ID   DSBD_PSEF5              Reviewed;         583 AA.
AC   Q4K909;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 39.
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=PFL_4182;
OS   Pseudomonas fluorescens (strain Pf-5 / ATCC BAA-477).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=220664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15980861; DOI=10.1038/nbt1110;
RA   Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA   Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA   Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A.,
RA   Rosovitz M.J., Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W.,
RA   Nelson W.C., Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A.,
RA   Pierson L.S. III, Thomashow L.S., Loper J.E.;
RT   "Complete genome sequence of the plant commensal Pseudomonas
RT   fluorescens Pf-5.";
RL   Nat. Biotechnol. 23:873-878(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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000076; AAY93438.1; -; Genomic_DNA.
DR   RefSeq; YP_261274.1; -.
DR   GeneID; 3476920; -.
DR   GenomeReviews; CP000076_GR; PFL_4182.
DR   KEGG; pfl:PFL_4182; -.
DR   NMPDR; fig|220664.3.peg.5994; -.
DR   HOGENOM; Q4K909; -.
DR   OMA; Q4K909; HILTIRI.
DR   BioCyc; PFLU220664:PFL_4182-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; 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     18       Potential.
FT   CHAIN        19    583       Thiol:disulfide interchange protein dsbD.
FT                                /FTId=PRO_0000304393.
FT   TRANSMEM    168    188       Potential.
FT   TRANSMEM    214    234       Potential.
FT   TRANSMEM    245    265       Potential.
FT   TRANSMEM    289    309       Potential.
FT   TRANSMEM    326    346       Potential.
FT   TRANSMEM    359    379       Potential.
FT   TRANSMEM    382    402       Potential.
FT   TRANSMEM    413    433       Potential.
FT   DOMAIN      458    581       Thioredoxin.
FT   DISULFID    118    124       Redox-active (By similarity).
FT   DISULFID    186    306       Redox-active (By similarity).
FT   DISULFID    496    499       Redox-active (By similarity).
SQ   SEQUENCE   583 AA;  62515 MW;  CAEBB141CBA77113 CRC64;
     MRRLFLLLFM LFTTLAHAGN NPFEVKPDFL PVGKAFVFTS ERLPSGETQL FWQIADGYYL
     YQKRLKFDGV APELQPTLPA GEDHSDEFFG QQTVYRQGLE VKLPAAASGK VKLGWQGCAD
     AGLCYPPQTL EVDLGGAPAV AASNVATTSN GSAQDQLLAN DLQHKSWGLG LLAFFGFGLL
     LAFAPCSLPM LPILAGMVVG SGASPRRGLA LASSYVLCMA LVYAGMGVIA ALLGSNLQAW
     LQQPWVLGSF AALFVLLSLP MFGFFELQMP ALLRDRLEGA SRQRQGGSLI GCGILGALSA
     LLVGPCMTAP LAGGLLYIAQ TGNALFGGLA LFALGLGIGL PLLLLVTLGN RFLPKPGPWM
     NLLKGVFGIL FLGTAIYMLR PVLNPGLWMG LWGALALVVA YCAWQQRAIA GRLLHLFGAG
     ALLFAAWGGM LLVGAAGGGD DLWRPLKVYR GGPVANSVTA HDAFTTVKSP AELQGALDSA
     RAQGQWVLLD YYADWCVSCK IMEKTVFGQP QVLEALKDVR LLRLDVTLDN ADGRELLSRY
     KVPGPPSMLW IGPDGSERRS QRITGEVDAN AFLQRWTQTR EAR
//