DSBA_PSESM
ID DSBA_PSESM Reviewed; 214 AA.
AC O52376;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Thiol:disulfide interchange protein DsbA;
DE Flags: Precursor;
GN Name=dsbA; OrderedLocusNames=PSPTO_0341;
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kloek A.P., Kunkel B.N.;
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
CC -!- FUNCTION: Involved in disulfide-bond formation. Acts by transferring
CC its disulfide bond to other proteins (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily.
CC {ECO:0000305}.
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DR EMBL; AF036929; AAB92367.1; -; Genomic_DNA.
DR EMBL; AE016853; AAO53886.1; -; Genomic_DNA.
DR RefSeq; NP_790191.1; NC_004578.1.
DR RefSeq; WP_005763490.1; NC_004578.1.
DR AlphaFoldDB; O52376; -.
DR SMR; O52376; -.
DR STRING; 223283.PSPTO_0341; -.
DR DNASU; 1181950; -.
DR EnsemblBacteria; AAO53886; AAO53886; PSPTO_0341.
DR GeneID; 1181950; -.
DR KEGG; pst:PSPTO_0341; -.
DR PATRIC; fig|223283.9.peg.357; -.
DR eggNOG; COG1651; Bacteria.
DR HOGENOM; CLU_088255_1_0_6; -.
DR OMA; NAIHKQK; -.
DR OrthoDB; 1805428at2; -.
DR PhylomeDB; O52376; -.
DR Proteomes; UP000002515; 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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..214
FT /note="Thiol:disulfide interchange protein DsbA"
FT /id="PRO_0000034263"
FT DOMAIN 23..154
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 57..60
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 214 AA; 23340 MW; 92F7DB1F31A6996B CRC64;
MRNLIISAAL VAASLFGMSA QAAEPIESGK QYVELTSAVP VAVPGKIEVI ELFWYGCPHC
YAFEPTINPW VEKLPSDVNF VRIPAMFGGP WDAHGQLFIT LDTMGVEHKV HAAVFEAIQK
GGKRLTDKND MADFVATQGV NKDDFLKTFD SFAVKGKIAQ YKELAKKYEV TGVPTMIVNG
KYRFDLGSAG GPEKTLQVAD QLIDKERAAA KAAK
