ID   DSBD_HAEDU              Reviewed;         573 AA.
AC   Q7VMZ4;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 122.
DE   RecName: Full=Thiol:disulfide interchange protein DsbD {ECO:0000255|HAMAP-Rule:MF_00399};
DE            EC=1.8.1.8 {ECO:0000255|HAMAP-Rule:MF_00399};
DE   AltName: Full=Protein-disulfide reductase {ECO:0000255|HAMAP-Rule:MF_00399};
DE            Short=Disulfide reductase {ECO:0000255|HAMAP-Rule:MF_00399};
DE   Flags: Precursor;
GN   Name=dsbD {ECO:0000255|HAMAP-Rule:MF_00399}; OrderedLocusNames=HD_0807;
OS   Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=233412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=35000HP / ATCC 700724;
RA   Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA   Nguyen D., Wang J., Forst C., Hood L.;
RT   "The complete genome sequence of Haemophilus ducreyi.";
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required to facilitate the formation of correct disulfide
CC       bonds in some periplasmic proteins and for the assembly of the
CC       periplasmic c-type cytochromes. Acts by transferring electrons from
CC       cytoplasmic thioredoxin to the periplasm. This transfer involves a
CC       cascade of disulfide bond formation and reduction steps.
CC       {ECO:0000255|HAMAP-Rule:MF_00399}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-dithiol + NAD(+) = [protein]-disulfide + H(+) +
CC         NADH; Xref=Rhea:RHEA:18749, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC         COMP:10594, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.8.1.8;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00399};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-dithiol + NADP(+) = [protein]-disulfide + H(+) +
CC         NADPH; Xref=Rhea:RHEA:18753, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC         COMP:10594, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.8;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00399};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00399}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00399}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbD subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00399}.
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DR   EMBL; AE017143; AAP95707.1; -; Genomic_DNA.
DR   RefSeq; WP_010944757.1; NC_002940.2.
DR   AlphaFoldDB; Q7VMZ4; -.
DR   SMR; Q7VMZ4; -.
DR   STRING; 233412.HD_0807; -.
DR   EnsemblBacteria; AAP95707; AAP95707; HD_0807.
DR   KEGG; hdu:HD_0807; -.
DR   eggNOG; COG4232; Bacteria.
DR   HOGENOM; CLU_014657_3_0_6; -.
DR   OMA; YRHRFQF; -.
DR   Proteomes; UP000001022; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0047134; F:protein-disulfide reductase (NAD(P)) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-UniRule.
DR   CDD; cd02953; DsbDgamma; 1.
DR   Gene3D; 2.60.40.1250; -; 1.
DR   HAMAP; MF_00399; DbsD; 1.
DR   InterPro; IPR003834; Cyt_c_assmbl_TM_dom.
DR   InterPro; IPR035671; DsbD_gamma.
DR   InterPro; IPR028250; DsbDN.
DR   InterPro; IPR036929; DsbDN_sf.
DR   InterPro; IPR022910; Thiol_diS_interchange_DbsD.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR32234:SF0; PTHR32234:SF0; 1.
DR   Pfam; PF11412; DsbC; 1.
DR   Pfam; PF02683; DsbD; 1.
DR   Pfam; PF13098; Thioredoxin_2; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   SUPFAM; SSF74863; SSF74863; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Cytochrome c-type biogenesis;
KW   Disulfide bond; Electron transport; Membrane; NAD; Oxidoreductase;
KW   Redox-active center; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   CHAIN           21..573
FT                   /note="Thiol:disulfide interchange protein DsbD"
FT                   /id="PRO_0000007375"
FT   TOPO_DOM        21..175
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   TOPO_DOM        197..227
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        228..248
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   TOPO_DOM        249..251
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        252..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   TOPO_DOM        273..292
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        293..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   TOPO_DOM        314..331
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        332..352
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   TOPO_DOM        353..365
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        366..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   TOPO_DOM        387..393
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        394..414
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   TOPO_DOM        415..425
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        426..446
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   TOPO_DOM        447..573
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          440..573
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   DISULFID        121..126
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   DISULFID        191..313
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   DISULFID        490..493
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
SQ   SEQUENCE   573 AA;  63070 MW;  2D1D3A9C7E3632D6 CRC64;
     MLKRFFLLLS SLLLVCNVQA GLFNNKPQYL TAAEAFIFSS SQQDGQLQLH WQIADGYYLY
     QKEIQLSAQN ATLGDVTFPT AEKYQDEFFG EVAIFRDQLK LPVKLTDLKE NPSLKIRYQG
     CTKGFCYPPE TVVIPLNPSL QGNNSANSAA LPSTIATPNA PQTELAENLS NNYLSIFGFL
     LLGIGLAFTP CVLPMLPLLS AIVIGHKNRP NTSRALLLSF TYVQGMALTY TLLGLTVAAI
     GLPFQVALQS PAVLISLAVL FTLLAASMFG LFEIRLPNTW QQKLNALSQQ QQGGAVGNVF
     IMGIIAGLVA SPCTSAPLSG ALLYVAQSGN LLIGGLALYL LALGMGLPLI LITVFGNQIL
     PKSGEWLFKV KTAFGFVMLA LPIFLISRIL PSHYEPFLWS TLALAFLGWL ISSLNYSTML
     KQAVRILLFI AFGLTAYPWA NLVWQTTSNT AQPTTPHLAM EKITSLTELE QKLTAYQGKK
     VMLDLYADWC VACKEFEKYT FTDPQVQQQL ATMAVLQIDM TKNSAENTAL MKHFNVLGLP
     TILFFDENGH EMTNVRITGF LTANQFLAWL NRL