Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P0AEG4

- DSBA_ECOLI

UniProt

P0AEG4 - DSBA_ECOLI

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 1 (06 Dec 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 binding Source: IntAct
    2. protein disulfide isomerase activity Source: EcoliWiki
    3. 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

    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

    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.
    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

    MKKIWLALAG LVLAFSASAA QYEDGKQYTT LEKPVAGAPQ VLEFFSFFCP    50
    HCYQFEEVLH ISDNVKKKLP EGVKMTKYHV NFMGGDLGKD LTQAWAVAMA 100
    LGVEDKVTVP LFEGVQKTQT IRSASDIRDV FINAGIKGEE YDAAWNSFVV 150
    KSLVAQQEKA AADVQLRGVP AMFVNGKYQL NPQGMDTSNM DVFVQQYADT 200
    VKYLSEKK 208
    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.
    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

    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 1, 2014
    This is version 85 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