DSBA_ECOLI
ID DSBA_ECOLI Reviewed; 208 AA.
AC P0AEG4; P24991; Q2M8F8; Q46951; Q46952;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Thiol:disulfide interchange protein DsbA;
DE Flags: Precursor;
GN Name=dsbA; Synonyms=dsf, ppfA; OrderedLocusNames=b3860, JW3832;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1934062; DOI=10.1016/0092-8674(91)90532-4;
RA Bardwell J.C.A., McGovern K., Beckwith J.;
RT "Identification of a protein required for disulfide bond formation in
RT vivo.";
RL Cell 67:581-589(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1740115; DOI=10.1002/j.1460-2075.1992.tb05027.x;
RA Kamitani S., Akiyama Y., Ito K.;
RT "Identification and characterization of an Escherichia coli gene required
RT for the formation of correctly folded alkaline phosphatase, a periplasmic
RT enzyme.";
RL EMBO J. 11:57-62(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-49.
RA Grauschopf U., Winther J., Korber P., Zander T., Dallinger P.,
RA Bardwell J.C.A.;
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PROTEIN SEQUENCE OF 20-24, AND CHARACTERIZATION.
RX PubMed=8494885; DOI=10.1021/bi00070a016;
RA Zapun A., Bardwell J.C.A., Creighton T.E.;
RT "The reactive and destabilizing disulfide bond of DsbA, a protein required
RT for protein disulfide bond formation in vivo.";
RL Biochemistry 32:5083-5092(1993).
RN [8]
RP PROTEIN SEQUENCE OF 20-31.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [9]
RP PROTEIN SEQUENCE OF 20-23.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9600841; DOI=10.1006/jmbi.1998.1726;
RA Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C.,
RA Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L.,
RA Hochstrasser D.F.;
RT "Protein identification with N and C-terminal sequence tags in proteome
RT projects.";
RL J. Mol. Biol. 278:599-608(1998).
RN [10]
RP MUTAGENESIS OF PRO-50 AND HIS-51.
RX PubMed=8521518; DOI=10.1016/0092-8674(95)90210-4;
RA Grauschopf U., Winther J.R., Korber P., Zander T., Dallinger P.,
RA Bardwell J.C.A.;
RT "Why is DsbA such an oxidizing disulfide catalyst?";
RL Cell 83:947-955(1995).
RN [11]
RP FUNCTION.
RX PubMed=1429594; DOI=10.1016/s0021-9258(18)41691-2;
RA Akiyama Y., Kamitani S., Kusukawa N., Ito K.;
RT "In vitro catalysis of oxidative folding of disulfide-bonded proteins by
RT the Escherichia coli dsbA (ppfA) gene product.";
RL J. Biol. Chem. 267:22440-22445(1992).
RN [12]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [13]
RP FUNCTION IN PHOP/PHOQ REGULATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=22267510; DOI=10.1128/jb.06055-11;
RA Lippa A.M., Goulian M.;
RT "Perturbation of the oxidizing environment of the periplasm stimulates the
RT PhoQ/PhoP system in Escherichia coli.";
RL J. Bacteriol. 194:1457-1463(2012).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=8413591; DOI=10.1038/365464a0;
RA Martin J.L., Bardwell J.C.A., Kuriyan J.;
RT "Crystal structure of the DsbA protein required for disulphide bond
RT formation in vivo.";
RL Nature 365:464-468(1993).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=9194175; DOI=10.1002/pro.5560060603;
RA Guddat L.W., Bardwell J.C.A., Zander T., Martin J.L.;
RT "The uncharged surface features surrounding the active site of Escherichia
RT coli DsbA are conserved and are implicated in peptide binding.";
RL Protein Sci. 6:1148-1156(1997).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF HIS-51 MUTANTS, AND DISULFIDE
RP BOND.
RX PubMed=9300489; DOI=10.1002/pro.5560060910;
RA Guddat L.W., Bardwell J.C.A., Glockshuber R., Huber-Wunderlich M.,
RA Zander T., Martin J.L.;
RT "Structural analysis of three His32 mutants of DsbA: support for an
RT electrostatic role of His32 in DsbA stability.";
RL Protein Sci. 6:1893-1900(1997).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=9655827; DOI=10.1016/s0969-2126(98)00077-x;
RA Guddat L.W., Bardwell J.C.A., Martin J.L.;
RT "Crystal structures of reduced and oxidized DsbA: investigation of domain
RT motion and thiolate stabilization.";
RL Structure 6:757-767(1998).
RN [18]
RP STRUCTURE BY NMR.
