ID   DSBD_YERPP              Reviewed;         595 AA.
AC   A4TRR6;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   16-JUN-2009, entry version 21.
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=YPDSF_3628;
OS   Yersinia pestis (strain Pestoides F).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Yersinia.
OX   NCBI_TaxID=386656;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Di Bartolo G., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Worsham P., Chu M.,
RA   Bearden S., Garcia E., Richardson P.;
RT   "Complete sequence of chromosome of Yersinia pestis Pestoides F.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000668; ABP41978.1; -; Genomic_DNA.
DR   RefSeq; YP_001164951.1; -.
DR   GeneID; 5062962; -.
DR   GenomeReviews; CP000668_GR; YPDSF_3628.
DR   KEGG; ypp:YPDSF_3628; -.
DR   OMA; A4TRR6; TITHILW.
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; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 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    595       Thiol:disulfide interchange protein dsbD.
FT                                /FTId=PRO_5000237106.
FT   TRANSMEM    197    217       Potential.
FT   TRANSMEM    233    253       Potential.
FT   TRANSMEM    270    290       Potential.
FT   TRANSMEM    311    331       Potential.
FT   TRANSMEM    332    352       Potential.
FT   TRANSMEM    353    373       Potential.
FT   TRANSMEM    384    404       Potential.
FT   TRANSMEM    411    431       Potential.
FT   TRANSMEM    435    455       Potential.
FT   DOMAIN      452    592       Thioredoxin.
FT   DISULFID    134    140       Redox-active (By similarity).
FT   DISULFID    209    331       Redox-active (By similarity).
FT   DISULFID    507    510       Redox-active (By similarity).
SQ   SEQUENCE   595 AA;  64506 MW;  D91ABB96DD6686C5 CRC64;
     MAQRFITLIL LLCSVLLAPH SAQSSLFGEN ASFGTKNSQS RFIPVDQAFA FDFHQQGDQL
     NLSWQIHPGY YLYRQQIKIV PQQAALGAFT LPEGITHHDE FYGEVEIFKQ QLTLKIPITQ
     AAEQASVSVT YQGCAEAGFC YPPETRVIPL DVVVAASTAS GTAAVNSSAT VNPPATTQPE
     GDATPVPSTL PFSPLWALLI GIGIAFTPCV LPMYPLISAV ILGREKPHSQ RRILILAVVY
     VQGMALTYTL LGLVVAAAGL QFQAALQHPY VLIGLSVLFV LLALSMFGLY SLQLPSSLQT
     RLTQWSNSQR GGSLAGVFAM GALAGLICSP CTTAPLSAIL LYIAQSGNML AGGGTLYLYA
     LGMGIPLVVV TLFGNKLIPR SGPWMQYVKE AFGFVILALP VFLLERVLGD VWGLRLWSLL
     AVAFFGWAFV LSLKAHAGWV RVCQLLLLAA LLIVARPLQD WAFNGNTQQN AVKHINFQPV
     ANLPQLQAVL AQAQGKPVML DLYADWCVAC KEFEKYTFSD DKVQRQLANT LLLQADVTAN
     NAEHATLLKK FNVLGLPTIL FFDSQGNEIT AARVTGFMDA AQFLQHLQNT PAVTK
//