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Escherichia coli K-12 substr. MG1655 Enzyme: DsbGreduced

Gene: dsbG Accession Numbers: G6333 (EcoCyc), b0604, ECK0598

Synonyms: ybdP

Regulation Summary Diagram: ?

Regulation summary diagram for dsbG

Subunit composition of DsbGreduced = [DsbG]2
         DsbGreduced = DsbG

Alternative forms of DsbGreduced: DsbGoxidized

Proteins containing single cysteine residues are vulnerable to oxidation to sulfenic acids. The E. coli DsbG protein forms part of a reducing system that controls the level of cysteine sulfenylation in the periplasm. Protein sulfenic acids accumulate in the periplasm of dsbG and dsbC null strains [Depuydt et al., 2009]. The periplasmic transpeptidases YbiS, ErfK and YahG are substrates of DsbG [Depuydt et al., 2009]. DsbG also acts as a disulfide isomerase which has narrower substrate specificity than the isomerase encoded by the dsbC gene [Bessette99]. The periplasmic isomerase is found exclusively in the reduced state in wild type cells despite the oxidizing conditions in the periplasm. The reduced state is maintained by the action of DsbD [Stewart99].

The protein also functions as a molecular chaperone, suppressing the aggregation of citrate synthase and luciferase [Shao00].

Citations: [vanStraaten98, Andersen97, Fabianek00]

Locations: periplasmic space

Map Position: [637,050 <- 637,796] (13.73 centisomes, 49°)
Length: 747 bp / 248 aa

Molecular Weight of Polypeptide: 27.495 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0002084 , DIP:DIP-9478N , EchoBASE:EB3306 , EcoGene:EG13535 , EcoliWiki:b0604 , IAF1260:2703937 , Mint:MINT-1232069 , ModBase:P77202 , OU-Microarray:b0604 , PortEco:dsbG , PR:PRO_000022484 , Pride:P77202 , Protein Model Portal:P77202 , RegulonDB:G6333 , SMR:P77202 , String:511145.b0604 , UniProt:P77202

Relationship Links: InterPro:IN-FAMILY:IPR012336 , InterPro:IN-FAMILY:IPR018950 , PDB:Structure:1V57 , PDB:Structure:1V58 , PDB:Structure:2H0G , PDB:Structure:2H0H , PDB:Structure:2H0I , PDB:Structure:2IY2 , Pfam:IN-FAMILY:PF13098 , Prosite:IN-FAMILY:PS00194

In Paralogous Gene Group: 164 (2 members)

In Reactions of unknown directionality:

Not in pathways:
DsbGoxidized[periplasmic space] + DsbDreduced[periplasmic space] = DsbGreduced[periplasmic space] + DsbDoxidized[periplasmic space]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Genetic Regulation Schematic: ?

Genetic regulation schematic for dsbG

GO Terms:

Biological Process: GO:0006457 - protein folding Inferred from experiment [Andersen97]
GO:0055114 - oxidation-reduction process Inferred from experiment [Depuydt et al., 2009]
Molecular Function: GO:0003756 - protein disulfide isomerase activity Inferred from experiment [Bessette99, Andersen97]
GO:0015035 - protein disulfide oxidoreductase activity Inferred from experiment [Depuydt et al., 2009]
Cellular Component: GO:0030288 - outer membrane-bounded periplasmic space Inferred by computational analysis [DiazMejia09]
GO:0042597 - periplasmic space Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]

MultiFun Terms: information transfer protein related chaperoning, repair (refolding)

Essentiality data for dsbG knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Last-Curated ? 19-Jan-2010 by Mackie A , Macquarie University

Enzymatic reaction of: periplasmic protein disulfide isomerase (DsbGreduced)

Synonyms: thiol:disulfide interchange protein DsbG

EC Number:

a protein with incorrect disulfide bonds <=> a protein with correct disulfide bonds

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

This reaction is reversible.

Enzymatic reaction of: protein disulfide oxidoreductase (DsbGreduced)

a protein with reduced sulfide groups <=> a protein with oxidized disulfide bonds

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

This reaction is reversible.

