DSBA_VIBCH
ID DSBA_VIBCH Reviewed; 200 AA.
AC P32557; Q9JQ15;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Thiol:disulfide interchange protein DsbA;
DE Flags: Precursor;
GN Name=dsbA; Synonyms=tpcG; OrderedLocusNames=VC_0034;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1631111; DOI=10.1073/pnas.89.13.6210;
RA Peek J.A., Taylor R.K.;
RT "Characterization of a periplasmic thiol:disulfide interchange protein
RT required for the functional maturation of secreted virulence factors of
RT Vibrio cholerae.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:6210-6214(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1324389; DOI=10.1111/j.1365-2958.1992.tb01368.x;
RA Yu J., Webb H., Hirst T.R.;
RT "A homologue of the Escherichia coli DsbA protein involved in disulphide
RT bond formation is required for enterotoxin biogenesis in Vibrio cholerae.";
RL Mol. Microbiol. 6:1949-1958(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND DISULFIDE BOND.
RX PubMed=9149147; DOI=10.1006/jmbi.1997.0940;
RA Hu S.-H., Peek J.A., Rattigan E., Taylor R.K., Martin J.L.;
RT "Structure of TcpG, the DsbA protein folding catalyst from Vibrio
RT cholerae.";
RL J. Mol. Biol. 268:137-146(1997).
CC -!- FUNCTION: Involved in disulfide-bond formation. Required for the
CC functional maturation of secreted virulence factors. Acts by
CC transferring its disulfide bond to other proteins.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily.
CC {ECO:0000305}.
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DR EMBL; M93713; AAA27568.1; -; Genomic_DNA.
DR EMBL; X64725; CAA45977.1; -; Genomic_DNA.
DR EMBL; AE003852; AAF93212.1; -; Genomic_DNA.
DR PIR; E82371; A46148.
DR RefSeq; NP_229693.1; NC_002505.1.
DR RefSeq; WP_000732279.1; NZ_LT906614.1.
DR PDB; 1BED; X-ray; 2.00 A; A=20-200.
DR PDB; 2IJY; NMR; -; A=20-200.
DR PDB; 4DVC; X-ray; 1.20 A; A=19-200.
DR PDB; 7LUI; X-ray; 1.74 A; A=20-200.
DR PDBsum; 1BED; -.
DR PDBsum; 2IJY; -.
DR PDBsum; 4DVC; -.
DR PDBsum; 7LUI; -.
DR AlphaFoldDB; P32557; -.
DR BMRB; P32557; -.
DR SMR; P32557; -.
DR STRING; 243277.VC_0034; -.
DR DNASU; 2614468; -.
DR EnsemblBacteria; AAF93212; AAF93212; VC_0034.
DR KEGG; vch:VC_0034; -.
DR PATRIC; fig|243277.26.peg.33; -.
DR eggNOG; COG1651; Bacteria.
DR HOGENOM; CLU_088255_3_0_6; -.
DR OMA; NAIHKQK; -.
DR BioCyc; VCHO:VC0034-MON; -.
DR EvolutionaryTrace; P32557; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; IPR013766; Thioredoxin_domain.
DR Pfam; PF01323; DSBA; 1.
DR PIRSF; PIRSF001488; Tdi_protein; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Periplasm; Redox-active center;
KW Reference proteome; Signal; Virulence.
FT SIGNAL 1..19
FT CHAIN 20..200
FT /note="Thiol:disulfide interchange protein DsbA"
FT /id="PRO_0000034268"
FT DOMAIN 20..198
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 49..52
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691,
FT ECO:0000269|PubMed:9149147"
FT CONFLICT 42
FT /note="N -> S (in Ref. 1; AAA27568)"
FT /evidence="ECO:0000305"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:4DVC"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:4DVC"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:4DVC"
FT HELIX 50..64
FT /evidence="ECO:0007829|PDB:4DVC"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:4DVC"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:4DVC"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:4DVC"
FT HELIX 85..97
FT /evidence="ECO:0007829|PDB:4DVC"
FT HELIX 101..113
FT /evidence="ECO:0007829|PDB:4DVC"
FT HELIX 122..130
FT /evidence="ECO:0007829|PDB:4DVC"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:4DVC"
FT HELIX 136..143
FT /evidence="ECO:0007829|PDB:4DVC"
FT HELIX 146..162
FT /evidence="ECO:0007829|PDB:4DVC"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:4DVC"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:4DVC"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:4DVC"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:4DVC"
FT HELIX 186..196
FT /evidence="ECO:0007829|PDB:4DVC"
SQ SEQUENCE 200 AA; 22567 MW; CBA756AC5EB05069 CRC64;
MKKLFALVAT LMLSVSAYAA QFKEGEHYQV LKTPASSSPV VNEFFSFYCP HCNTFEPIIA
QLKQQLPEGA KFQKNHVSFM GGNMGQAMSK AYATMIALEV EDKMVPVMFN RIHTLRKPPK
DEQELRQIFL DEGIDAAKFD AAYNGFAVDS MVRRFDKQFQ DSGLTGVPAV VVNNRYLVQG
QSVKSLDEYF DLVNYLLTLK
