ID   DSBD_COLP3              Reviewed;         608 AA.
AC   Q487R3;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 33.
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=CPS_0953;
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic
RT   analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
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; CP000083; AAZ24775.1; -; Genomic_DNA.
DR   RefSeq; YP_267702.1; -.
DR   GeneID; 3518818; -.
DR   GenomeReviews; CP000083_GR; CPS_0953.
DR   KEGG; cps:CPS_0953; -.
DR   NMPDR; fig|167879.3.peg.920; -.
DR   TIGR; CPS_0953; -.
DR   HOGENOM; Q487R3; -.
DR   OMA; Q487R3; TITHILW.
DR   BioCyc; CPSY167879:CPS_0953-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; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   Pfam; PF02683; DsbD; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; FALSE_NEG.
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     22       Potential.
FT   CHAIN        23    608       Thiol:disulfide interchange protein dsbD.
FT                                /FTId=PRO_0000304384.
FT   TRANSMEM    194    214       Potential.
FT   TRANSMEM    241    261       Potential.
FT   TRANSMEM    273    293       Potential.
FT   TRANSMEM    314    334       Potential.
FT   TRANSMEM    352    372       Potential.
FT   TRANSMEM    387    407       Potential.
FT   TRANSMEM    414    434       Potential.
FT   TRANSMEM    456    476       Potential.
FT   DOMAIN      469    608       Thioredoxin.
FT   DISULFID    135    141       Redox-active (By similarity).
FT   DISULFID    212    334       Redox-active (By similarity).
FT   DISULFID    522    525       Redox-active (By similarity).
SQ   SEQUENCE   608 AA;  66804 MW;  61FA123A713FA0B7 CRC64;
     MKNLLSLCFL MLAAFTLNPA AAQEKQSIFD VSNSSLFSND DEFLKVDQAF AFNFYQKNNL
     LEVSFDIAPE YYLYRHQFKF KGKNTQFTSV LLPDGIDHED EFFGVQKIFT ENLAFTVNLE
     NVSNDASIKI TYQGCAEKGL CYPPTSKVIK LSKFILGEST SAPSSDAAQQ TNEGEVKKSE
     QHQLSDMLKQ DSLLLTLIAF FVGGLLLSFT PCVFPMYPIL TGIIVGQGEG LTTKKAFTLS
     FFYVQGMAIT YTLLGVVVAM AGAKFQAVFQ HPIVLIGLSI LFIFLALSMF GVFNLALPAS
     WQNKLNNVSN KQKGGSITGV LMMGVISGLV ASPCTTAPLT GALLYISQTG DVVLGASALY
     ALSLGMGLPL LILGSSGGKL LPKAGAWMNI IKNIFGLLLL AVPVFLLERF IPEVASQALW
     ALLILVSASY FYVANQNHAA AQNVQQGKGF WYGLRSLVIF LMLFFGANLA YQLIYPSSNN
     VTNNAQHASF KQVTSLAQLE DEVKKANMQG KTVMVDLYAD WCIACKEFEK YTFVDADVQK
     ALSNSVWLQI DMTEFDSTDN AELVQHYTIL GLPSILFFDL QGNELTKQRT TGFMKAAEFS
     AHVKSIFK
//