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dsbG protein sulfenic acid reductase and chaperone DsbG [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 945224, updated on 4-Apr-2024

Summary

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Gene symbol
dsbG
Gene description
protein sulfenic acid reductase and chaperone DsbG
Primary source
ASAP:ABE-0002084
Locus tag
b0604
See related
ECOCYC:G6333
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
ECK0598; ybdP
Summary
A dsbG defect iscorrected by DsbAB overexpression. [More information is available at EcoGene: EG13535].
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Genomic context

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Sequence:
NC_000913.3 (637827..638573, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene ParB-like nuclease domain-containing protein YbdM Neighboring gene putative PAPS reductase/DUF3440 domain-containing protein YbdN Neighboring gene putative LysR family DNA-binding transcriptional regulator YbdO Neighboring gene alkyl hydroperoxide reductase, AhpC component Neighboring gene alkyl hydroperoxide reductase, AhpF component

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Converting a Sulfenic Acid Reductase into a Disulfide Bond Isomerase. Chatelle C, et al. Antioxid Redox Signal, 2015 Oct 20. PMID 26191605, Free PMC Article
  2. Crystal structures of the DsbG disulfide isomerase reveal an unstable disulfide. Heras B, et al. Proc Natl Acad Sci U S A, 2004 Jun 15. PMID 15184683, Free PMC Article
  3. DsbG, a protein disulfide isomerase with chaperone activity. Shao F, et al. J Biol Chem, 2000 May 5. PMID 10788443
  4. The functional properties of DsbG, a thiol-disulfide oxidoreductase from the periplasm of Escherichia coli. van Straaten M, et al. FEBS Lett, 1998 May 29. PMID 9654144
  5. A new Escherichia coli gene, dsbG, encodes a periplasmic protein involved in disulphide bond formation, required for recycling DsbA/DsbB and DsbC redox proteins. Andersen CL, et al. Mol Microbiol, 1997 Oct. PMID 9383195

See all (34) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. We showed, for the first time, that the periplasmic protein DsbG has chaperone activity in vivo.
    Title: The Chaperone Activities of DsbG and Spy Restore Peptidoglycan Biosynthesis in the elyC Mutant by Preventing Envelope Protein Aggregation.
  2. By borrowing the CGPC active site of Trx-1 in combination with a T200M point mutation, we transformed DsbG into an enzyme highly reactive toward GSNO and YbiS. The pKa of the nucleophilic cysteine, as well as the redox and thermodynamic properties of the engineered DsbG are dramatically changed and become similar to those of Trx-1.
    Title: Sulfur Denitrosylation by an Engineered Trx-like DsbG Enzyme Identifies Nucleophilic Cysteine Hydrogen Bonds as Key Functional Determinant.
  3. Study isolated utilized a screen to isolate mutants of the sulfenic acid reductase (DsbG) that allowed this protein to act as a disulfide bond isomerase.
    Title: Converting a Sulfenic Acid Reductase into a Disulfide Bond Isomerase.
  4. study found that DsbG & DsbC control the global sulfenic acid content of the periplasm & protect single cysteine residues from oxidation; DsbG interacts with the YbiS protein and, along with DsbC, regulates oxidation of its catalytic cysteine residue
    Title: A periplasmic reducing system protects single cysteine residues from oxidation.
  5. N-terminus verified by Edman degradation on mature peptide
    Title: A new Escherichia coli gene, dsbG, encodes a periplasmic protein involved in disulphide bond formation, required for recycling DsbA/DsbB and DsbC redox proteins.
  6. Protein Disulfide-Isomerase
    Title: Laboratory evolution of one disulfide isomerase to resemble another.
Submit: New GeneRIF Correction

Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables protein disulfide isomerase activity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
enables protein homodimerization activity IDA
Inferred from Direct Assay
more info
 PubMed 
Process Evidence Code Pubs
acts_upstream_of_or_within chaperone-mediated protein folding IDA
Inferred from Direct Assay
more info
 PubMed 
Component Evidence Code Pubs
located_in outer membrane-bounded periplasmic space IDA
Inferred from Direct Assay
more info
 PubMed 
located_in periplasmic space IEA
Inferred from Electronic Annotation
more info
  

General protein information

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Preferred Names
protein sulfenic acid reductase and chaperone DsbG
NP_415137.2

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000913.3 Reference assembly

    Range
    637827..638573 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_415137.2 protein sulfenic acid reductase and chaperone DsbG [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_415137.2

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A5B9AA36, A0A8I0CCS5
    Conserved Domains (1) summary
    PRK11657
    Location:16 → 248
    dsbG; disulfide isomerase/thiol-disulfide oxidase; Provisional
Nucleotide Protein
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