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P0AEG4 (DSBA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thiol:disulfide interchange protein DsbA
Gene names
Name:dsbA
Synonyms:dsf, ppfA
Ordered Locus Names:b3860, JW3832
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length208 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbA is reoxidized by DsbB. Required for pilus biogenesis. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway. Ref.11 Ref.13

Subcellular location

Periplasm.

Disruption phenotype

Induction of the PhoP/PhoQ two-component regulatory system, suppressed by 50 µM CuSO4. Ref.13

Sequence similarities

Belongs to the thioredoxin family. DsbA subfamily.

Contains 1 thioredoxin domain.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.7 Ref.8 Ref.9
Chain20 – 208189Thiol:disulfide interchange protein DsbA
PRO_0000034252

Regions

Domain20 – 150131Thioredoxin

Amino acid modifications

Disulfide bond49 ↔ 52Redox-active Ref.16

Secondary structure

............................... 208
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AEG4 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 10527E876FCAEE55

FASTA20823,105
        10         20         30         40         50         60 
MKKIWLALAG LVLAFSASAA QYEDGKQYTT LEKPVAGAPQ VLEFFSFFCP HCYQFEEVLH 

        70         80         90        100        110        120 
ISDNVKKKLP EGVKMTKYHV NFMGGDLGKD LTQAWAVAMA LGVEDKVTVP LFEGVQKTQT 

       130        140        150        160        170        180 
IRSASDIRDV FINAGIKGEE YDAAWNSFVV KSLVAQQEKA AADVQLRGVP AMFVNGKYQL 

       190        200 
NPQGMDTSNM DVFVQQYADT VKYLSEKK 

« Hide

References

« Hide 'large scale' references
[1]"Identification of a protein required for disulfide bond formation in vivo."
Bardwell J.C.A., McGovern K., Beckwith J.
Cell 67:581-589(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme."
Kamitani S., Akiyama Y., Ito K.
EMBO J. 11:57-62(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[3]"Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes."
Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.
Nucleic Acids Res. 21:3391-3398(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]Grauschopf U., Winther J., Korber P., Zander T., Dallinger P., Bardwell J.C.A.
Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-49.
[7]"The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo."
Zapun A., Bardwell J.C.A., Creighton T.E.
Biochemistry 32:5083-5092(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-24, CHARACTERIZATION.
[8]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-31.
Strain: K12 / EMG2.
[9]"Protein identification with N and C-terminal sequence tags in proteome projects."
Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F.
J. Mol. Biol. 278:599-608(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-23.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[10]"Why is DsbA such an oxidizing disulfide catalyst?"
Grauschopf U., Winther J.R., Korber P., Zander T., Dallinger P., Bardwell J.C.A.
Cell 83:947-955(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF PRO-50 AND HIS-51.
[11]"In vitro catalysis of oxidative folding of disulfide-bonded proteins by the Escherichia coli dsbA (ppfA) gene product."
Akiyama Y., Kamitani S., Kusukawa N., Ito K.
J. Biol. Chem. 267:22440-22445(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[13]"Perturbation of the oxidizing environment of the periplasm stimulates the PhoQ/PhoP system in Escherichia coli."
Lippa A.M., Goulian M.
J. Bacteriol. 194:1457-1463(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOP/PHOQ REGULATION, DISRUPTION PHENOTYPE.
Strain: K12 / MG1655 / ATCC 47076.
[14]"Crystal structure of the DsbA protein required for disulphide bond formation in vivo."
Martin J.L., Bardwell J.C.A., Kuriyan J.
Nature 365:464-468(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[15]"The uncharged surface features surrounding the active site of Escherichia coli DsbA are conserved and are implicated in peptide binding."
Guddat L.W., Bardwell J.C.A., Zander T., Martin J.L.
Protein Sci. 6:1148-1156(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[16]"Structural analysis of three His32 mutants of DsbA: support for an electrostatic role of His32 in DsbA stability."
Guddat L.W., Bardwell J.C.A., Glockshuber R., Huber-Wunderlich M., Zander T., Martin J.L.
Protein Sci. 6:1893-1900(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF HIS-51 MUTANTS, DISULFIDE BOND.
[17]"Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization."
Guddat L.W., Bardwell J.C.A., Martin J.L.
Structure 6:757-767(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[18]"Structure of reduced DsbA from Escherichia coli in solution."
Schirra H.J., Renner C., Czisch M., Huber-Wunderlich M., Holak T.A., Glockshuber R.
Biochemistry 37:6263-6276(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[19]"On the role of the cis-proline residue in the active site of DsbA."
Charbonnier J.-B., Belin P., Moutiez M., Stura E.A., Quemeneur E.
Protein Sci. 8:96-105(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[20]"Intriguing conformation changes associated with the trans/cis isomerization of a prolyl residue in the active site of the DsbA C33A mutant."
Ondo-Mbele E., Vives C., Kone A., Serre L.
J. Mol. Biol. 347:555-563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT ALA-52 OF 20-208.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X80762 Genomic DNA. Translation: CAA56736.1.
M77746 Genomic DNA. Translation: AAA23715.1.
X63186 Genomic DNA. Translation: CAA44868.1.
L19201 Genomic DNA. Translation: AAB02995.1.
U00096 Genomic DNA. Translation: AAC76858.1.
AP009048 Genomic DNA. Translation: BAE77448.1.
U35817 Genomic DNA. Translation: AAC43519.1.
U35818 Genomic DNA. Translation: AAC43520.1.
U35819 Genomic DNA. Translation: AAC43521.1.
U35820 Genomic DNA. Translation: AAC43522.1.
U35821 Genomic DNA. Translation: AAC43523.1.
U35822 Genomic DNA. Translation: AAC43524.1.
U35823 Genomic DNA. Translation: AAC43525.1.
U35824 Genomic DNA. Translation: AAC43526.1.
U35825 Genomic DNA. Translation: AAC43527.1.
U36828 Genomic DNA. Translation: AAC43528.1.
U36829 Genomic DNA. Translation: AAC43529.1.
U36830 Genomic DNA. Translation: AAC43530.1.
U36831 Genomic DNA. Translation: AAC43531.1.
U36832 Genomic DNA. Translation: AAC43532.1.
U36833 Genomic DNA. Translation: AAC43533.1.
U36834 Genomic DNA. Translation: AAC43534.1.
U36835 Genomic DNA. Translation: AAC43535.1.
U35662 Genomic DNA. Translation: AAA82614.1.
PIRA39292.
RefSeqNP_418297.1. NC_000913.3.
YP_491589.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A23NMR-A20-208[»]
1A24NMR-A20-208[»]
1A2JX-ray2.00A20-208[»]
1A2LX-ray2.70A/B20-208[»]
1A2MX-ray2.70A/B20-208[»]
1AC1X-ray2.00A/B20-208[»]
1ACVX-ray1.90A/B20-208[»]
1BQ7X-ray2.80A/B/C/D/E/F20-208[»]
1DSBX-ray2.00A/B20-208[»]
1FVJX-ray2.06A/B20-208[»]
1FVKX-ray1.70A/B20-208[»]
1TI1X-ray2.60A20-208[»]
1U3AX-ray2.00A/B/D/E20-208[»]
1UN2X-ray2.40A20-118[»]
2B3SX-ray1.96A/B20-208[»]
2B6MX-ray2.65A/B20-208[»]
2HI7X-ray3.70A20-208[»]
2LEGNMR-A20-208[»]
2ZUPX-ray3.70A20-208[»]
3E9JX-ray3.70B/E20-208[»]
ProteinModelPortalP0AEG4.
SMRP0AEG4. Positions 20-207.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-35886N.
IntActP0AEG4. 19 interactions.
MINTMINT-1247943.
STRING511145.b3860.