Sequence Features

Protein sequence of DsbGreduced with features indicated

Feature Class Location Citations Comment
Signal-Sequence 1 -> 17
[vanStraaten98, UniProt11]
Chain 18 -> 248
UniProt: Thiol:disulfide interchange protein dsbG;
Mutagenesis-Variant 126
[Shao00, UniProt11]
[Shao00, UniProt11]
C → A: Complete loss of redox activity.
C → S: No loss of chaperone activity; when associated with S-129.
Disulfide-Bond-Site 126, 129
[Heras04, UniProt11]
UniProt: Redox-active.
Mutagenesis-Variant 129
[Depuydt et al., 2009, Shao00, UniProt11]
[Depuydt et al., 2009, Shao00, UniProt11]
C → S: No loss of chaperone activity; when associated with S-126.
C → A: Partial loss of redox activity. Traps the protein in complex with ErfK, YbiS and YnhG.

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Units:

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram


Peter D. Karp on Wed Jan 18, 2006:
Gene right-end position adjusted based on analysis performed in the 2005 E. coli annotation update [Riley06 ].
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


Andersen97: Andersen CL, 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 1997;26(1);121-32. PMID: 9383195

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Bessette99: Bessette PH, Cotto JJ, Gilbert HF, Georgiou G (1999). "In vivo and in vitro function of the Escherichia coli periplasmic cysteine oxidoreductase DsbG." J Biol Chem 1999;274(12);7784-92. PMID: 10075670

Depuydt et al., 2009: Depuydt M, Leonard SE, Vertommen D, Denoncin K, Morsomme P, Wahni K, Messens J, Carroll KS, Collet JF (2009). "A periplasmic reducing system protects single cysteine residues from oxidation." Science 326(5956);1109-11. PMID: 19965429

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Fabianek00: Fabianek RA, Hennecke H, Thony-Meyer L (2000). "Periplasmic protein thiol:disulfide oxidoreductases of Escherichia coli." FEMS Microbiol Rev 2000;24(3);303-16. PMID: 10841975

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

Heras04: Heras B, Edeling MA, Schirra HJ, Raina S, Martin JL (2004). "Crystal structures of the DsbG disulfide isomerase reveal an unstable disulfide." Proc Natl Acad Sci U S A 101(24);8876-81. PMID: 15184683

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Riley06: Riley M, Abe T, Arnaud MB, Berlyn MK, Blattner FR, Chaudhuri RR, Glasner JD, Horiuchi T, Keseler IM, Kosuge T, Mori H, Perna NT, Plunkett G, Rudd KE, Serres MH, Thomas GH, Thomson NR, Wishart D, Wanner BL (2006). "Escherichia coli K-12: a cooperatively developed annotation snapshot--2005." Nucleic Acids Res 34(1);1-9. PMID: 16397293

Shao00: Shao F, Bader MW, Jakob U, Bardwell JC (2000). "DsbG, a protein disulfide isomerase with chaperone activity." J Biol Chem 2000;275(18);13349-52. PMID: 10788443

Stewart99: Stewart EJ, Katzen F, Beckwith J (1999). "Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli." EMBO J 18(21);5963-71. PMID: 10545108

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

vanStraaten98: van Straaten M, Missiakas D, Raina S, Darby NJ (1998). "The functional properties of DsbG, a thiol-disulfide oxidoreductase from the periplasm of Escherichia coli." FEBS Lett 1998;428(3);255-8. PMID: 9654144

Other References Related to Gene Regulation

Storz90: Storz G, Tartaglia LA, Ames BN (1990). "Transcriptional regulator of oxidative stress-inducible genes: direct activation by oxidation." Science 1990;248(4952);189-94. PMID: 2183352

Tartaglia89: Tartaglia LA, Storz G, Ames BN (1989). "Identification and molecular analysis of oxyR-regulated promoters important for the bacterial adaptation to oxidative stress." J Mol Biol 1989;210(4);709-19. PMID: 2693740

Tartaglia92: Tartaglia LA, Gimeno CJ, Storz G, Ames BN (1992). "Multidegenerate DNA recognition by the OxyR transcriptional regulator." J Biol Chem 267(3);2038-45. PMID: 1730735

Toledano94: Toledano MB, Kullik I, Trinh F, Baird PT, Schneider TD, Storz G (1994). "Redox-dependent shift of OxyR-DNA contacts along an extended DNA-binding site: a mechanism for differential promoter selection." Cell 78(5);897-909. PMID: 8087856

Zheng01b: Zheng M, Wang X, Doan B, Lewis KA, Schneider TD, Storz G (2001). "Computation-directed identification of OxyR DNA binding sites in Escherichia coli." J Bacteriol 183(15);4571-9. PMID: 11443092

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 19.0 on Fri Aug 28, 2015, biocyc12.