DSBD_TATCI
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 25-MAY-2022, entry version 107.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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 + 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 -!- 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 -!- 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: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; 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
