ID   DSBA_BORA1              Reviewed;         209 AA.
AC   Q2KTN7;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Thiol:disulfide interchange protein DsbA;
DE   Flags: Precursor;
GN   Name=dsbA; OrderedLocusNames=BAV3363;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=197N;
RX   PubMed=16885469; DOI=10.1128/jb.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA   Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA   Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA   Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT   with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT   extensive diversity in surface structures associated with host
RT   interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AM167904; CAJ50973.1; -; Genomic_DNA.
DR   RefSeq; WP_012419000.1; NC_010645.1.
DR   AlphaFoldDB; Q2KTN7; -.
DR   SMR; Q2KTN7; -.
DR   STRING; 360910.BAV3363; -.
DR   EnsemblBacteria; CAJ50973; CAJ50973; BAV3363.
DR   GeneID; 41395195; -.
DR   KEGG; bav:BAV3363; -.
DR   eggNOG; COG1651; Bacteria.
DR   HOGENOM; CLU_088255_1_0_4; -.
DR   OMA; EVVEFFW; -.
DR   OrthoDB; 1805428at2; -.
DR   Proteomes; UP000001977; 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   Pfam; PF00085; Thioredoxin; 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..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..209
FT                   /note="Thiol:disulfide interchange protein DsbA"
FT                   /id="PRO_0000245629"
FT   DOMAIN          28..165
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   209 AA;  22767 MW;  8C723D9C8B9A8D56 CRC64;
     MLSSSISRLL AAAALAATTF FAPASHAEGN AYVTLSPALP SDTPGKIEVL EFFAYTCPHC
     AAIEPMVEDW AKTKPEDVVL KQVPIAFNAG MKPLQQLYYT LMALDRPDLH IKVFNAIHGE
     RKRLFDKKAM GDWVASQGVD RAKFDAVFDS FSVQTQVQRA NQLAEAYRID GTPSFGVGGK
     FLTSPVLAGN SYEGAIKEIN KLIPMARAK