BDBC_CHLCV
ID BDBC_CHLCV Reviewed; 136 AA.
AC Q822U2;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=CCA_00587;
OS Chlamydia caviae (strain ATCC VR-813 / DSM 19441 / 03DC25 / GPIC)
OS (Chlamydophila caviae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=227941;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-813 / DSM 19441 / 03DC25 / GPIC;
RX PubMed=12682364; DOI=10.1093/nar/gkg321;
RA Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T.,
RA Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A.,
RA Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O.,
RA Salzberg S.L., Hsia R.-C., McClarty G., Rank R.G., Bavoil P.M.,
RA Fraser C.M.;
RT "Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC):
RT examining the role of niche-specific genes in the evolution of the
RT Chlamydiaceae.";
RL Nucleic Acids Res. 31:2134-2147(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}.
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; AE015925; AAP05329.1; -; Genomic_DNA.
DR RefSeq; WP_011006544.1; NC_003361.3.
DR AlphaFoldDB; Q822U2; -.
DR STRING; 227941.CCA_00587; -.
DR EnsemblBacteria; AAP05329; AAP05329; CCA_00587.
DR KEGG; cca:CCA_00587; -.
DR eggNOG; COG1495; Bacteria.
DR HOGENOM; CLU_128688_0_0_0; -.
DR OMA; INWFGFI; -.
DR OrthoDB; 1859420at2; -.
DR Proteomes; UP000002193; 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 Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..136
FT /note="Probable disulfide formation protein"
FT /id="PRO_0000059379"
FT TRANSMEM 7..26
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
FT TRANSMEM 41..60
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
FT TRANSMEM 67..84
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
FT TRANSMEM 109..133
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
FT DISULFID 36..39
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
FT DISULFID 96..101
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
SQ SEQUENCE 136 AA; 15214 MW; 1427FE4AA8FCD8A3 CRC64;
MIRFLRNNAL YFAWLICSTG TVMSIYYSYL LNIEPCVLCY YQRICLFPLS IILGIATYRE
DNLVKIYALP LSITGMVIAV YQICLQEISG MTIDICGRVS CSTKLFVFGF ITVPMASALA
FCAISCLLIL SGSKKK