2D gel databases

SWISS-2DPAGEP0AEG4.

Proteomic databases

PaxDbP0AEG4.
PRIDEP0AEG4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76858; AAC76858; b3860.
BAE77448; BAE77448; BAE77448.
GeneID12932206.
948353.
KEGGecj:Y75_p3325.
eco:b3860.
PATRIC32123217. VBIEscCol129921_3969.

Organism-specific databases

EchoBASEEB1274.
EcoGeneEG11297. dsbA.

Phylogenomic databases

eggNOGCOG0526.
HOGENOMHOG000265316.
KOK03673.
OMAQVMEFFS.
OrthoDBEOG68Q0Q6.
PhylomeDBP0AEG4.

Enzyme and pathway databases

BioCycEcoCyc:DISULFOXRED-MONOMER.
ECOL316407:JW3832-MONOMER.
MetaCyc:DISULFOXRED-MONOMER.

Gene expression databases

GenevestigatorP0AEG4.

Family and domain databases

Gene3D3.40.30.10. 2 hits.
InterProIPR001853. DSBA-like_thioredoxin_dom.
IPR023205. DsbA/DsbL.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
[Graphical view]
PfamPF01323. DSBA. 1 hit.
[Graphical view]
PIRSFPIRSF001488. Tdi_protein. 1 hit.
SUPFAMSSF52833. SSF52833. 1 hit.
PROSITEPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0AEG4.
PROP0AEG4.

Entry information

Entry nameDSBA_ECOLI
AccessionPrimary (citable) accession number: P0AEG4
Secondary accession number(s): P24991 expand/collapse secondary AC list , Q2M8F8, Q46951, Q46952
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: July 9, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene