Thiol:disulfide interchange protein DsbG (P77202)

Identification
Name:Thiol:disulfide interchange protein DsbG
Synonyms:Not Available
Gene Name:dsbG
Enzyme Class:Not Available
Biological Properties
General Function:Posttranslational modification, protein turnover, chaperones
Specific Function:Involved in disulfide bond formation. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins such as ErfK, YbiS and YnhG. Probably also functions as a disulfide isomerase with a narrower substrate specificity than DsbC. DsbG is maintained in a reduced state by DsbD. Displays chaperone activity in both redox states in vitro
Cellular Location:Periplasm
SMPDB Pathways:Not Available
KEGG Pathways:Not Available
Complex Reactions:
1.0fused thiol:disulfide interchange protein (reduced)+1.0periplasmic disulfide isomerase/thiol-disulphide oxidase (oxidized) → 1.0fused thiol:disulfide interchange protein (oxidized)+1.0periplasmic disulfide isomerase/thiol-disulphide oxidase (reduced)
1.0fused thiol:disulfide interchange protein (reduced) + 1.0periplasmic disulfide isomerase/thiol-disulphide oxidase (oxidized) → 1.0fused thiol:disulfide interchange protein (oxidized) + 1.0periplasmic disulfide isomerase/thiol-disulphide oxidase (reduced)
ReactionCard
1.0periplasmic disulfide isomerase/thiol-disulphide oxidase (oxidized)+2.0Thumb → 1.0periplasmic disulfide isomerase/thiol-disulphide oxidase (reduced)+1.0Thumb
1.0periplasmic disulfide isomerase/thiol-disulphide oxidase (oxidized) + 2.0Glutathione → 1.0periplasmic disulfide isomerase/thiol-disulphide oxidase (reduced) + 1.0Glutathione disulfide
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00125GlutathioneMetaboCard
ECMDB21221Glutathione disulfideMetaboCard
GO Classification:Not Available
Gene Properties
Blattner:b0604
Gene OrientationCounterclockwise
Centisome Percentage:13.73
Left Sequence End637050
Right Sequence End637796
Gene Sequence:
>747 bp
ATGTTAAAAAAGATACTTTTACTGGCTCTGCTTCCTGCAATCGCCTTCGCAGAGGAACTT
CCTGCTCCAGTAAAAGCGATTGAAAAACAGGGCATTACAATCATCAAAACATTCGATGCC
CCCGGAGGAATGAAAGGTTATCTCGGAAAGTATCAGGATATGGGCGTCACCATCTACCTG
ACTCCAGATGGTAAGCACGCTATCTCTGGTTACATGTACAACGAGAAAGGTGAAAACCTG
AGTAACACACTTATCGAAAAAGAAATTTACGCACCAGCCGGACGCGAAATGTGGCAACGG
ATGGAACAATCCCACTGGCTCCTCGACGGTAAAAAAGATGCGCCGGTCATTGTCTACGTC
TTCGCCGATCCGTTCTGCCCATATTGTAAACAGTTCTGGCAGCAGGCGCGCCCGTGGGTA
GATTCTGGCAAAGTGCAATTAAGAACATTGTTGGTTGGGGTTATCAAGCCAGAAAGCCCG
GCGACAGCAGCGGCAATTCTTGCCTCCAAAGATCCCGCAAAAACCTGGCAACAATATGAA
GCCTCTGGTGGCAAGCTTAAGCTAAACGTGCCTGCAAACGTAAGTACAGAGCAAATGAAA
GTGTTAAGTGACAATGAGAAACTGATGGACGATCTGGGGGCAAATGTCACGCCGGCTATC
TATTACATGAGTAAGGAAAATACGCTACAACAGGCCGTGGGGTTGCCCGATCAGAAAACG
CTTAATATCATTATGGGGAATAAATAA
Protein Properties
Pfam Domain Function:Not Available
Protein Residues:248
Protein Molecular Weight:27495
Protein Theoretical pI:9