RX PubMed=9572841; DOI=10.1021/bi980136y;
RA Schirra H.J., Renner C., Czisch M., Huber-Wunderlich M., Holak T.A.,
RA Glockshuber R.;
RT "Structure of reduced DsbA from Escherichia coli in solution.";
RL Biochemistry 37:6263-6276(1998).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=10210188; DOI=10.1110/ps.8.1.96;
RA Charbonnier J.-B., Belin P., Moutiez M., Stura E.A., Quemeneur E.;
RT "On the role of the cis-proline residue in the active site of DsbA.";
RL Protein Sci. 8:96-105(1999).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT ALA-52 OF 20-208.
RX PubMed=15755450; DOI=10.1016/j.jmb.2005.01.049;
RA Ondo-Mbele E., Vives C., Kone A., Serre L.;
RT "Intriguing conformation changes associated with the trans/cis
RT isomerization of a prolyl residue in the active site of the DsbA C33A
RT mutant.";
RL J. Mol. Biol. 347:555-563(2005).
CC -!- FUNCTION: Required for disulfide bond formation in some periplasmic
CC proteins such as PhoA or OmpA. Acts by transferring its disulfide bond
CC to other proteins and is reduced in the process. DsbA is reoxidized by
CC DsbB. Required for pilus biogenesis. PhoP-regulated transcription is
CC redox-sensitive, being activated when the periplasm becomes more
CC reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB
CC acts between DsbA/DsbB and PhoP/PhoQ in this pathway.
CC {ECO:0000269|PubMed:1429594, ECO:0000269|PubMed:22267510}.
CC -!- INTERACTION:
CC P0AEG4; P0A6M2: dsbB; NbExp=5; IntAct=EBI-549711, EBI-1170740;
CC P0AEG4; P00634: phoA; NbExp=2; IntAct=EBI-549711, EBI-552958;
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- DISRUPTION PHENOTYPE: Induction of the PhoP/PhoQ two-component
CC regulatory system, suppressed by 50 uM CuSO(4).
CC {ECO:0000269|PubMed:22267510}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily.
CC {ECO:0000305}.
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DR EMBL; X80762; CAA56736.1; -; Genomic_DNA.
DR EMBL; M77746; AAA23715.1; -; Genomic_DNA.
DR EMBL; X63186; CAA44868.1; -; Genomic_DNA.
DR EMBL; L19201; AAB02995.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76858.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77448.1; -; Genomic_DNA.
DR EMBL; U35817; AAC43519.1; -; Genomic_DNA.
DR EMBL; U35818; AAC43520.1; -; Genomic_DNA.
DR EMBL; U35819; AAC43521.1; -; Genomic_DNA.
DR EMBL; U35820; AAC43522.1; -; Genomic_DNA.
DR EMBL; U35821; AAC43523.1; -; Genomic_DNA.
DR EMBL; U35822; AAC43524.1; -; Genomic_DNA.
DR EMBL; U35823; AAC43525.1; -; Genomic_DNA.
DR EMBL; U35824; AAC43526.1; -; Genomic_DNA.
DR EMBL; U35825; AAC43527.1; -; Genomic_DNA.
DR EMBL; U36828; AAC43528.1; -; Genomic_DNA.
DR EMBL; U36829; AAC43529.1; -; Genomic_DNA.
DR EMBL; U36830; AAC43530.1; -; Genomic_DNA.
DR EMBL; U36831; AAC43531.1; -; Genomic_DNA.
DR EMBL; U36832; AAC43532.1; -; Genomic_DNA.
DR EMBL; U36833; AAC43533.1; -; Genomic_DNA.
DR EMBL; U36834; AAC43534.1; -; Genomic_DNA.
DR EMBL; U36835; AAC43535.1; -; Genomic_DNA.
DR EMBL; U35662; AAA82614.1; -; Genomic_DNA.
DR PIR; A39292; A39292.
DR RefSeq; NP_418297.1; NC_000913.3.
DR RefSeq; WP_000725337.1; NZ_SSZK01000026.1.
DR PDB; 1A23; NMR; -; A=20-208.
DR PDB; 1A24; NMR; -; A=20-208.
DR PDB; 1A2J; X-ray; 2.00 A; A=20-208.
DR PDB; 1A2L; X-ray; 2.70 A; A/B=20-208.
DR PDB; 1A2M; X-ray; 2.70 A; A/B=20-208.
DR PDB; 1AC1; X-ray; 2.00 A; A/B=20-208.
DR PDB; 1ACV; X-ray; 1.90 A; A/B=20-208.
DR PDB; 1BQ7; X-ray; 2.80 A; A/B/C/D/E/F=20-208.
DR PDB; 1DSB; X-ray; 2.00 A; A/B=20-208.
