U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

Links from GEO Profiles

    • Showing Current items.

    groS cochaperonin GroES [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 948655, updated on 3-Dec-2024

    Summary

    Go to the top of the page Help
    Official Symbol
    groS
    Official Full Name
    cochaperonin GroES
    Primary source
    ECOCYC:EG10600
    Locus tag
    b4142
    See related
    ASAP:ABE-0013566
    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
    ECK4136; groES; mopB
    Summary
    GroS binds and regulates rpoH. [More information is available at EcoGene: EG10600]. The Escherichia coli chaperone protein GroEL (Hsp60) and its regulator GroES are necessary for the proper folding of certain proteins , . [More information is available at EcoCyc: EG10600].
    NEW
    Try the new Gene table
    Try the new Transcript table

    Genomic context

    Go to the top of the page Help
    Sequence:
    NC_000913.3 (4370688..4370981)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene protein FxsA Neighboring gene L-methionine/branched chain amino acid exporter Neighboring gene chaperonin GroEL Neighboring gene DUF4156 domain-containing lipoprotein YjeI

    Genomic regions, transcripts, and products

    Go to the top of the page Help
    Genomic Sequence:
    NC_000913.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

    Go to the top of the pageHelp

    Related articles in PubMed

    1. Folding and assembly pathways of co-chaperonin proteins 10: Origin of bacterial thermostability. Luke K, et al. Arch Biochem Biophys, 2006 Dec 1. PMID 17084377
    2. Structural plasticity and noncovalent substrate binding in the GroEL apical domain. A study using electrospay ionization mass spectrometry and fluorescence binding studies. Ashcroft AE, et al. J Biol Chem, 2002 Sep 6. PMID 12065585
    3. Structural stability and solution structure of chaperonin GroES heptamer studied by synchrotron small-angle X-ray scattering. Higurashi T, et al. J Mol Biol, 2003 Oct 24. PMID 14556748
    4. Unfolding and refolding of Escherichia coli chaperonin GroES is expressed by a three-state model. Higurashi T, et al. J Mol Biol, 1999 Aug 20. PMID 10448048
    5. Amyloid-like fibril formation of co-chaperonin GroES: nucleation and extension prefer different degrees of molecular compactness. Higurashi T, et al. J Mol Biol, 2005 Sep 2. PMID 16054644

    See all (180) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Human embryo models are getting more realistic - raising ethical questions.
      Title: Human embryo models are getting more realistic - raising ethical questions.
    2. While GroEL and GroES increases the folding rate of PepQ by over 15-fold, the slow spontaneous folding of PepQ is not caused by aggregation.
      Title: GroEL actively stimulates folding of the endogenous substrate protein PepQ.
    3. Evidence is provided for an interaction between GroESL and CspC that results in enhanced, temperature-dependent proteolysis of the latter.
      Title: Novel interaction between the major bacterial heat shock chaperone (GroESL) and an RNA chaperone (CspC).
    4. Single-molecule observation of protein folding in symmetric GroEL-(GroES)2 complexes
      Title: Single-molecule observation of protein folding in symmetric GroEL-(GroES)2 complexes.
    5. Studies indicate that the amount of GroEL and GroES in an E. coli cell under normal conditions is sufficient to assist in the folding of no more than 5% of the proteins within the cell.
      Title: What distinguishes GroEL substrates from other Escherichia coli proteins?
    6. substrate folding activity of a single ring GroEL variant is stimulated by modulating the cochaperonin GroES
      Title: Stimulating the substrate folding activity of a single ring GroEL variant by modulating the cochaperonin GroES.
    7. unfolded GroES has covalent structural changes that lead to amyloid fibril formation detected by NMR
      Title: Covalent structural changes in unfolded GroES that lead to amyloid fibril formation detected by NMR: insight into intrinsically disordered proteins.
    8. The association of ATP and GroES to a polypeptide-bound ring of GroEL encapsulates the folding proteins in the central cavity of that ring (cis ring) and allows it to fold in a protected environment where the risk of aggregation is reduced.
      Title: Characterisation of a GroEL single-ring mutant that supports growth of Escherichia coli and has GroES-dependent ATPase activity.
    9. Data show that structure-forming characteristics of GroES appear to be conserved through the backbone reversal process, although the differential conformational behavior upon heating also indicates differences.
      Title: Folding behavior of a backbone-reversed protein: reversible polyproline type II to beta-sheet thermal transitions in retro-GroES multimers with GroES-like features.
    10. there is an an intermediate GroEL/substrate/GroES complex in which the substrate and GroES bind to GroEL by sharing seven common binding sites
      Title: Determination of the number of active GroES subunits in the fused heptamer GroES required for interactions with GroEL.
    Submit: New GeneRIF Correction See all GeneRIFs (19)

    Interactions

    Go to the top of the page Help
    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

    Go to the top of the page Help

    Homology

    General protein information

    Go to the top of the page Help
    Preferred Names
    cochaperonin GroES
    NP_418566.1

    NCBI Reference Sequences (RefSeq)

    Go to the top of the page Help

    NEW Try the new Transcript table

    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
      4370688..4370981
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_418566.1 cochaperonin GroES [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_418566.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A377E3U5
      Conserved Domains (1) summary
      PRK00364
      Location:1 → 96
      groES; co-chaperonin GroES; Reviewed
    Nucleotide Protein
    Heading Accession and Version

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.