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groL chaperonin GroEL [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 948665, updated on 3-Dec-2024
Official Symbol
groL
Official Full Name
chaperonin GroEL
Primary source
ECOCYC:EG10599
Locus tag
b4143
See related
ASAP:ABE-0013568
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
ECK4137; groEL; mopA
Summary
groL is an essential gene. [More information is available at EcoGene: EG10599]. 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: EG10599].
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Sequence:
NC_000913.3 (4371025..4372671)

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

Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Purification, crystallization and structure determination of native GroEL from Escherichia coli lacking bound potassium ions. Kiser PD, et al. Acta Crystallogr Sect F Struct Biol Cryst Commun, 2007 Jun 1. PMID 17554162, Free PMC Article
  2. Denaturation and reassembly of chaperonin GroEL studied by solution X-ray scattering. Arai M, et al. Protein Sci, 2003 Apr. PMID 12649424, Free PMC Article
  3. Annealing function of GroEL: structural and bioinformatic analysis. Stan G, et al. Biophys Chem, 2003. PMID 12646383
  4. Fast-scanning atomic force microscopy reveals the ATP/ADP-dependent conformational changes of GroEL. Yokokawa M, et al. EMBO J, 2006 Oct 4. PMID 16977315, Free PMC Article
  5. Global aggregation of newly translated proteins in an Escherichia coli strain deficient of the chaperonin GroEL. Chapman E, et al. Proc Natl Acad Sci U S A, 2006 Oct 24. PMID 17043235, Free PMC Article

See all (245) 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. In vitro Evolution of Uracil Glycosylase Towards DnaKJ and GroEL Binding Evolves Different Misfolded States.
    Title: In vitro Evolution of Uracil Glycosylase Towards DnaKJ and GroEL Binding Evolves Different Misfolded States.
  3. The Functional Differences between the GroEL Chaperonin of Escherichia coli and the HtpB Chaperonin of Legionella pneumophila Can Be Mapped to Specific Amino Acid Residues.
    Title: The Functional Differences between the GroEL Chaperonin of Escherichia coli and the HtpB Chaperonin of Legionella pneumophila Can Be Mapped to Specific Amino Acid Residues.
  4. 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.
  5. study confirmed the altered GroEL dependence of green fluorescent protein variants with in vitro folding assays; mutations at positions predicted to be highly frustrated were found to correlate with decreased GroEL dependence; conversely, mutations at positions with low frustration were found to correlate with increased GroEL dependence
    Title: Local energetic frustration affects the dependence of green fluorescent protein folding on the chaperonin GroEL.
  6. Data suggest that neither DnaK nor GroEL singly can modulate sigma32 stability in vivo; there is ordered network between them, where GroEL acts upstream of DnaK.
    Title: GroEL to DnaK chaperone network behind the stability modulation of σ(32) at physiological temperature in Escherichia coli.
  7. In the case of GroEL, individualisation of monomers thus leads to individualisation of homomultimeric protein complexes, effectively providing the prerequisites for evolving an orthogonal intracellular GroEL folding machine.
    Title: Towards functional orthogonalisation of protein complexes: individualisation of GroEL monomers leads to distinct quasihomogeneous single rings.
  8. 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).
  9. Investigated the role of the surface-associated GroEL in the binding of E. coli to macrophages. Results showed that GroEL on E. coli was recognized by LOX-1 on macrophages, leading to the phagocytosis of pathogen by macrophages.
    Title: Surface-associated GroEL facilitates the adhesion of Escherichia coli to macrophages through lectin-like oxidized low-density lipoprotein receptor-1.
  10. Nuclear magnetic resonance (NMR) observation of the uniformly (2) H,(15) N-labeled stringent 33-kDa substrate protein rhodanese in a productive complex with the uniformly (14) N-labeled 400 kDa single-ring version of the E. coli chaperonin GroEL, SR1.
    Title: Nuclear magnetic resonance spectroscopy with the stringent substrate rhodanese bound to the single-ring variant SR1 of the E. coli chaperonin GroEL.
Submit: New GeneRIF Correction See all GeneRIFs (38)
Products Interactant Other Gene Complex Source Pubs Description

Homology

Preferred Names
chaperonin GroEL
NP_418567.1

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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
    4371025..4372671
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_418567.1 chaperonin GroEL [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_418567.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A376ZKM4
    Conserved Domains (1) summary
    PRK00013
    Location:2 → 530
    groEL; chaperonin GroEL; Reviewed
Nucleotide Protein
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