DR PDB; 1FVJ; X-ray; 2.06 A; A/B=20-208.
DR PDB; 1FVK; X-ray; 1.70 A; A/B=20-208.
DR PDB; 1TI1; X-ray; 2.60 A; A=20-208.
DR PDB; 1U3A; X-ray; 2.00 A; A/B/D/E=20-208.
DR PDB; 1UN2; X-ray; 2.40 A; A=20-208.
DR PDB; 2B3S; X-ray; 1.96 A; A/B=20-208.
DR PDB; 2B6M; X-ray; 2.65 A; A/B=20-208.
DR PDB; 2HI7; X-ray; 3.70 A; A=20-208.
DR PDB; 2LEG; NMR; -; A=20-208.
DR PDB; 2NDO; NMR; -; A=20-208.
DR PDB; 2ZUP; X-ray; 3.70 A; A=20-208.
DR PDB; 3E9J; X-ray; 3.70 A; B/E=20-208.
DR PDB; 4TKY; X-ray; 2.50 A; A/B/C/D=20-208.
DR PDB; 4ZIJ; X-ray; 1.78 A; A/B=20-207.
DR PDB; 5QKC; X-ray; 2.15 A; A/B=20-208.
DR PDB; 5QKD; X-ray; 2.11 A; A/B=20-208.
DR PDB; 5QKE; X-ray; 2.12 A; A/B=20-208.
DR PDB; 5QKF; X-ray; 2.14 A; A/B=20-208.
DR PDB; 5QKG; X-ray; 1.90 A; A/B=20-208.
DR PDB; 5QKH; X-ray; 2.65 A; A/B=20-208.
DR PDB; 5QKI; X-ray; 2.30 A; A/B=20-208.
DR PDB; 5QKJ; X-ray; 2.13 A; A/B=20-208.
DR PDB; 5QKK; X-ray; 2.08 A; A/B=20-208.
DR PDB; 5QKL; X-ray; 2.70 A; A/B=20-208.
DR PDB; 5QKM; X-ray; 2.49 A; A/B=20-208.
DR PDB; 5QKN; X-ray; 1.90 A; A/B=20-208.
DR PDB; 5QKO; X-ray; 2.00 A; A/B=20-208.
DR PDB; 5QKP; X-ray; 1.88 A; A/B=20-208.
DR PDB; 5QKQ; X-ray; 2.42 A; A/B=20-208.
DR PDB; 5QKR; X-ray; 2.50 A; A/B=20-208.
DR PDB; 5QKS; X-ray; 2.12 A; A/B=20-208.
DR PDB; 5QKT; X-ray; 1.90 A; A/B=20-208.
DR PDB; 5QKU; X-ray; 2.31 A; A/B=20-208.
DR PDB; 5QKV; X-ray; 2.14 A; A/B=20-208.
DR PDB; 5QKW; X-ray; 1.97 A; A/B=20-208.
DR PDB; 5QKX; X-ray; 2.00 A; A/B=20-208.
DR PDB; 5QKY; X-ray; 2.42 A; A/B=20-208.
DR PDB; 5QKZ; X-ray; 2.38 A; A/B=20-208.
DR PDB; 5QL0; X-ray; 2.04 A; A/B=20-208.
DR PDB; 5QL1; X-ray; 2.14 A; A/B=20-208.
DR PDB; 5QL2; X-ray; 2.11 A; A/B=20-208.
DR PDB; 5QL3; X-ray; 1.96 A; A/B=20-208.
DR PDB; 5QL4; X-ray; 2.01 A; A/B=20-208.
DR PDB; 5QL5; X-ray; 2.14 A; A/B=20-208.
DR PDB; 5QL6; X-ray; 2.08 A; A/B=20-208.
DR PDB; 5QL7; X-ray; 2.15 A; A/B=20-208.
DR PDB; 5QL8; X-ray; 2.30 A; A/B=20-208.
DR PDB; 5QL9; X-ray; 2.15 A; A/B=20-208.
DR PDB; 5QLA; X-ray; 1.86 A; A/B=20-208.
DR PDB; 5QLB; X-ray; 1.96 A; A/B=20-208.
DR PDB; 5QLC; X-ray; 2.21 A; A/B=20-208.
DR PDB; 5QLD; X-ray; 2.12 A; A/B=20-208.
DR PDB; 5QLE; X-ray; 1.95 A; A/B=20-208.
DR PDB; 5QLF; X-ray; 2.00 A; A/B=20-208.
DR PDB; 5QLG; X-ray; 2.48 A; A/B=20-208.
DR PDB; 5QLH; X-ray; 1.89 A; A/B=20-208.
DR PDB; 5QLI; X-ray; 2.04 A; A/B=20-208.
