Thiol:disulfide interchange protein DsbA

Details

Name
Thiol:disulfide interchange protein DsbA
Synonyms
  • dsf
  • ppfA
Gene Name
dsbA
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0013048|Thiol:disulfide interchange protein DsbA
MKKIWLALAGLVLAFSASAAQYEDGKQYTTLEKPVAGAPQVLEFFSFFCPHCYQFEEVLH
ISDNVKKKLPEGVKMTKYHVNFMGGDLGKDLTQAWAVAMALGVEDKVTVPLFEGVQKTQT
IRSASDIRDVFINAGIKGEEYDAAWNSFVVKSLVAQQEKAAADVQLRGVPAMFVNGKYQL
NPQGMDTSNMDVFVQQYADTVKYLSEKK
Number of residues
208
Molecular Weight
23104.435
Theoretical pI
6.27
GO Classification
Functions
protein disulfide isomerase activity / protein disulfide oxidoreductase activity
Processes
cell redox homeostasis / cellular response to antibiotic / oxidation-reduction process / protein folding
Components
outer membrane-bounded periplasmic space
General Function
Protein disulfide oxidoreductase activity
Specific 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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Periplasm
Gene sequence
>lcl|BSEQ0013049|Thiol:disulfide interchange protein DsbA (dsbA)
ATGAAAAAGATTTGGCTGGCGCTGGCTGGTTTAGTTTTAGCGTTTAGCGCATCGGCGGCG
CAGTATGAAGATGGTAAACAGTACACTACCCTGGAAAAACCGGTAGCTGGCGCGCCGCAA
GTGCTGGAGTTTTTCTCTTTCTTCTGCCCGCACTGCTATCAGTTTGAAGAAGTTCTGCAT
ATTTCTGATAATGTGAAGAAAAAACTGCCGGAAGGCGTGAAGATGACTAAATACCACGTC
AACTTCATGGGTGGTGACCTGGGCAAAGATCTGACTCAGGCATGGGCTGTGGCGATGGCG
CTGGGCGTGGAAGACAAAGTGACTGTTCCGCTGTTTGAAGGCGTACAGAAAACCCAGACC
ATTCGTTCTGCTTCTGATATCCGCGATGTATTTATCAACGCAGGTATTAAAGGTGAAGAG
TACGACGCGGCGTGGAACAGCTTCGTGGTGAAATCTCTGGTCGCTCAGCAGGAAAAAGCT
GCAGCTGACGTGCAATTGCGTGGCGTTCCGGCGATGTTTGTTAACGGTAAATATCAGCTG
AATCCGCAGGGTATGGATACCAGCAATATGGATGTTTTTGTTCAGCAGTATGCTGATACA
GTGAAATATCTGTCCGAGAAAAAATAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0AEG4
UniProtKB Entry NameDSBA_ECOLI
GenBank Protein ID762927
GenBank Gene IDX80762
General References
  1. Bardwell JC, McGovern K, Beckwith J: Identification of a protein required for disulfide bond formation in vivo. Cell. 1991 Nov 1;67(3):581-9. [Article]
  2. Kamitani S, Akiyama Y, Ito K: Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme. EMBO J. 1992 Jan;11(1):57-62. [Article]
  3. Plunkett G 3rd, Burland V, Daniels DL, Blattner FR: Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes. Nucleic Acids Res. 1993 Jul 25;21(15):3391-8. [Article]
  4. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  5. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  6. Zapun A, Bardwell JC, Creighton TE: The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo. Biochemistry. 1993 May 18;32(19):5083-92. [Article]
  7. Link AJ, Robison K, Church GM: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis. 1997 Aug;18(8):1259-313. [Article]
  8. Wilkins MR, Gasteiger E, Tonella L, Ou K, Tyler M, Sanchez JC, Gooley AA, Walsh BJ, Bairoch A, Appel RD, Williams KL, Hochstrasser DF: Protein identification with N and C-terminal sequence tags in proteome projects. J Mol Biol. 1998 May 8;278(3):599-608. [Article]
  9. Grauschopf U, Winther JR, Korber P, Zander T, Dallinger P, Bardwell JC: Why is DsbA such an oxidizing disulfide catalyst? Cell. 1995 Dec 15;83(6):947-55. [Article]
  10. Akiyama Y, Kamitani S, Kusukawa N, Ito K: In vitro catalysis of oxidative folding of disulfide-bonded proteins by the Escherichia coli dsbA (ppfA) gene product. J Biol Chem. 1992 Nov 5;267(31):22440-5. [Article]
  11. VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
  12. Lippa AM, Goulian M: Perturbation of the oxidizing environment of the periplasm stimulates the PhoQ/PhoP system in Escherichia coli. J Bacteriol. 2012 Mar;194(6):1457-63. doi: 10.1128/JB.06055-11. Epub 2012 Jan 20. [Article]
  13. Martin JL, Bardwell JC, Kuriyan J: Crystal structure of the DsbA protein required for disulphide bond formation in vivo. Nature. 1993 Sep 30;365(6445):464-8. [Article]
  14. Guddat LW, Bardwell JC, Zander T, Martin JL: The uncharged surface features surrounding the active site of Escherichia coli DsbA are conserved and are implicated in peptide binding. Protein Sci. 1997 Jun;6(6):1148-56. [Article]
  15. Guddat LW, Bardwell JC, Glockshuber R, Huber-Wunderlich M, Zander T, Martin JL: Structural analysis of three His32 mutants of DsbA: support for an electrostatic role of His32 in DsbA stability. Protein Sci. 1997 Sep;6(9):1893-900. [Article]
  16. Guddat LW, Bardwell JC, Martin JL: Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization. Structure. 1998 Jun 15;6(6):757-67. [Article]
  17. Schirra HJ, Renner C, Czisch M, Huber-Wunderlich M, Holak TA, Glockshuber R: Structure of reduced DsbA from Escherichia coli in solution. Biochemistry. 1998 May 5;37(18):6263-76. [Article]
  18. Charbonnier JB, Belin P, Moutiez M, Stura EA, Quemeneur E: On the role of the cis-proline residue in the active site of DsbA. Protein Sci. 1999 Jan;8(1):96-105. [Article]
  19. Ondo-Mbele E, Vives C, Kone A, Serre L: Intriguing conformation changes associated with the trans/cis isomerization of a prolyl residue in the active site of the DsbA C33A mutant. J Mol Biol. 2005 Apr 1;347(3):555-63. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB08689Ubiquinone Q1experimentalunknownDetails