ID   BDBC_DEIRA              Reviewed;         153 AA.
AC   Q9RWB5;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 118.
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=DR_0754;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS   4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
CC   -!- FUNCTION: Required for disulfide bond formation in some proteins.
CC       {ECO:0000255|HAMAP-Rule:MF_00287}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00287};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-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; AE000513; AAF10333.1; -; Genomic_DNA.
DR   PIR; F75478; F75478.
DR   RefSeq; NP_294478.1; NC_001263.1.
DR   RefSeq; WP_010887400.1; NZ_CP015081.1.
DR   AlphaFoldDB; Q9RWB5; -.
DR   STRING; 243230.DR_0754; -.
DR   EnsemblBacteria; AAF10333; AAF10333; DR_0754.
DR   KEGG; dra:DR_0754; -.
DR   PATRIC; fig|243230.17.peg.934; -.
DR   eggNOG; COG1495; Bacteria.
DR   HOGENOM; CLU_128688_0_0_0; -.
DR   InParanoid; Q9RWB5; -.
DR   OMA; WVNYFGF; -.
DR   OrthoDB; 1859420at2; -.
DR   Proteomes; UP000002524; Chromosome I.
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; Redox-active center; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..153
FT                   /note="Probable disulfide formation protein"
FT                   /id="PRO_0000059384"
FT   TRANSMEM        4..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
FT   TRANSMEM        38..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
FT   TRANSMEM        64..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
FT   TRANSMEM        117..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
FT   DISULFID        33..36
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
FT   DISULFID        93..101
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
SQ   SEQUENCE   153 AA;  16821 MW;  16FC185C019EC9E2 CRC64;
     MNRDTRLYLA WLVALAATLG SLYFSEIRHF NPCPLCWAQR IFMYPLAVIL GIAAFVGDHG
     VRRYVLPLAA LGLGFAIFQN LETWGFVQSI KACTVNAAAA CNTPWPVWGT SQDTLNRALT
     IPVLSMIAFA LILALLSWPR QRVTVPESAA VQG