ID   DSBD_SODGM              Reviewed;         590 AA.
AC   Q2NW99;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   16-JUN-2009, entry version 34.
DE   RecName: Full=Thiol:disulfide interchange protein dsbD;
DE            EC=1.8.1.8;
DE   AltName: Full=Protein-disulfide reductase;
DE            Short=Disulfide reductase;
DE   Flags: Precursor;
GN   Name=dsbD; OrderedLocusNames=SG0301;
OS   Sodalis glossinidius (strain morsitans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Sodalis.
OX   NCBI_TaxID=343509;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16365377; DOI=10.1101/gr.4106106;
RA   Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K.,
RA   Hattori M., Aksoy S.;
RT   "Massive genome erosion and functional adaptations provide insights
RT   into the symbiotic lifestyle of Sodalis glossinidius in the tsetse
RT   host.";
RL   Genome Res. 16:149-156(2006).
CC   -!- FUNCTION: Required to facilitate the formation of correct
CC       disulfide bonds in some periplasmic proteins and for the assembly
CC       of the periplasmic c-type cytochromes. Acts by transferring
CC       electrons from cytoplasmic thioredoxin to the periplasm. This
CC       transfer involves a cascade of disulfide bond formation and
CC       reduction steps (By similarity).
CC   -!- CATALYTIC ACTIVITY: Protein dithiol + NAD(P)(+) = protein
CC       disulfide + NAD(P)H.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
CC       protein (By similarity).
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbD subfamily.
CC   -!- SIMILARITY: Contains 1 thioredoxin domain.
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DR   EMBL; AP008232; BAE73576.1; -; Genomic_DNA.
DR   RefSeq; YP_453981.1; -.
DR   GeneID; 3868569; -.
DR   GenomeReviews; AP008232_GR; SG0301.
DR   KEGG; sgl:SG0301; -.
DR   NMPDR; fig|343509.6.peg.709; -.
DR   HOGENOM; Q2NW99; -.
DR   OMA; Q2NW99; HTDEYFG.
DR   BioCyc; SGLO343509:SG0301-MON; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron carrier activity; IEA:HAMAP.
DR   GO; GO:0047134; F:protein-disulfide reductase activity; IEA:HAMAP.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0017004; P:cytochrome complex assembly; IEA:HAMAP.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   HAMAP; MF_00399; -; 1.
DR   InterPro; IPR003834; Cyt_c_assmbl_TM.
DR   InterPro; IPR017936; Thioredoxin-like.
DR   InterPro; IPR015467; Thioredoxin_core.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   PANTHER; PTHR10438; Trx; 1.
DR   Pfam; PF02683; DsbD; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Complete proteome;
KW   Cytochrome c-type biogenesis; Disulfide bond; Electron transport;
KW   Membrane; NAD; Oxidoreductase; Redox-active center; Signal;
KW   Transmembrane; Transport.
FT   SIGNAL        1     24       Potential.
FT   CHAIN        25    590       Thiol:disulfide interchange protein dsbD.
FT                                /FTId=PRO_0000304400.
FT   TRANSMEM    193    213       Potential.
FT   TRANSMEM    229    249       Potential.
FT   TRANSMEM    266    286       Potential.
FT   TRANSMEM    310    330       Potential.
FT   TRANSMEM    349    369       Potential.
FT   TRANSMEM    388    408       Potential.
FT   TRANSMEM    409    429       Potential.
FT   TRANSMEM    438    458       Potential.
FT   DOMAIN      457    590       Thioredoxin.
FT   DISULFID    128    134       Redox-active (By similarity).
FT   DISULFID    205    327       Redox-active (By similarity).
FT   DISULFID    505    508       Redox-active (By similarity).
SQ   SEQUENCE   590 AA;  64142 MW;  6D2389126F0E9D2A CRC64;
     MAQRRFTLIL LACLTCLPLL PAHAALFGNS HGNQFIPAEQ AFRFDFRQQG SQLTLSWDIH
     PGYYLYRQQI RLEPVNATLG AFTLPAGSRH HDEFYGDDVA IYRDELNITL PLAQAQNDSQ
     LRVTWQGCAE AGFCYPPETQ VIPLSAIAAA PPSGTGIGST ALIPAPPPAG GQGIITPAPP
     PQSNNLPFSP LWALLIGIGI AFTPCVLPMY PLISAVILGN RLQLSTARVL LLAVVYVMGM
     AITYTLLGVA VAAAGLQFQA VLQQPALLIG LAALFILLAL SMFGVFTLQL PSALQTHLAL
     WSNRQRQGTL PGVFIMGALA GLFCSPCTTA PLSAILLYIA QSGNLWFSGF TLWLYAVGMG
     IPLILVALFG HRLLPKRGPW MQQVKQGFGF VILALPVFLL ERVLGDSWGT RLWSLLGVAF
     FGWGFLLCLQ ARWRGARWLA VLMLGLTLIS ARPLQDWLWG APADMTSTTG AAPVFQPVQT
     LAQITQALNA APGKPVMLDL YADWCVACKE FDKYTFRDPA VVEQMSRFTL LQADVTANAP
     VQRMLLGQLQ VIGLPTILFF DSRGHEIPGS RLTGYMNAAD FTRHLRKLAP
//