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 27-MAR-2024, entry version 99.
DE RecName: Full=Thiol:disulfide interchange protein DsbA;
DE Flags: Precursor;
GN Name=dsbA; OrderedLocusNames=BAV3363;
OS Bordetella avium (strain 197N).
OC Bacteria; Pseudomonadota; 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}.
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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 GeneID; 41395195; -.
DR KEGG; bav:BAV3363; -.
DR eggNOG; COG1651; Bacteria.
DR HOGENOM; CLU_088255_1_0_4; -.
DR OrthoDB; 9784896at2; -.
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 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 PIRSF; PIRSF001488; Tdi_protein; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 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
//
