DSBD_YERPE
ID DSBD_YERPE Reviewed; 595 AA.
AC Q8ZIY9; Q0WJW5;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 152.
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};
GN OrderedLocusNames=YPO0345, y0603, YP_0499;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(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; AL590842; CAL19027.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM84190.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS60769.1; -; Genomic_DNA.
DR PIR; AI0042; AI0042.
DR RefSeq; WP_002209121.1; NZ_WUCM01000014.1.
DR RefSeq; YP_002345423.1; NC_003143.1.
DR AlphaFoldDB; Q8ZIY9; -.
DR SMR; Q8ZIY9; -.
DR IntAct; Q8ZIY9; 3.
DR STRING; 214092.YPO0345; -.
DR PaxDb; Q8ZIY9; -.
DR DNASU; 1145549; -.
DR EnsemblBacteria; AAM84190; AAM84190; y0603.
DR EnsemblBacteria; AAS60769; AAS60769; YP_0499.
DR GeneID; 57974263; -.
DR KEGG; ype:YPO0345; -.
DR KEGG; ypk:y0603; -.
DR KEGG; ypm:YP_0499; -.
DR PATRIC; fig|214092.21.peg.581; -.
DR eggNOG; COG4232; Bacteria.
DR HOGENOM; CLU_014657_3_0_6; -.
DR OMA; YRHRFQF; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; 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:0015035; F:protein-disulfide reductase activity; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
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..24
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT CHAIN 25..595
FT /note="Thiol:disulfide interchange protein DsbD"
FT /id="PRO_0000007391"
FT TRANSMEM 200..222
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT TRANSMEM 234..256
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT TRANSMEM 271..293
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT TRANSMEM 314..336
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT TRANSMEM 356..378
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT TRANSMEM 391..408
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT TRANSMEM 412..431
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT TRANSMEM 438..455
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT DOMAIN 452..592
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT REGION 166..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 134..140
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT DISULFID 209..331
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT DISULFID 507..510
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT CONFLICT 92
FT /note="P -> Q (in Ref. 3; AAS60769)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 595 AA; 64506 MW; D91ABB96DD6686C5 CRC64;
MAQRFITLIL LLCSVLLAPH SAQSSLFGEN ASFGTKNSQS RFIPVDQAFA FDFHQQGDQL
NLSWQIHPGY YLYRQQIKIV PQQAALGAFT LPEGITHHDE FYGEVEIFKQ QLTLKIPITQ
AAEQASVSVT YQGCAEAGFC YPPETRVIPL DVVVAASTAS GTAAVNSSAT VNPPATTQPE
GDATPVPSTL PFSPLWALLI GIGIAFTPCV LPMYPLISAV ILGREKPHSQ RRILILAVVY
VQGMALTYTL LGLVVAAAGL QFQAALQHPY VLIGLSVLFV LLALSMFGLY SLQLPSSLQT
RLTQWSNSQR GGSLAGVFAM GALAGLICSP CTTAPLSAIL LYIAQSGNML AGGGTLYLYA
LGMGIPLVVV TLFGNKLIPR SGPWMQYVKE AFGFVILALP VFLLERVLGD VWGLRLWSLL
AVAFFGWAFV LSLKAHAGWV RVCQLLLLAA LLIVARPLQD WAFNGNTQQN AVKHINFQPV
ANLPQLQAVL AQAQGKPVML DLYADWCVAC KEFEKYTFSD DKVQRQLANT LLLQADVTAN
NAEHATLLKK FNVLGLPTIL FFDSQGNEIT AARVTGFMDA AQFLQHLQNT PAVTK
