BDBC_COXBU
ID BDBC_COXBU Reviewed; 147 AA.
AC Q83D55;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
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};
GN OrderedLocusNames=CBU_0888;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(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; AE016828; AAO90418.1; -; Genomic_DNA.
DR RefSeq; NP_819904.1; NC_002971.3.
DR RefSeq; WP_010957868.1; NZ_CCYB01000044.1.
DR AlphaFoldDB; Q83D55; -.
DR STRING; 227377.CBU_0888; -.
DR EnsemblBacteria; AAO90418; AAO90418; CBU_0888.
DR GeneID; 1208781; -.
DR KEGG; cbu:CBU_0888; -.
DR PATRIC; fig|227377.7.peg.875; -.
DR eggNOG; COG1495; Bacteria.
DR HOGENOM; CLU_128688_0_0_6; -.
DR OMA; INWFGFI; -.
DR Proteomes; UP000002671; 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 inner membrane; Cell membrane; Chaperone; Disulfide bond;
KW Electron transport; Membrane; Oxidoreductase; Redox-active center;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..147
FT /note="Probable disulfide formation protein"
FT /id="PRO_0000059383"
FT TRANSMEM 9..28
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
FT TRANSMEM 43..62
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
FT TRANSMEM 69..86
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
FT TRANSMEM 115..139
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
FT DISULFID 38..41
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
FT DISULFID 99..106
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
SQ SEQUENCE 147 AA; 16792 MW; D1625F6E51D8F4DE CRC64;
MMVSRLLKNY SLYFAWLTAL IATLGSLYLS LVRHIPVCDL CWYQRVCIYP LTILLGIAAY
RTDRGVVKYA LPLVVLGFLF SVYQYLQQMI PGFAPINLCG STSPHCSEIH WEIFGFITLP
FLGMLATLIM SFFLIMAFYS LDKRLAN
