ID   DSBD_HAEIG              Reviewed;         579 AA.
AC   A5UI29;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   16-JUN-2009, entry version 20.
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=CGSHiGG_07975;
OS   Haemophilus influenzae (strain PittGG).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=374931;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA   Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R.,
RA   Post J.C., Ehrlich G.D.;
RT   "Characterization and modeling of the Haemophilus influenzae core and
RT   supragenomes based on the complete genomic sequences of Rd and 12
RT   clinical nontypeable strains.";
RL   Genome Biol. 8:RESEARCH103.1-RESEARCH103.18(2007).
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; CP000672; ABR00435.1; -; Genomic_DNA.
DR   RefSeq; YP_001292818.1; -.
DR   GeneID; 5227482; -.
DR   GenomeReviews; CP000672_GR; CGSHiGG_07975.
DR   KEGG; hiq:CGSHiGG_07975; -.
DR   OMA; A5UI29; PVFLLSR.
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     16       Potential.
FT   CHAIN        17    579       Thiol:disulfide interchange protein dsbD.
FT                                /FTId=PRO_1000049610.
FT   TRANSMEM    178    198       Potential.
FT   TRANSMEM    230    250       Potential.
FT   TRANSMEM    254    274       Potential.
FT   TRANSMEM    296    316       Potential.
FT   TRANSMEM    337    357       Potential.
FT   TRANSMEM    376    396       Potential.
FT   TRANSMEM    397    417       Potential.
FT   TRANSMEM    420    440       Potential.
FT   DOMAIN      449    579       Thioredoxin.
FT   DISULFID    124    129       Redox-active (By similarity).
FT   DISULFID    193    315       Redox-active (By similarity).
FT   DISULFID    495    498       Redox-active (By similarity).
SQ   SEQUENCE   579 AA;  64454 MW;  A156D89A9059E681 CRC64;
     MKKLFLFFTL IFTAFAANSG LFDKKQTFLK VDDAFAFSAT LSTDKSQLQA HWDIADGYYL
     YQDKISAELV GKSNPLSLHT QQAAELHQDP YFGEVKVFTH SIDGIFRGTF NNADDKVEIT
     YQGCTEGFCY PPETKVLRIG DLAVSQEQIV EKTVEKNTAL LSEQDRLADG LFHSKWAIFG
     FFVLGLGLAF TPCVLPMLPL LSAIVIGQQQ RPNMMRAFSL AFLYVQGMAL TYTLLGLAVA
     AIGLPFQIAL QHPYVMIGLS ILFVVLALSM FGLFTIQLPN SLQNKLNTWS QKQTSGAFGG
     AFAMGMIAGL VASPCTSAPL SGALLYVAQS GDLFTGAVTL YLLALGMGVP LMLITLFGNK
     ILPKSGEWMN TVKQTFGFVM LALPVFLLSR ILPEVWESRL WAGLATVFFI WFALQMSKNG
     FGYAIKIISF ALAMVTVQPL QNWIWQTQTT TQSAVENMPV SQVKFKQIKN TEELDRTLAE
     NPHSIAMLDL YADWCVACKE FEKLTFSDPQ VQQQFQNILL LQVNMTKNSP ENKALMERFN
     VMGLPTILFF DQQNNEIKGS RVTGFMDADA FSNWIEKLL
//