DR PDB; 5QLJ; X-ray; 1.96 A; A/B=20-208.
DR PDB; 5QLK; X-ray; 1.99 A; A/B=20-208.
DR PDB; 5QLL; X-ray; 1.96 A; A/B=20-208.
DR PDB; 5QLM; X-ray; 2.07 A; A/B=20-208.
DR PDB; 5QLN; X-ray; 2.41 A; A/B=20-208.
DR PDB; 5QLO; X-ray; 2.37 A; A/B=20-208.
DR PDB; 5QLP; X-ray; 2.52 A; A/B=20-208.
DR PDB; 5QLQ; X-ray; 1.87 A; A/B=20-208.
DR PDB; 5QLR; X-ray; 1.97 A; A/B=20-208.
DR PDB; 5QLS; X-ray; 2.01 A; A/B=20-208.
DR PDB; 5QLT; X-ray; 2.40 A; A/B=20-208.
DR PDB; 5QLU; X-ray; 2.20 A; A/B=20-208.
DR PDB; 5QLV; X-ray; 2.34 A; A/B=20-208.
DR PDB; 5QLW; X-ray; 1.96 A; A/B=20-208.
DR PDB; 5QLX; X-ray; 1.90 A; A/B=20-208.
DR PDB; 5QLY; X-ray; 2.17 A; A/B=20-208.
DR PDB; 5QLZ; X-ray; 2.00 A; A/B=20-208.
DR PDB; 5QM0; X-ray; 1.92 A; A/B=20-208.
DR PDB; 5QM1; X-ray; 1.96 A; A/B=20-208.
DR PDB; 5QM2; X-ray; 1.92 A; A/B=20-208.
DR PDB; 5QM3; X-ray; 1.98 A; A/B=20-208.
DR PDB; 5QM4; X-ray; 2.01 A; A/B=20-208.
DR PDB; 5QM5; X-ray; 2.01 A; A/B=20-208.
DR PDB; 5QM6; X-ray; 2.30 A; A/B=20-208.
DR PDB; 5QM7; X-ray; 2.04 A; A/B=20-208.
DR PDB; 5QM8; X-ray; 1.96 A; A/B=20-208.
DR PDB; 5QM9; X-ray; 1.96 A; A/B=20-208.
DR PDB; 5QMA; X-ray; 2.14 A; A/B=20-208.
DR PDB; 5QMB; X-ray; 1.90 A; A/B=20-208.
DR PDB; 5QMC; X-ray; 1.89 A; A/B=20-208.
DR PDB; 5QMD; X-ray; 1.97 A; A/B=20-208.
DR PDB; 5QME; X-ray; 1.83 A; A/B=20-208.
DR PDB; 5QMF; X-ray; 2.00 A; A/B=20-208.
DR PDB; 5QMG; X-ray; 2.11 A; A/B=20-208.
DR PDB; 5QMH; X-ray; 2.08 A; A/B=20-208.
DR PDB; 5QMI; X-ray; 1.67 A; A/B=20-208.
DR PDB; 5QMJ; X-ray; 2.30 A; A/B=20-208.
DR PDB; 5QMK; X-ray; 1.84 A; A/B=20-208.
DR PDB; 5QML; X-ray; 2.19 A; A/B=20-208.
DR PDB; 5QMM; X-ray; 1.96 A; A/B=20-208.
DR PDB; 5QMN; X-ray; 1.98 A; A/B=20-208.
DR PDB; 5QMO; X-ray; 2.05 A; A/B=20-208.
DR PDB; 5QMP; X-ray; 2.00 A; A/B=20-208.
DR PDB; 5QMQ; X-ray; 1.90 A; A/B=20-208.
DR PDB; 5QMR; X-ray; 2.00 A; A/B=20-208.
DR PDB; 5QMS; X-ray; 2.05 A; A/B=20-208.
DR PDB; 5QMT; X-ray; 2.04 A; A/B=20-208.
DR PDB; 5QMU; X-ray; 2.04 A; A/B=20-208.
DR PDB; 5QMV; X-ray; 1.91 A; A/B=20-208.
DR PDB; 5QMW; X-ray; 1.96 A; A/B=20-208.
DR PDB; 5QMX; X-ray; 1.92 A; A/B=20-208.
DR PDB; 5QMY; X-ray; 2.22 A; A/B=20-208.
DR PDB; 5QMZ; X-ray; 2.08 A; A/B=20-208.
DR PDB; 5QN0; X-ray; 2.01 A; A/B=20-208.
DR PDB; 5QN1; X-ray; 2.20 A; A/B=20-208.
