ID   BDBC_PSERE              Reviewed;         144 AA.
AC   Q8GHM3;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Probable disulfide formation protein {ECO:0000255|HAMAP-Rule:MF_00287};
DE   AltName: Full=Disulfide oxidoreductase {ECO:0000255|HAMAP-Rule:MF_00287};
DE   AltName: Full=Thiol-disulfide oxidoreductase {ECO:0000255|HAMAP-Rule:MF_00287};
OS   Pseudomonas resinovorans.
OG   Plasmid pCAR1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=53412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CA10;
RX   PubMed=12547188; DOI=10.1016/s0022-2836(02)01400-6;
RA   Maeda K., Nojiri H., Shintani M., Yoshida T., Habe H., Omori T.;
RT   "Complete nucleotide sequence of carbazole/dioxin-degrading plasmid pCAR1
RT   in Pseudomonas resinovorans strain CA10 indicates its mosaicity and the
RT   presence of large catabolic transposon Tn4676.";
RL   J. Mol. Biol. 326:21-33(2003).
CC   -!- FUNCTION: Required for disulfide bond formation in some proteins.
CC       {ECO:0000255|HAMAP-Rule:MF_00287}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00287}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00287}.
CC   -!- SIMILARITY: Belongs to the DsbB family. BdbC subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00287}.
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DR   EMBL; AB088420; BAC41700.1; -; Genomic_DNA.
DR   RefSeq; NP_758722.1; NC_004444.1.
DR   RefSeq; WP_011078038.1; NC_004444.1.
DR   AlphaFoldDB; Q8GHM3; -.
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:InterPro.
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 inner membrane; Cell membrane; Chaperone; Disulfide bond;
KW   Electron transport; Membrane; Oxidoreductase; Plasmid; Redox-active center;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..144
FT                   /note="Probable disulfide formation protein"
FT                   /id="PRO_0000059386"
FT   TRANSMEM        10..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
FT   TRANSMEM        44..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
FT   TRANSMEM        70..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
FT   TRANSMEM        116..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
FT   DISULFID        39..42
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
FT   DISULFID        100..107
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
SQ   SEQUENCE   144 AA;  15638 MW;  F6B25AF1BF55C3EE CRC64;
     MNPQPSGMTW NLLLLTWLVA LISTLSALFI GEVMGQAPCV LCWFQRAFMF PLTVILAIAC
     YRSDFTVWRY ALPLTVIGAA LAFVHTLLYA GLIPQPIQPC TATGPSCSGA GMTLFGVVPL
     PALALFAFII IAILLIIIRR RTTP