ID   DSBD_PECAS              Reviewed;         577 AA.
AC   Q6D9J6;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 116.
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=ECA0618;
OS   Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS   carotovora subsp. atroseptica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=218491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA   Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA   Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA   Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA   Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA   Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA   Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT   "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT   subsp. atroseptica and characterization of virulence factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
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; BX950851; CAG73534.1; -; Genomic_DNA.
DR   RefSeq; WP_011092237.1; NC_004547.2.
DR   AlphaFoldDB; Q6D9J6; -.
DR   SMR; Q6D9J6; -.
DR   STRING; 218491.ECA0618; -.
DR   EnsemblBacteria; CAG73534; CAG73534; ECA0618.
DR   GeneID; 57207368; -.
DR   KEGG; eca:ECA0618; -.
DR   PATRIC; fig|218491.5.peg.614; -.
DR   eggNOG; COG4232; Bacteria.
DR   HOGENOM; CLU_014657_3_0_6; -.
DR   OMA; YYADWCV; -.
DR   OrthoDB; 1055204at2; -.
DR   Proteomes; UP000007966; 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; 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   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..23
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   CHAIN           24..577
FT                   /note="Thiol:disulfide interchange protein DsbD"
FT                   /id="PRO_0000304385"
FT   TRANSMEM        182..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   TRANSMEM        225..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   TRANSMEM        255..275
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   TRANSMEM        308..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   TRANSMEM        338..358
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   TRANSMEM        369..389
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   TRANSMEM        396..416
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   DOMAIN          437..577
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   DISULFID        131..137
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   DISULFID        194..316
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   DISULFID        492..495
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
SQ   SEQUENCE   577 AA;  62917 MW;  28B54B667E4016C0 CRC64;
     MAQRIFTLIF LLWTAVGTPQ VAASSFGQKL FGNSTTSRFL PVDGAFAFEF QQQGNQLNLR
     WDIHPDYYLY RAQIKIEGNG ATLGKVELPQ GESHNDEFFG QVFILRDRLA LAVPIEQAES
     GATVKVTYQG CADAGFCYPP ETRTVPLSQV LATANTDSPI NTLSGQTAPP QTTPMPFSPW
     WALLIGIGVA FTPCVLPMYP LIASLVLGRK EQLTPRRTLL LSMTYVQGMA LTYTLLGLIV
     AAAGLRFQAA LQHPYILIGL SVMFIALALS MFGLYTLQLP SSVQTRLTEW SNRQQGGSVT
     GVFCMGALAG LICSPCTTAP LSAILLYIAQ SGNMLAGGGT LYLYALGMGL PLILVTLFGN
     KLLPRSGPWM QYVKEAFGFI ILALPVFLLE RILGEAWGIR LWSALGIAFF GWALMLTLSS
     KKGWMRGVQL LLLAGVVISA KPLQDWVFPP TGTAQTHTSA LNFAPVANIA DLNSALAKSP
     QPVMLDLYAD WCVACKEFEK YTFSDPAVQN HLSRITLLQA DVTANREEQN ALLKKLQVLG
     LPTIVFFDTQ GKEIPGSRVT GFMNAEQFQA HLQKFSP