ID   DSBD_TATCI              Reviewed;         578 AA.
AC   Q9XDB2;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   02-SEP-2026, entry version 118.
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;
OS   Tatumella citrea (Pantoea citrea).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Erwiniaceae; Tatumella.
OX   NCBI_TaxID=53336;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=1056R;
RX   PubMed=10735866; DOI=10.1128/jb.182.8.2230-2237.2000;
RA   Pujol C.J., Kado C.I.;
RT   "Genetic and biochemical characterization of the pathway in Pantoea citrea
RT   leading to pink disease of pineapple.";
RL   J. Bacteriol. 182:2230-2237(2000).
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-dithiol + NAD(+) = [protein]-disulfide + NADH +
CC         H(+); 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-dithiol + NADP(+) = [protein]-disulfide + NADPH +
CC         H(+); 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   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbD subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF102175; AAD38449.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9XDB2; -.
DR   SMR; Q9XDB2; -.
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)H] activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:TreeGrafter.
DR   GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-UniRule.
DR   CDD; cd02953; DsbDgamma; 1.
DR   FunFam; 3.40.30.10:FF:000116; Thiol:disulfide interchange protein DsbD; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 2.60.40.1250; Thiol:disulfide interchange protein DsbD, N-terminal domain; 1.
DR   HAMAP; MF_00399; DbsD; 1.
DR   InterPro; IPR003834; Cyt_c_assmbl_TM_dom.
DR   InterPro; IPR035671; DsbD_gamma.
DR   InterPro; IPR061926; DsbD_link.
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   NCBIfam; NF001419; PRK00293.1; 1.
DR   PANTHER; PTHR32234; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBD; 1.
DR   PANTHER; PTHR32234:SF0; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBD; 1.
DR   Pfam; PF30370; DsbD_link; 1.
DR   Pfam; PF11412; DsbD_N; 1.
DR   Pfam; PF02683; DsbD_TM; 1.
DR   Pfam; PF13098; Thioredoxin_2; 1.
DR   SUPFAM; SSF74863; Thiol:disulfide interchange protein DsbD, N-terminal domain (DsbD-alpha); 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 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; Signal; Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..578
FT                   /note="Thiol:disulfide interchange protein DsbD"
FT                   /id="PRO_0000007379"
FT   TOPO_DOM        23..180
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        181..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        202..216
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        217..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        238..253
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        254..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        275..306
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        307..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        328..336
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        337..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        358..367
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        368..388
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        389..394
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        395..415
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        416..428
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        429..449
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        450..578
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          436..577
FT                   /note="Thioredoxin"
FT   DISULFID        125..131
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
FT   DISULFID        193..315
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
FT   DISULFID        492..495
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   578 AA;  62547 MW;  383B32797B7FA0E4 CRC64;
     MVARLTRLII LALTLFSLHA QAGLFDSGSS PHFVTVNQAF GFDFSQNNHN VVLRWKVKPG
     YYLYRQQFSI TGTNAVIAGI ALPSGQPHED EFFGKSQIFP QDVQIPVTLK STLPGATLKI
     SYQGCAAAGF CYPPETREVP LSQVSTTRSE APATAAATPA PVPEPQSGPA VSRLPFSPLW
     ALLIGIGIAF TPCVLPMYPL ISAIILGGRR DVRASRILLL AFVYVQGMGL TYTLMGIVVA
     AAGLRFQAAL QSPVILLSLS AVFILLALSM FGLFSLQLPS SLQTRLTLWS NRQQGGSLSG
     VFLMGALAGL ICSPCTTAPL SAILLYIAQS GNMLAGGGTL YLYALGMGLP LIIVTLFGNK
     LLPKSGPWMQ SVKEGFGFVI LALPVFLIDR VAGDLWGMRL WSLLGVAFFG WAFALSLKSP
     KGWMRVLQIV WLLAALVAAR PLQDWAFATP GVTASQEQAL PFQNIGTVAD LQQQLSQAQG
     KITMVDLYAD WCVACKEFEK YTFTDPQVRQ EFSQFRLVQA NVTANSAQDN ALLTHLNVLG
     LPTLLFFDAN GHEIPDSRVT GYMNASQFLA HLRKLRAE
//