DR PDB; 5QN2; X-ray; 2.30 A; A/B=20-208.
DR PDB; 5QN3; X-ray; 2.14 A; A/B=20-208.
DR PDB; 5QN4; X-ray; 2.37 A; A/B=20-208.
DR PDB; 5QN5; X-ray; 1.89 A; A/B=20-208.
DR PDB; 5QN6; X-ray; 1.90 A; A/B=20-208.
DR PDB; 5QN7; X-ray; 2.14 A; A/B=20-208.
DR PDB; 5QN8; X-ray; 1.87 A; A/B=20-208.
DR PDB; 5QN9; X-ray; 1.94 A; A/B=20-208.
DR PDB; 5QNA; X-ray; 2.14 A; A/B=20-208.
DR PDB; 5QNB; X-ray; 1.91 A; A/B=20-208.
DR PDB; 5QNC; X-ray; 2.14 A; A/B=20-208.
DR PDB; 5QND; X-ray; 1.90 A; A/B=20-208.
DR PDB; 5QNE; X-ray; 2.39 A; A/B=20-208.
DR PDB; 5QNF; X-ray; 1.96 A; A/B=20-208.
DR PDB; 5QNG; X-ray; 1.90 A; A/B=20-208.
DR PDB; 5QNH; X-ray; 2.21 A; A/B=20-208.
DR PDB; 5QNI; X-ray; 1.97 A; A/B=20-208.
DR PDB; 5QNJ; X-ray; 1.86 A; A/B=20-208.
DR PDB; 5QNK; X-ray; 1.90 A; A/B=20-208.
DR PDB; 5QNL; X-ray; 1.75 A; A/B=20-208.
DR PDB; 5QNM; X-ray; 1.86 A; A/B=20-208.
DR PDB; 5QNN; X-ray; 1.79 A; A/B=20-208.
DR PDB; 5QNO; X-ray; 1.95 A; A/B=20-208.
DR PDB; 5QNP; X-ray; 1.67 A; A/B=20-208.
DR PDB; 5QNQ; X-ray; 1.67 A; A/B=20-208.
DR PDB; 5QNR; X-ray; 1.75 A; A/B=20-208.
DR PDB; 5QNS; X-ray; 1.78 A; A/B=20-208.
DR PDB; 5QNT; X-ray; 1.75 A; A/B=20-208.
DR PDB; 5QNU; X-ray; 1.86 A; A/B=20-208.
DR PDB; 5QNV; X-ray; 1.75 A; A/B=20-208.
DR PDB; 5QNW; X-ray; 1.88 A; A/B=20-208.
DR PDB; 5QNX; X-ray; 1.68 A; A/B=20-208.
DR PDB; 5QNY; X-ray; 1.59 A; A/B=20-208.
DR PDB; 5QNZ; X-ray; 1.79 A; A/B=20-208.
DR PDB; 5QO0; X-ray; 1.83 A; A/B=20-208.
DR PDB; 5QO1; X-ray; 1.84 A; A/B=20-208.
DR PDB; 5QO2; X-ray; 1.64 A; A/B=20-208.
DR PDB; 5QO3; X-ray; 1.73 A; A/B=20-208.
DR PDB; 5QO4; X-ray; 1.78 A; A/B=20-208.
DR PDB; 5QO5; X-ray; 1.77 A; A/B=20-208.
DR PDB; 5QO6; X-ray; 1.79 A; A/B=20-208.
DR PDB; 5QO7; X-ray; 1.97 A; A/B=20-208.
DR PDB; 5QO8; X-ray; 1.73 A; A/B=20-208.
DR PDB; 5QO9; X-ray; 1.59 A; A/B=20-208.
DR PDB; 5QOA; X-ray; 1.98 A; A/B=20-208.
DR PDB; 5QOB; X-ray; 1.70 A; A/B=20-208.
DR PDB; 5QOC; X-ray; 1.67 A; A/B=20-208.
DR PDB; 5QOD; X-ray; 1.91 A; A/B=20-208.
DR PDB; 5QOE; X-ray; 1.67 A; A/B=20-208.
DR PDB; 5QOF; X-ray; 1.64 A; A/B=20-208.
DR PDB; 5QOG; X-ray; 1.79 A; A/B=20-208.
DR PDB; 6BQX; X-ray; 1.99 A; A/B=20-208.
DR PDB; 6BR4; X-ray; 1.99 A; A/B=20-208.
DR PDB; 6PBI; X-ray; 1.90 A; A/B=20-208.
DR PDB; 6PC9; X-ray; 2.30 A; A/B=20-208.
DR PDB; 6PD7; X-ray; 1.92 A; A/B=20-208.
