.D., Salzberg S.L., Pop M., Shumway M.F., Umayam L., Jiang L.,
RA   Holtzapple E., Busch J.D., Smith K.L., Schupp J.M., Solomon D., Keim P.,
RA   Fraser C.M.;
RT   "Comparative genome sequencing for discovery of novel polymorphisms in
RT   Bacillus anthracis.";
RL   Science 296:2028-2033(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames ancestor;
RX   PubMed=18952800; DOI=10.1128/jb.01347-08;
RA   Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA   Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT   "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL   J. Bacteriol. 191:445-446(2009).
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAD32443.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF065404; AAD32443.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE011190; AAM26150.1; -; Genomic_DNA.
DR   EMBL; AE017336; AAT35497.1; -; Genomic_DNA.
DR   PIR; B59108; B59108.
DR   RefSeq; NP_052834.1; NC_001496.1.
DR   RefSeq; WP_003171436.1; NZ_VTZH01000012.1.
DR   RefSeq; WP_010890036.1; NC_001496.1.
DR   AlphaFoldDB; Q8KYH8; -.
DR   SMR; Q8KYH8; -.
DR   EnsemblBacteria; AAT35497; AAT35497; GBAA_pXO1_0208.
DR   GeneID; 45025537; -.
DR   KEGG; bar:GBAA_pXO1_0208; -.
DR   HOGENOM; CLU_128688_0_0_9; -.
DR   OMA; WVNYFGF; -.
DR   Proteomes; UP000000594; Plasmid pXO1.
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; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..140
FT                   /note="Probable disulfide formation protein C 2"
FT                   /id="PRO_0000059371"
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..134
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   140 AA;  16023 MW;  F64379113546ED8F CRC64;
     MTIIRKYHIA IAWTIATSAM LISLIFSEWM KLPPCDLCWY QRMAMYPLVL ILGIGMYRKD
     SNVSIYAFPF ACIGLIISVY QITIQAFPTS EMKICSVGVS CTENYLNLFG FISIPMLSFV
     GFLAIIILLY INQIKRQKNK