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P0AEG4

- DSBA_ECOLI

UniProt

P0AEG4 - DSBA_ECOLI

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Protein

Thiol:disulfide interchange protein DsbA

Gene

dsbA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  1. protein disulfide isomerase activity Source: EcoliWiki
  2. protein disulfide oxidoreductase activity Source: EcoCyc

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. cellular response to antibiotic Source: EcoliWiki
  3. oxidation-reduction process Source: GOC
  4. protein folding Source: GOC
Complete GO annotation...

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Thiol:disulfide interchange protein DsbA
Gene namesi
Name:dsbA
Synonyms:dsf, ppfA
Ordered Locus Names:b3860, JW3832
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11297. dsbA.

Subcellular locationi

GO - Cellular componenti

  1. outer membrane-bounded periplasmic space Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Disruption phenotypei

Induction of the PhoP/PhoQ two-component regulatory system, suppressed by 50 µM CuSO4.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19193 PublicationsAdd
BLAST
Chaini20 – 208189Thiol:disulfide interchange protein DsbAPRO_0000034252Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi49 ↔ 52Redox-active1 PublicationPROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP0AEG4.
PRIDEiP0AEG4.

2D gel databases

SWISS-2DPAGEP0AEG4.

Expressioni

Gene expression databases

GenevestigatoriP0AEG4.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
dsbBP0A6M25EBI-549711,EBI-1170740
phoAP006342EBI-549711,EBI-552958

Protein-protein interaction databases

DIPiDIP-35886N.
IntActiP0AEG4. 19 interactions.
MINTiMINT-1247943.
STRINGi511145.b3860.

Structurei

Secondary structure

1
208
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni25 – 273
Beta strandi28 – 303
Beta strandi40 – 456
Helixi50 – 578
Helixi61 – 666
Beta strandi75 – 795
Beta strandi81 – 844
Helixi85 – 10117
Helixi104 – 11613
Helixi124 – 13310
Helixi138 – 1469
Helixi148 – 16316
Beta strandi168 – 1747
Turni175 – 1773
Beta strandi178 – 1803
Helixi182 – 1843
Helixi190 – 20516

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP0AEG4.
SMRiP0AEG4. Positions 20-207.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AEG4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 150131ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the thioredoxin family. DsbA subfamily.Curated
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Signal

Phylogenomic databases

eggNOGiCOG0526.
HOGENOMiHOG000265316.
InParanoidiP0AEG4.
KOiK03673.
OMAiQVMEFFS.
OrthoDBiEOG68Q0Q6.
PhylomeDBiP0AEG4.

Family and domain databases

Gene3Di3.40.30.10. 2 hits.
InterProiIPR001853. DSBA-like_thioredoxin_dom.
IPR023205. DsbA/DsbL.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
[Graphical view]
PfamiPF01323. DSBA. 1 hit.
[Graphical view]
PIRSFiPIRSF001488. Tdi_protein. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AEG4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKKIWLALAG LVLAFSASAA QYEDGKQYTT LEKPVAGAPQ VLEFFSFFCP
60 70 80 90 100
HCYQFEEVLH ISDNVKKKLP EGVKMTKYHV NFMGGDLGKD LTQAWAVAMA
110 120 130 140 150
LGVEDKVTVP LFEGVQKTQT IRSASDIRDV FINAGIKGEE YDAAWNSFVV
160 170 180 190 200
KSLVAQQEKA AADVQLRGVP AMFVNGKYQL NPQGMDTSNM DVFVQQYADT

VKYLSEKK
Length:208
Mass (Da):23,105
Last modified:December 6, 2005 - v1
Checksum:i10527E876FCAEE55
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiA39292.
RefSeqiNP_418297.1. NC_000913.3.
YP_491589.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76858; AAC76858; b3860.
BAE77448; BAE77448; BAE77448.
GeneIDi12932206.
948353.
KEGGiecj:Y75_p3325.
eco:b3860.
PATRICi32123217. VBIEscCol129921_3969.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi A39292.
RefSeqi NP_418297.1. NC_000913.3.
YP_491589.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A23 NMR - A 20-208 [» ]
1A24 NMR - A 20-208 [» ]
1A2J X-ray 2.00 A 20-208 [» ]
1A2L X-ray 2.70 A/B 20-208 [» ]
1A2M X-ray 2.70 A/B 20-208 [» ]
1AC1 X-ray 2.00 A/B 20-208 [» ]
1ACV X-ray 1.90 A/B 20-208 [» ]
1BQ7 X-ray 2.80 A/B/C/D/E/F 20-208 [» ]
1DSB X-ray 2.00 A/B 20-208 [» ]
1FVJ X-ray 2.06 A/B 20-208 [» ]
1FVK X-ray 1.70 A/B 20-208 [» ]
1TI1 X-ray 2.60 A 20-208 [» ]
1U3A X-ray 2.00 A/B/D/E 20-208 [» ]
1UN2 X-ray 2.40 A 20-118 [» ]
2B3S X-ray 1.96 A/B 20-208 [» ]
2B6M X-ray 2.65 A/B 20-208 [» ]
2HI7 X-ray 3.70 A 20-208 [» ]
2LEG NMR - A 20-208 [» ]
2ZUP X-ray 3.70 A 20-208 [» ]
3E9J X-ray 3.70 B/E 20-208 [» ]
ProteinModelPortali P0AEG4.
SMRi P0AEG4. Positions 20-207.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-35886N.
IntActi P0AEG4. 19 interactions.
MINTi MINT-1247943.
STRINGi 511145.b3860.

2D gel databases

SWISS-2DPAGE P0AEG4.

Proteomic databases

PaxDbi P0AEG4.
PRIDEi P0AEG4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76858 ; AAC76858 ; b3860 .
BAE77448 ; BAE77448 ; BAE77448 .
GeneIDi 12932206.
948353.
KEGGi ecj:Y75_p3325.
eco:b3860.
PATRICi 32123217. VBIEscCol129921_3969.

Organism-specific databases

EchoBASEi EB1274.
EcoGenei EG11297. dsbA.

Phylogenomic databases

eggNOGi COG0526.
HOGENOMi HOG000265316.
InParanoidi P0AEG4.
KOi K03673.
OMAi QVMEFFS.
OrthoDBi EOG68Q0Q6.
PhylomeDBi P0AEG4.

Enzyme and pathway databases

BioCyci EcoCyc:DISULFOXRED-MONOMER.
ECOL316407:JW3832-MONOMER.
MetaCyc:DISULFOXRED-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0AEG4.
PROi P0AEG4.

Gene expression databases

Genevestigatori P0AEG4.

Family and domain databases

Gene3Di 3.40.30.10. 2 hits.
InterProi IPR001853. DSBA-like_thioredoxin_dom.
IPR023205. DsbA/DsbL.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
[Graphical view ]
Pfami PF01323. DSBA. 1 hit.
[Graphical view ]
PIRSFi PIRSF001488. Tdi_protein. 1 hit.
SUPFAMi SSF52833. SSF52833. 1 hit.
PROSITEi PS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: PROTEIN SEQUENCE OF 20-23.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  10. 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. 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.

Entry informationi

Entry nameiDSBA_ECOLI
AccessioniPrimary (citable) accession number: P0AEG4
Secondary accession number(s): P24991
, Q2M8F8, Q46951, Q46952
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: October 29, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3