DR PDB; 6PDH; X-ray; 1.96 A; A/B=20-208.
DR PDB; 6PG1; X-ray; 2.01 A; A/B=20-208.
DR PDB; 6PG2; X-ray; 1.91 A; A/B=20-208.
DR PDB; 6PGJ; X-ray; 1.90 A; A/B=20-208.
DR PDB; 6PIQ; X-ray; 2.10 A; A/B=20-208.
DR PDB; 6PLI; X-ray; 1.93 A; A/B=20-208.
DR PDB; 6PMF; X-ray; 1.95 A; A/B=20-208.
DR PDB; 6PML; X-ray; 2.00 A; A/B=20-208.
DR PDB; 6POH; X-ray; 1.67 A; A/B=20-208.
DR PDB; 6POI; X-ray; 1.77 A; A/B=20-208.
DR PDB; 6POQ; X-ray; 1.80 A; A/B=20-208.
DR PDB; 6PVY; X-ray; 1.74 A; A/B=20-208.
DR PDB; 6PVZ; X-ray; 1.99 A; A/B=20-208.
DR PDB; 6WHD; X-ray; 1.99 A; A/B=20-208.
DR PDB; 6XSP; X-ray; 2.30 A; A/B=20-208.
DR PDB; 6XSQ; X-ray; 2.30 A; A/B=20-208.
DR PDB; 6XT3; X-ray; 1.99 A; A/B=20-208.
DR PDB; 7L76; X-ray; 1.83 A; A/B=20-208.
DR PDB; 7L7C; X-ray; 1.80 A; A/B=20-208.
DR PDB; 7LHP; X-ray; 1.90 A; A/B=20-208.
DR PDB; 7LSM; X-ray; 1.79 A; A=20-208.
DR PDBsum; 1A23; -.
DR PDBsum; 1A24; -.
DR PDBsum; 1A2J; -.
DR PDBsum; 1A2L; -.
DR PDBsum; 1A2M; -.
DR PDBsum; 1AC1; -.
DR PDBsum; 1ACV; -.
DR PDBsum; 1BQ7; -.
DR PDBsum; 1DSB; -.
DR PDBsum; 1FVJ; -.
DR PDBsum; 1FVK; -.
DR PDBsum; 1TI1; -.
DR PDBsum; 1U3A; -.
DR PDBsum; 1UN2; -.
DR PDBsum; 2B3S; -.
DR PDBsum; 2B6M; -.
DR PDBsum; 2HI7; -.
DR PDBsum; 2LEG; -.
DR PDBsum; 2NDO; -.
DR PDBsum; 2ZUP; -.
DR PDBsum; 3E9J; -.
DR PDBsum; 4TKY; -.
DR PDBsum; 4ZIJ; -.
DR PDBsum; 5QKC; -.
DR PDBsum; 5QKD; -.
DR PDBsum; 5QKE; -.
DR PDBsum; 5QKF; -.
DR PDBsum; 5QKG; -.
DR PDBsum; 5QKH; -.
DR PDBsum; 5QKI; -.
DR PDBsum; 5QKJ; -.
DR PDBsum; 5QKK; -.
DR PDBsum; 5QKL; -.
DR PDBsum; 5QKM; -.
DR PDBsum; 5QKN; -.
DR PDBsum; 5QKO; -.
DR PDBsum; 5QKP; -.
DR PDBsum; 5QKQ; -.
DR PDBsum; 5QKR; -.
DR PDBsum; 5QKS; -.
DR PDBsum; 5QKT; -.
DR PDBsum; 5QKU; -.
DR PDBsum; 5QKV; -.
DR PDBsum; 5QKW; -.
DR PDBsum; 5QKX; -.
DR PDBsum; 5QKY; -.
DR PDBsum; 5QKZ; -.
DR PDBsum; 5QL0; -.
DR PDBsum; 5QL1; -.
DR PDBsum; 5QL2; -.
DR PDBsum; 5QL3; -.
DR PDBsum; 5QL4; -.
DR PDBsum; 5QL5; -.
DR PDBsum; 5QL6; -.
DR PDBsum; 5QL7; -.
DR PDBsum; 5QL8; -.
DR PDBsum; 5QL9; -.
DR PDBsum; 5QLA; -.
DR PDBsum; 5QLB; -.
DR PDBsum; 5QLC; -.
DR PDBsum; 5QLD; -.
DR PDBsum; 5QLE; -.
DR PDBsum; 5QLF; -.
DR PDBsum; 5QLG; -.
DR PDBsum; 5QLH; -.
DR PDBsum; 5QLI; -.
DR PDBsum; 5QLJ; -.
DR PDBsum; 5QLK; -.
DR PDBsum; 5QLL; -.
