ID   DSBA_BORPA              Reviewed;         209 AA.
AC   Q7W2Q0;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Thiol:disulfide interchange protein DsbA;
DE   Flags: Precursor;
GN   Name=dsbA; OrderedLocusNames=BPP4354;
OS   Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257311;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12822 / ATCC BAA-587 / NCTC 13253;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(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}.
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; BX640436; CAE39633.1; -; Genomic_DNA.
DR   RefSeq; WP_003815939.1; NC_002928.3.
DR   PDB; 3HD5; X-ray; 2.35 A; A/B/C=25-208.
DR   PDBsum; 3HD5; -.
DR   AlphaFoldDB; Q7W2Q0; -.
DR   SMR; Q7W2Q0; -.
DR   EnsemblBacteria; CAE39633; CAE39633; BPP4354.
DR   GeneID; 56476559; -.
DR   GeneID; 66440860; -.
DR   KEGG; bpa:BPP4354; -.
DR   HOGENOM; CLU_088255_1_0_4; -.
DR   OMA; EVVEFFW; -.
DR   EvolutionaryTrace; Q7W2Q0; -.
DR   Proteomes; UP000001421; 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   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; Periplasm; Redox-active center; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..209
FT                   /note="Thiol:disulfide interchange protein DsbA"
FT                   /id="PRO_0000245631"
FT   DOMAIN          28..166
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        58..61
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   STRAND          48..54
FT                   /evidence="ECO:0007829|PDB:3HD5"
FT   HELIX           59..73
FT                   /evidence="ECO:0007829|PDB:3HD5"
FT   STRAND          79..85
FT                   /evidence="ECO:0007829|PDB:3HD5"
FT   HELIX           90..92
FT                   /evidence="ECO:0007829|PDB:3HD5"
FT   HELIX           93..104
FT                   /evidence="ECO:0007829|PDB:3HD5"
FT   HELIX           110..119
FT                   /evidence="ECO:0007829|PDB:3HD5"
FT   HELIX           128..137
FT                   /evidence="ECO:0007829|PDB:3HD5"
FT   HELIX           142..149
FT                   /evidence="ECO:0007829|PDB:3HD5"
FT   HELIX           152..167
FT                   /evidence="ECO:0007829|PDB:3HD5"
FT   STRAND          172..178
FT                   /evidence="ECO:0007829|PDB:3HD5"
FT   TURN            179..181
FT                   /evidence="ECO:0007829|PDB:3HD5"
FT   STRAND          182..184
FT                   /evidence="ECO:0007829|PDB:3HD5"
FT   TURN            186..190
FT                   /evidence="ECO:0007829|PDB:3HD5"
FT   HELIX           191..193
FT                   /evidence="ECO:0007829|PDB:3HD5"
FT   HELIX           196..208
FT                   /evidence="ECO:0007829|PDB:3HD5"
SQ   SEQUENCE   209 AA;  22817 MW;  9F1C04B4703FA582 CRC64;
     MQSTTFTRLL AAAALAATTL FAPATQAQGA QQYVNINPPM PSDTPGKIEV LEFFAYTCPH
     CAAIEPMVED WAKTAPQDVV LKQVPIAFNA GMKPLQQLYY TLQALERPDL HPKVFTAIHT
     ERKRLFDKKA MGEWAASQGV DRAKFDSVFD SFSVQTQVQR ASQLAEAAHI DGTPAFAVGG
     RYMTSPVLAG NDYAGALKVV DQLIVQSRK