ID   DSBA_YERPE              Reviewed;         207 AA.
AC   Q9XBV2; Q0WKS6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Thiol:disulfide interchange protein DsbA;
DE   Flags: Precursor;
GN   Name=dsbA; OrderedLocusNames=YPO0015, y3812, YP_0017;
OS   Yersinia pestis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=KIM;
RX   PubMed=10438793; DOI=10.1128/jb.181.16.5126-5130.1999;
RA   Jackson M.W., Plano G.V.;
RT   "DsbA is required for stable expression of outer membrane protein YscC and
RT   for efficient Yop secretion in Yersinia pestis.";
RL   J. Bacteriol. 181:5126-5130(1999).
RN   [2]
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   [3]
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   [4]
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 for disulfide bond formation in some periplasmic
CC       proteins such as PhoA or OmpA. Acts by transferring its disulfide bond
CC       to other proteins and is reduced in the process. DsbA is reoxidized by
CC       DsbB. It is required for pilus biogenesis (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF155130; AAD38401.1; -; Genomic_DNA.
DR   EMBL; AL590842; CAL18706.1; -; Genomic_DNA.
DR   EMBL; AE009952; AAM87357.1; -; Genomic_DNA.
DR   EMBL; AE017042; AAS60298.1; -; Genomic_DNA.
DR   PIR; AI0002; AI0002.
DR   RefSeq; WP_002213168.1; NZ_WUCM01000127.1.
DR   RefSeq; YP_002345112.1; NC_003143.1.
DR   AlphaFoldDB; Q9XBV2; -.
DR   SMR; Q9XBV2; -.
DR   STRING; 214092.YPO0015; -.
DR   PaxDb; Q9XBV2; -.
DR   PRIDE; Q9XBV2; -.
DR   DNASU; 1148759; -.
DR   EnsemblBacteria; AAM87357; AAM87357; y3812.
DR   EnsemblBacteria; AAS60298; AAS60298; YP_0017.
DR   GeneID; 66843587; -.
DR   KEGG; ype:YPO0015; -.
DR   KEGG; ypk:y3812; -.
DR   KEGG; ypm:YP_0017; -.
DR   PATRIC; fig|1028802.3.peg.1672; -.
DR   eggNOG; COG1651; Bacteria.
DR   HOGENOM; CLU_088255_3_0_6; -.
DR   OMA; NAIHKQK; -.
DR   Proteomes; UP000000815; Chromosome.
DR   Proteomes; UP000001019; Chromosome.
DR   Proteomes; UP000002490; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:UniProt.
DR   CDD; cd03019; DsbA_DsbA; 1.
DR   InterPro; IPR001853; DSBA-like_thioredoxin_dom.
DR   InterPro; IPR023205; DsbA/DsbL.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF01323; DSBA; 1.
DR   PIRSF; PIRSF001488; Tdi_protein; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Periplasm; Redox-active center; Reference proteome; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250"
FT   CHAIN           20..207
FT                   /note="Thiol:disulfide interchange protein DsbA"
FT                   /id="PRO_0000034269"
FT   DOMAIN          20..149
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        49..52
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   207 AA;  23100 MW;  A9089DD370CAB107 CRC64;
     MKNVWLALVG IVMAFSVTAA QFTDGKQYLT LDKPVTGEPQ VLEFFSFYCP HCYQFEEVYQ
     VPKAVKKALP EGTKMTRYHV EFLGPLGKQL TQAWAVAMAL GVEEKITPLM FEGVQKTQTV
     QTPGDIRNVF IKAGISGEDY DAALNSFVVK SLVAQQQKAA EDLQLRGVPA MFVNGKYMIK
     NDGMDTSSMD NYVKQYADVV TFLLTQK