PDB File:1V58
Signaling Regions:
  • 1-17
Transmembrane Regions:
  • None
Protein Sequence:
>Thiol:disulfide interchange protein DsbG
MLKKILLLALLPAIAFAEELPAPVKAIEKQGITIIKTFDAPGGMKGYLGKYQDMGVTIYL
TPDGKHAISGYMYNEKGENLSNTLIEKEIYAPAGREMWQRMEQSHWLLDGKKDAPVIVYV
FADPFCPYCKQFWQQARPWVDSGKVQLRTLLVGVIKPESPATAAAILASKDPAKTWQQYE
ASGGKLKLNVPANVSTEQMKVLSDNEKLMDDLGANVTPAIYYMSKENTLQQAVGLPDQKT
LNIIMGNK
References
External Links:
ResourceLink
Uniprot ID:P77202
Uniprot Name:DSBG_ECOLI
GenBank Gene ID:AF000956
Genebank Protein ID:2078304
PDB ID:1V58
Ecogene ID:EG13535
Ecocyc:EG13535
ColiBase:b0604
Kegg Gene:b0604
EchoBASE ID:EB3306
CCDB:DSBG_ECOLI
BacMap:90111151
General Reference:
  • Andersen, C. L., Matthey-Dupraz, A., Missiakas, D., Raina, S. (1997). "A new Escherichia coli gene, dsbG, encodes a periplasmic protein involved in disulphide bond formation, required for recycling DsbA/DsbB and DsbC redox proteins." Mol Microbiol 26:121-132. Pubmed: 9383195
  • Bessette, P. H., Cotto, J. J., Gilbert, H. F., Georgiou, G. (1999). "In vivo and in vitro function of the Escherichia coli periplasmic cysteine oxidoreductase DsbG." J Biol Chem 274:7784-7792. Pubmed: 10075670
  • 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
  • Depuydt, M., Leonard, S. E., Vertommen, D., Denoncin, K., Morsomme, P., Wahni, K., Messens, J., Carroll, K. S., Collet, J. F. (2009). "A periplasmic reducing system protects single cysteine residues from oxidation." Science 326:1109-1111. Pubmed: 19965429
  • 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
  • Heras, B., Edeling, M. A., Schirra, H. J., Raina, S., Martin, J. L. (2004). "Crystal structures of the DsbG disulfide isomerase reveal an unstable disulfide." Proc Natl Acad Sci U S A 101:8876-8881. Pubmed: 15184683
  • Oshima, T., Aiba, H., Baba, T., Fujita, K., Hayashi, K., Honjo, A., Ikemoto, K., Inada, T., Itoh, T., Kajihara, M., Kanai, K., Kashimoto, K., Kimura, S., Kitagawa, M., Makino, K., Masuda, S., Miki, T., Mizobuchi, K., Mori, H., Motomura, K., Nakamura, Y., Nashimoto, H., Nishio, Y., Saito, N., Horiuchi, T., et, a. l. .. (1996). "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." DNA Res 3:137-155. Pubmed: 8905232
  • Shao, F., Bader, M. W., Jakob, U., Bardwell, J. C. (2000). "DsbG, a protein disulfide isomerase with chaperone activity." J Biol Chem 275:13349-13352. Pubmed: 10788443
  • van Straaten, M., Missiakas, D., Raina, S., Darby, N. J. (1998). "The functional properties of DsbG, a thiol-disulfide oxidoreductase from the periplasm of Escherichia coli." FEBS Lett 428:255-258. Pubmed: 9654144
  • Yeh, S. M., Koon, N., Squire, C., Metcalf, P. (2007). "Structures of the dimerization domains of the Escherichia coli disulfide-bond isomerase enzymes DsbC and DsbG." Acta Crystallogr D Biol Crystallogr 63:465-471. Pubmed: 17372350