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

    Gene ID: 945224, updated on 3-Dec-2024

    Summary

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    Official Symbol
    dsbG
    Official Full Name
    protein sulfenic acid reductase and chaperone DsbG
    Primary source
    ECOCYC:G6333
    Locus tag
    b0604
    See related
    ASAP:ABE-0002084
    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. DsbG, a protein disulfide isomerase with chaperone activity. Shao F, et al. J Biol Chem, 2000 May 5. PMID 10788443
    2. 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
    3. 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
    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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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables protein disulfide isomerase activity EXP
    Inferred from Experiment
    more info
    		 PubMed 
    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
      A0A8I0CCS5
      Conserved Domains (1) summary
      PRK11657
      Location:16 → 248
      dsbG; disulfide isomerase/thiol-disulfide oxidase; Provisional
    Nucleotide Protein
    Heading Accession and Version

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