Identification
Name:Thiol:disulfide interchange protein dsbA
Synonyms:Not Available
Gene Name:dsbA
Enzyme Class:Not Available
Biological Properties
General Function:Involved in 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. It is required for pilus biogenesis
Cellular Location:Periplasm
SMPDB Pathways:Not Available
KEGG Pathways:
  • Cationic antimicrobial peptide (CAMP) resistance eco01503
Complex Reactions:
Thumb+periplasmic protein disulfide isomerase I (reduced)Thumb+periplasmic protein disulfide isomerase I (oxidized)
Ubiquinone-8 + periplasmic protein disulfide isomerase I (reduced) → Ubiquinol-8 + periplasmic protein disulfide isomerase I (oxidized)
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Menaquinone 8+periplasmic protein disulfide isomerase I (reduced)Thumb+periplasmic protein disulfide isomerase I (oxidized)
Menaquinone 8 + periplasmic protein disulfide isomerase I (reduced) → Menaquinol 8 + periplasmic protein disulfide isomerase I (oxidized)
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Metabolites:
ECMDB IDNameView
ECMDB21245Menaquinol 8MetaboCard
ECMDB01060Ubiquinol-8MetaboCard
ECMDB21296Ubiquinone-8MetaboCard
GO Classification:
Component
cell part
outer membrane-bounded periplasmic space
periplasmic space
Function
catalytic activity
disulfide oxidoreductase activity
oxidoreductase activity
oxidoreductase activity, acting on a sulfur group of donors
protein disulfide oxidoreductase activity
Process
cell redox homeostasis
cellular homeostasis
cellular process
Gene Properties
Blattner:b3860
Gene OrientationClockwise
Centisome Percentage:87.11
Left Sequence End4041441
Right Sequence End4042067
Gene Sequence:
>627 bp
ATGACATACGATAGTGAATTCGGATCACATGTATCCCTATATCGGGATAGAATCAAACAG
GTTATTGATGACTCCCTAAACGAACATCTTAACTCAATGATTCTACGTGTTGATCTGCAT
GACCCAATTGATACAGAAAATATGGATAACCCATTCTTTCAACCCAGGGTTGACTCTGGT
GCTATATCTCGCTTTACCAGTGCGTTAAAAGCAAAGCTTAAACATGATAAGCATATTAAA
ACTCAACGGAAAGACTGGCCTGATAGTCGACATTCCACTTTACGTTACGCATGGGTCAGA
GAATATACCAAAAATAGAAAGCGGCATTACCATTTGATACTGTGTTTCAATCAGGATGCT
TATTATCATTTAGGTGATTACGACTTAAACCGTAACACGTTACGTACAATGATAACGACA
GCTTGGTACAGTGCACTTGGCATCCCTATAGATAGCTCGGGGAAGTTAGTTAATTACCCG
CCAAATGGCAAATACCTTCTCAATCGTAAAAGGGACAACTTTGAGCAGACTTATAGCGAT
TTGATGAATAGGGTGGATTACATGACCAAAGTAAGGACTAAAATAGTCGGTGACGGAGAC
CGTAATTTCGGCTGCAGTCGCGGGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:208
Protein Molecular Weight:23104
Protein Theoretical pI:6
PDB File:1A2J
Signaling Regions:
  • 1-19
Transmembrane Regions:
  • None
Protein Sequence:
>Thiol:disulfide interchange protein dsbA
MKKIWLALAGLVLAFSASAAQYEDGKQYTTLEKPVAGAPQVLEFFSFFCPHCYQFEEVLH
ISDNVKKKLPEGVKMTKYHVNFMGGDLGKDLTQAWAVAMALGVEDKVTVPLFEGVQKTQT
IRSASDIRDVFINAGIKGEEYDAAWNSFVVKSLVAQQEKAAADVQLRGVPAMFVNGKYQL
NPQGMDTSNMDVFVQQYADTVKYLSEKK
References
External Links:
ResourceLink
Uniprot ID:P0AEG4
Uniprot Name:DSBA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85675489
PDB ID:1A2J
Ecogene ID:EG11297
Ecocyc:EG11297
ColiBase:b3860
Kegg Gene:b3860
EchoBASE ID:EB1274
CCDB:DSBA_ECOLI
BacMap:16131701
General Reference:
  • Akiyama, Y., Kamitani, S., Kusukawa, N., Ito, K. (1992). "In vitro catalysis of oxidative folding of disulfide-bonded proteins by the Escherichia coli dsbA (ppfA) gene product." J Biol Chem 267:22440-22445. Pubmed: 1429594
  • Bardwell, J. C., McGovern, K., Beckwith, J. (1991). "Identification of a protein required for disulfide bond formation in vivo." Cell 67:581-589. Pubmed: 1934062
  • Blattner, F. R., Plunkett, G. 3rd, 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. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Charbonnier, J. B., Belin, P., Moutiez, M., Stura, E. A., Quemeneur, E. (1999). "On the role of the cis-proline residue in the active site of DsbA." Protein Sci 8:96-105. Pubmed: 10210188
  • Grauschopf, U., Winther, J. R., Korber, P., Zander, T., Dallinger, P., Bardwell, J. C. (1995). "Why is DsbA such an oxidizing disulfide catalyst?" Cell 83:947-955. Pubmed: 8521518
  • Guddat, L. W., Bardwell, J. C., Glockshuber, R., Huber-Wunderlich, M., Zander, T., Martin, J. L. (1997). "Structural analysis of three His32 mutants of DsbA: support for an electrostatic role of His32 in DsbA stability." Protein Sci 6:1893-1900. Pubmed: 9300489
  • Guddat, L. W., Bardwell, J. C., Martin, J. L. (1998). "Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization." Structure 6:757-767. Pubmed: 9655827
  • Guddat, L. W., Bardwell, J. C., Zander, T., Martin, J. L. (1997). "The uncharged surface features surrounding the active site of Escherichia coli DsbA are conserved and are implicated in peptide binding." Protein Sci 6:1148-1156. Pubmed: 9194175
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Kamitani, S., Akiyama, Y., Ito, K. (1992). "Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme." EMBO J 11:57-62. Pubmed: 1740115
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
  • Martin, J. L., Bardwell, J. C., Kuriyan, J. (1993). "Crystal structure of the DsbA protein required for disulphide bond formation in vivo." Nature 365:464-468. Pubmed: 8413591
  • Ondo-Mbele, E., Vives, C., Kone, A., Serre, L. (2005). "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 347:555-563. Pubmed: 15755450
  • Plunkett, G. 3rd, Burland, V., Daniels, D. L., Blattner, F. R. (1993). "Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes." Nucleic Acids Res 21:3391-3398. Pubmed: 8346018
  • Schirra, H. J., Renner, C., Czisch, M., Huber-Wunderlich, M., Holak, T. A., Glockshuber, R. (1998). "Structure of reduced DsbA from Escherichia coli in solution." Biochemistry 37:6263-6276. Pubmed: 9572841
  • 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. (1998). "Protein identification with N and C-terminal sequence tags in proteome projects." J Mol Biol 278:599-608. Pubmed: 9600841
  • Zapun, A., Bardwell, J. C., Creighton, T. E. (1993). "The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo." Biochemistry 32:5083-5092. Pubmed: 8494885