ID DSBA_BORPE Reviewed; 209 AA.
AC Q7W0K2;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=Thiol:disulfide interchange protein DsbA;
DE Flags: Precursor;
GN Name=dsbA; OrderedLocusNames=BP0113;
OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257313;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
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).
RN [2]
RP FUNCTION IN PERTUSSIS TOXIN SECRETION.
RC STRAIN=Tohama I / BP338;
RX PubMed=11953363; DOI=10.1128/iai.70.5.2297-2303.2002;
RA Stenson T.H., Weiss A.A.;
RT "DsbA and DsbC are required for secretion of pertussis toxin by Bordetella
RT pertussis.";
RL Infect. Immun. 70:2297-2303(2002).
CC -!- FUNCTION: Involved in disulfide-bond formation. Acts by transferring
CC its disulfide bond to other proteins (By similarity). Required for
CC periplasmic assembly of the pertussis toxin (PTX). {ECO:0000250,
CC ECO:0000269|PubMed:11953363}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily.
CC {ECO:0000305}.
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DR EMBL; BX640411; CAE40493.1; -; Genomic_DNA.
DR RefSeq; NP_879015.1; NC_002929.2.
DR RefSeq; WP_010929628.1; NZ_CP039022.1.
DR AlphaFoldDB; Q7W0K2; -.
DR SMR; Q7W0K2; -.
DR STRING; 257313.BP0113; -.
DR PaxDb; 257313-BP0113; -.
DR GeneID; 69603628; -.
DR KEGG; bpe:BP0113; -.
DR PATRIC; fig|257313.5.peg.115; -.
DR eggNOG; COG1651; Bacteria.
DR HOGENOM; CLU_088255_1_0_4; -.
DR Proteomes; UP000002676; 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 Gene3D; 3.40.30.10; Glutaredoxin; 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 PANTHER; PTHR35891; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBA; 1.
DR PANTHER; PTHR35891:SF2; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBA; 1.
DR Pfam; PF01323; DSBA; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR PIRSF; PIRSF001488; Tdi_protein; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
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_0000245632"
FT DISULFID 58..61
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 209 AA; 22784 MW; 9891E9CD35C39E22 CRC64;
MQSTTFTRLL AAAALGATTL FAPATQAQGA QQYVNINPPM PSDTPGKIEV LEFFAYTCPH
CAAIEPMVED WAKTAPQDVV LKQVPIAFNA GMKPLQQLYY TLQALERPDL HPKVFTAIHT
ERKRLFDKKA MGEWAASQGV DRAKFDSVFD SFSVQTQVQH ASQLAEAAHI DGTPAFAVGG
RYMTSPVLAG NDYAGALKVV DQLIVQSRK
//