DR PDBsum; 5QLM; -.
DR PDBsum; 5QLN; -.
DR PDBsum; 5QLO; -.
DR PDBsum; 5QLP; -.
DR PDBsum; 5QLQ; -.
DR PDBsum; 5QLR; -.
DR PDBsum; 5QLS; -.
DR PDBsum; 5QLT; -.
DR PDBsum; 5QLU; -.
DR PDBsum; 5QLV; -.
DR PDBsum; 5QLW; -.
DR PDBsum; 5QLX; -.
DR PDBsum; 5QLY; -.
DR PDBsum; 5QLZ; -.
DR PDBsum; 5QM0; -.
DR PDBsum; 5QM1; -.
DR PDBsum; 5QM2; -.
DR PDBsum; 5QM3; -.
DR PDBsum; 5QM4; -.
DR PDBsum; 5QM5; -.
DR PDBsum; 5QM6; -.
DR PDBsum; 5QM7; -.
DR PDBsum; 5QM8; -.
DR PDBsum; 5QM9; -.
DR PDBsum; 5QMA; -.
DR PDBsum; 5QMB; -.
DR PDBsum; 5QMC; -.
DR PDBsum; 5QMD; -.
DR PDBsum; 5QME; -.
DR PDBsum; 5QMF; -.
DR PDBsum; 5QMG; -.
DR PDBsum; 5QMH; -.
DR PDBsum; 5QMI; -.
DR PDBsum; 5QMJ; -.
DR PDBsum; 5QMK; -.
DR PDBsum; 5QML; -.
DR PDBsum; 5QMM; -.
DR PDBsum; 5QMN; -.
DR PDBsum; 5QMO; -.
DR PDBsum; 5QMP; -.
DR PDBsum; 5QMQ; -.
DR PDBsum; 5QMR; -.
DR PDBsum; 5QMS; -.
DR PDBsum; 5QMT; -.
DR PDBsum; 5QMU; -.
DR PDBsum; 5QMV; -.
DR PDBsum; 5QMW; -.
DR PDBsum; 5QMX; -.
DR PDBsum; 5QMY; -.
DR PDBsum; 5QMZ; -.
DR PDBsum; 5QN0; -.
DR PDBsum; 5QN1; -.
DR PDBsum; 5QN2; -.
DR PDBsum; 5QN3; -.
DR PDBsum; 5QN4; -.
DR PDBsum; 5QN5; -.
DR PDBsum; 5QN6; -.
DR PDBsum; 5QN7; -.
DR PDBsum; 5QN8; -.
DR PDBsum; 5QN9; -.
DR PDBsum; 5QNA; -.
DR PDBsum; 5QNB; -.
DR PDBsum; 5QNC; -.
DR PDBsum; 5QND; -.
DR PDBsum; 5QNE; -.
DR PDBsum; 5QNF; -.
DR PDBsum; 5QNG; -.
DR PDBsum; 5QNH; -.
DR PDBsum; 5QNI; -.
DR PDBsum; 5QNJ; -.
DR PDBsum; 5QNK; -.
DR PDBsum; 5QNL; -.
DR PDBsum; 5QNM; -.
DR PDBsum; 5QNN; -.
DR PDBsum; 5QNO; -.
DR PDBsum; 5QNP; -.
DR PDBsum; 5QNQ; -.
DR PDBsum; 5QNR; -.
DR PDBsum; 5QNS; -.
DR PDBsum; 5QNT; -.
DR PDBsum; 5QNU; -.
DR PDBsum; 5QNV; -.
DR PDBsum; 5QNW; -.
DR PDBsum; 5QNX; -.
DR PDBsum; 5QNY; -.
DR PDBsum; 5QNZ; -.
DR PDBsum; 5QO0; -.
DR PDBsum; 5QO1; -.
DR PDBsum; 5QO2; -.
DR PDBsum; 5QO3; -.
DR PDBsum; 5QO4; -.
DR PDBsum; 5QO5; -.
DR PDBsum; 5QO6; -.
DR PDBsum; 5QO7; -.
DR PDBsum; 5QO8; -.
DR PDBsum; 5QO9; -.
DR PDBsum; 5QOA; -.
DR PDBsum; 5QOB; -.
DR PDBsum; 5QOC; -.
DR PDBsum; 5QOD; -.
DR PDBsum; 5QOE; -.
DR PDBsum; 5QOF; -.
DR PDBsum; 5QOG; -.
DR PDBsum; 6BQX; -.
DR PDBsum; 6BR4; -.
DR PDBsum; 6PBI; -.
DR PDBsum; 6PC9; -.
DR PDBsum; 6PD7; -.
