BDBC_CHLTR
ID BDBC_CHLTR Reviewed; 135 AA.
AC O84179;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 119.
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=CT_176;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
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; AE001273; AAC67767.1; -; Genomic_DNA.
DR PIR; G71547; G71547.
DR RefSeq; NP_219680.1; NC_000117.1.
DR RefSeq; WP_009871522.1; NC_000117.1.
DR AlphaFoldDB; O84179; -.
DR STRING; 813.O172_00945; -.
DR EnsemblBacteria; AAC67767; AAC67767; CT_176.
DR GeneID; 884955; -.
DR KEGG; ctr:CT_176; -.
DR PATRIC; fig|272561.5.peg.190; -.
DR HOGENOM; CLU_128688_0_0_0; -.
DR InParanoid; O84179; -.
DR OMA; INWFGFI; -.
DR Proteomes; UP000000431; 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..135
FT /note="Probable disulfide formation protein"
FT /id="PRO_0000059382"
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..131
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 135 AA; 15005 MW; F0FFA07BB9B85E3A CRC64;
MIKHLRSYCL YLAWLFSCIG TLMSVYYSYI LNVEPCLLCY YQRICLFPLV VILGIAAYRE
DISIKIYTLP LALVGFGIAI YQVCLQEIPG MTLDICGKVS CSTKLFLLGF ITMPMASAAA
FCAIACLLVL ATKSK
