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    cnoX chaperedoxin [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 947119, updated on 17-Dec-2024

    Summary

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    Official Symbol
    cnoX
    Official Full Name
    chaperedoxin
    Primary source
    ECOCYC:G6268
    Locus tag
    b0492
    See related
    ASAP:ABE-0001707
    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
    ECK0486; ybbN
    Summary
    The function of YbbN as both an thiol-disulfide oxidoreductase and as a chaperone is controversial (Vlamis-Gardikas, 2008): [More information is available at EcoGene: EG13261]. YbbN is a thioredoxin-like protein with chaperone and protein oxidoreductase activity. [More information is available at EcoCyc: G6268].
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    Genomic context

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    Sequence:
    NC_000913.3 (517425..518279, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene NfeD-like family protein YbbJ Neighboring gene PHB domain-containing protein QmcA Neighboring gene putative iron ABC exporter ATP-binding subunit FetA Neighboring gene putative iron ABC exporter membrane subunit FetB Neighboring gene NADP(+)-dependent aldehyde reductase YbbO Neighboring gene multifunctional acyl-CoA thioesterase I and protease I and lysophospholipase L1 Neighboring gene putative ABC transporter ATP-binding protein YbbA Neighboring gene putative ABC transporter membrane subunit YbbP

    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. DNA replication defects in a mutant deficient in the thioredoxin homolog YbbN. Le HT, et al. Biochem Biophys Res Commun, 2011 Feb 4. PMID 21195694
    2. The multiple functions of the thiol-based electron flow pathways of Escherichia coli: Eternal concepts revisited. Vlamis-Gardikas A. Biochim Biophys Acta, 2008 Nov. PMID 18423382
    3. The origami of thioredoxin-like folds. Pan JL, et al. Protein Sci, 2006 Oct. PMID 17008712, Free PMC Article
    4. CnoX Is a Chaperedoxin: A Holdase that Protects Its Substrates from Irreversible Oxidation. Goemans CV, et al. Mol Cell, 2018 May 17. PMID 29754824
    5. The thioredoxin homolog YbbN functions as a chaperone rather than as an oxidoreductase. Kthiri F, et al. Biochem Biophys Res Commun, 2008 Oct 3. PMID 18657513

    See all (17) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. These results suggest that the DNA replication and cell division defects of the ybbN mutant might best be explained by chaperone functions of YbbN in the biogenesis of DNA polymerase 3 holoenzyme.
      Title: DNA replication defects in a mutant deficient in the thioredoxin homolog YbbN.
    2. The chaperone properties of YbbN are more important in vivo than its redox properties.
      Title: The thioredoxin homolog YbbN functions as a chaperone rather than as an oxidoreductase.
    3. YbbN catalyzes the oxidation of reduced RNase and the isomerization of scrambled RNase. YbbN also possesses chaperone properties.
      Title: The Escherichia coli thioredoxin homolog YbbN/Trxsc is a chaperone and a weak protein oxidoreductase.
    Submit: New GeneRIF Correction

    General gene information

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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables unfolded protein binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in cell redox homeostasis IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within cellular response to oxidative stress IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    acts_upstream_of_or_within chaperone-mediated protein folding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    acts_upstream_of_or_within maintenance of unfolded protein IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    acts_upstream_of_or_within protein refolding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in response to stress IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    chaperedoxin

    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
      517425..518279 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_415025.4 chaperedoxin [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_415025.4

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0AAN3IKI2
      Conserved Domains (2) summary
      COG3118
      Location:1 → 284
      YbbN; Negative regulator of GroEL, contains thioredoxin-like and TPR-like domains [Posttranslational modification, protein turnover, chaperones]
      sd00008
      Location:114 → 143
      TPR_YbbN; TPR repeat [structural motif]
    Nucleotide Protein
    Heading Accession and Version

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