DR PDBsum; 6PDH; -.
DR PDBsum; 6PG1; -.
DR PDBsum; 6PG2; -.
DR PDBsum; 6PGJ; -.
DR PDBsum; 6PIQ; -.
DR PDBsum; 6PLI; -.
DR PDBsum; 6PMF; -.
DR PDBsum; 6PML; -.
DR PDBsum; 6POH; -.
DR PDBsum; 6POI; -.
DR PDBsum; 6POQ; -.
DR PDBsum; 6PVY; -.
DR PDBsum; 6PVZ; -.
DR PDBsum; 6WHD; -.
DR PDBsum; 6XSP; -.
DR PDBsum; 6XSQ; -.
DR PDBsum; 6XT3; -.
DR PDBsum; 7L76; -.
DR PDBsum; 7L7C; -.
DR PDBsum; 7LHP; -.
DR PDBsum; 7LSM; -.
DR AlphaFoldDB; P0AEG4; -.
DR BMRB; P0AEG4; -.
DR SMR; P0AEG4; -.
DR BioGRID; 4261200; 185.
DR DIP; DIP-35886N; -.
DR IntAct; P0AEG4; 20.
DR MINT; P0AEG4; -.
DR STRING; 511145.b3860; -.
DR BindingDB; P0AEG4; -.
DR ChEMBL; CHEMBL3559645; -.
DR DrugBank; DB08689; Ubiquinone Q1.
DR SWISS-2DPAGE; P0AEG4; -.
DR jPOST; P0AEG4; -.
DR PaxDb; P0AEG4; -.
DR PRIDE; P0AEG4; -.
DR EnsemblBacteria; AAC76858; AAC76858; b3860.
DR EnsemblBacteria; BAE77448; BAE77448; BAE77448.
DR GeneID; 66672234; -.
DR GeneID; 948353; -.
DR KEGG; ecj:JW3832; -.
DR KEGG; eco:b3860; -.
DR PATRIC; fig|1411691.4.peg.2855; -.
DR EchoBASE; EB1274; -.
DR eggNOG; COG1651; Bacteria.
DR HOGENOM; CLU_088255_3_0_6; -.
DR InParanoid; P0AEG4; -.
DR OMA; NAIHKQK; -.
DR PhylomeDB; P0AEG4; -.
DR BioCyc; EcoCyc:DISULFOXRED-MON; -.
DR BioCyc; MetaCyc:DISULFOXRED-MON; -.
DR BRENDA; 1.8.4.15; 2026.
DR EvolutionaryTrace; P0AEG4; -.
DR PRO; PR:P0AEG4; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IDA:EcoliWiki.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IDA:EcoCyc.
DR GO; GO:0071236; P:cellular response to antibiotic; IMP:EcoliWiki.
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 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; Direct protein sequencing; Disulfide bond; Periplasm;
KW Redox-active center; Reference proteome; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:8494885,
FT ECO:0000269|PubMed:9298646, ECO:0000269|PubMed:9600841"
FT CHAIN 20..208
FT /note="Thiol:disulfide interchange protein DsbA"
FT /id="PRO_0000034252"
FT DOMAIN 20..150
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:9300489"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:5QO9"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:5QO9"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:5QO9"
FT HELIX 50..57
FT /evidence="ECO:0007829|PDB:5QO9"
FT HELIX 61..66
FT /evidence="ECO:0007829|PDB:5QO9"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:5QO9"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:5QO9"
FT HELIX 85..101
FT /evidence="ECO:0007829|PDB:5QO9"
FT HELIX 104..116
FT /evidence="ECO:0007829|PDB:5QO9"
FT HELIX 124..133
FT /evidence="ECO:0007829|PDB:5QO9"
FT HELIX 138..145
FT /evidence="ECO:0007829|PDB:5QO9"
FT HELIX 148..163
FT /evidence="ECO:0007829|PDB:5QO9"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:5QO9"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:5QO9"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:5QO9"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:5QO9"
FT HELIX 190..205
FT /evidence="ECO:0007829|PDB:5QO9"
SQ SEQUENCE 208 AA; 23105 MW; 10527E876FCAEE55 CRC64;
MKKIWLALAG LVLAFSASAA QYEDGKQYTT LEKPVAGAPQ VLEFFSFFCP HCYQFEEVLH
ISDNVKKKLP EGVKMTKYHV NFMGGDLGKD LTQAWAVAMA LGVEDKVTVP LFEGVQKTQT
IRSASDIRDV FINAGIKGEE YDAAWNSFVV KSLVAQQEKA AADVQLRGVP AMFVNGKYQL
NPQGMDTSNM DVFVQQYADT VKYLSEKK
