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    dsbC protein disulfide isomerase DsbC [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 947363, updated on 3-Dec-2024

    Summary

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    Official Symbol
    dsbC
    Official Full Name
    protein disulfide isomerase DsbC
    Primary source
    ECOCYC:EG11070
    Locus tag
    b2893
    See related
    ASAP:ABE-0009494
    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
    ECK2888; xprA
    Summary
    DsbC rearranges incorrect disulfide bonds during oxidative protein folding. [More information is available at EcoGene: EG11070].
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    Genomic context

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    Sequence:
    NC_000913.3 (3038112..3038822, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene peptide chain release factor RF2 Neighboring gene ssDNA-specific exonuclease RecJ Neighboring gene site-specific recombinase Neighboring gene flavodoxin 2

    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. The multidrug resistance IncA/C transferable plasmid encodes a novel domain-swapped dimeric protein-disulfide isomerase. Premkumar L, et al. J Biol Chem, 2014 Jan 31. PMID 24311786, Free PMC Article
    2. Effects of mutations in genes for proteins involved in disulphide bond formation in the periplasm on the activities of anaerobically induced electron transfer chains in Escherichia coli K12. Metheringham R, et al. Mol Gen Genet, 1996 Nov 27. PMID 9003292
    3. Overexpression of protein disulfide isomerase DsbC stabilizes multiple-disulfide-bonded recombinant protein produced and transported to the periplasm in Escherichia coli. Kurokawa Y, et al. Appl Environ Microbiol, 2000 Sep. PMID 10966415, Free PMC Article
    4. Folding of Escherichia coli DsbC: characterization of a monomeric folding intermediate. Ke H, et al. Biochemistry, 2006 Dec 19. PMID 17154548
    5. Effect of oxidized and reduced forms of Escherichia coli DsbC on protein refolding. Kohda J, et al. J Biosci Bioeng, 2002. PMID 16233282

    See all (89) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Data indicate that protein disulfide-isomerases DsbC is involved in the protection of single cysteine residues against oxidative stress.
      Title: A new role for Escherichia coli DsbC protein in protection against oxidative stress.
    2. Our data reveal that the conserved plasmid-encoded DsbP protein is a bona fide disulfide isomerase and suggest that a dedicated oxidative folding enzyme is important for conjugative plasmid transfer.
      Title: The multidrug resistance IncA/C transferable plasmid encodes a novel domain-swapped dimeric protein-disulfide isomerase.
    3. DsbC either prevents the formation of these mixed disulphides or resolves these adducts subsequently. In the process, DsbC itself gets oxidized and proceeds to catalyse disulphide bond formation.
      Title: Overexpression of the rhodanese PspE, a single cysteine-containing protein, restores disulphide bond formation to an Escherichia coli strain lacking DsbA.
    4. Crystal structure of the outer membrane protein RcsF, a new substrate for the periplasmic protein-disulfide isomerase DsbC
      Title: Crystal structure of the outer membrane protein RcsF, a new substrate for the periplasmic protein-disulfide isomerase DsbC.
    5. Data found that the periplasmic disulfide isomerase DsbC cooperates with SurA and the thiol oxidase DsbA in the folding of the essential beta-barrel protein LptD.
      Title: The protein-disulfide isomerase DsbC cooperates with SurA and DsbA in the assembly of the essential β-barrel protein LptD.
    6. The thermal stability of DsbC has been studied by using temperature-dependent Fourier transformation infrared and time-resolved infrared spectroscopy coupled with temperature-jump initiation
      Title: Thermal-induced dissociation and unfolding of homodimeric DsbC revealed by temperature-jump time-resolved infrared spectra.
    7. 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.
    8. The data indicate that DsbC can assist DsbA in a DsbD-independent manner to oxidatively fold envelope proteins.
      Title: The disulphide isomerase DsbC cooperates with the oxidase DsbA in a DsbD-independent manner.
    9. N-terminus verified by Edman degradation on mature peptide
      Title: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.
    10. x-ray crystallographic structure of reduced disulfide-bond isomerase DsbC
      Title: Structure of the reduced disulfide-bond isomerase DsbC from Escherichia coli.
    Submit: New GeneRIF Correction See all GeneRIFs (13)

    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 disulfide oxidoreductase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein disulfide isomerase activity IDA
    Inferred from Direct Assay
    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 
    enables protein-disulfide reductase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Process Evidence Code Pubs
    acts_upstream_of_or_within chaperone-mediated protein folding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    acts_upstream_of_or_within response to copper ion IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in outer membrane-bounded periplasmic space IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in outer membrane-bounded periplasmic space NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    located_in 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 disulfide isomerase DsbC
    NP_417369.1

    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
      3038112..3038822 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_417369.1 protein disulfide isomerase DsbC [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_417369.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A8S7ED91
      Conserved Domains (1) summary
      PRK10877
      Location:1 → 231
      PRK10877; protein disulfide isomerase II DsbC; Provisional
    Nucleotide Protein
    Heading Accession and Version

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