A0A0N9IF12 · A0A0N9IF12_9PSEU

Function

function

Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

  • ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide.
    EC:5.6.1.7 (UniProtKB | ENZYME | Rhea)

Features

Showing features for binding site.

154050100150200250300350400450500
TypeIDPosition(s)Description
Binding site29-32ATP (UniProtKB | ChEBI)
Binding site86-90ATP (UniProtKB | ChEBI)
Binding site413ATP (UniProtKB | ChEBI)
Binding site477-479ATP (UniProtKB | ChEBI)
Binding site493ATP (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcapsule
Cellular Componentcell surface
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular FunctionATP-dependent protein folding chaperone
Molecular Functionisomerase activity
Molecular Functionunfolded protein binding
Biological Processprotein refolding

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Chaperonin GroEL
  • EC number
  • Alternative names
    • 60 kDa chaperonin
    • Chaperonin-60
      (Cpn60
      )

Gene names

    • Name
      groEL
    • Synonyms
      groL
    • ORF names
      AOZ06_49315

Organism names

  • Taxonomic identifier
  • Strain
    • KLBMP1111
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Pseudonocardiales > Pseudonocardiaceae > Kibdelosporangium

Accessions

  • Primary accession
    A0A0N9IF12

Proteomes

Subcellular Location

Cell surface
Cytoplasm
Secreted, capsule
Secreted, cell wall

Keywords

Interaction

Subunit

Forms a cylinder of 14 subunits composed of two heptameric rings stacked back-to-back. Interacts with the co-chaperonin GroES.

Protein-protein interaction databases

Family & Domains

Features

Showing features for coiled coil, region, compositional bias.

TypeIDPosition(s)Description
Coiled coil330-357
Region516-540Disordered
Compositional bias517-533Basic and acidic residues

Sequence similarities

Belongs to the chaperonin (HSP60) family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    540
  • Mass (Da)
    56,688
  • Last updated
    2016-01-20 v1
  • Checksum
    D076386AEF573954
MPKQISFDEDARRALERGVNKLADAVKVTLGPRGRHVVLAKKFGGPTVTLDGVTVAREIELEDSFENLGAQLAKSVATKTNDVAGDGTTTATVLAQALVRVGMRNIAAGANPTSLGRGIQAAVDKVVEVLTAKATPIKGRDNIAQVGTVTSRDASIGALLGEAIERVGEDGVITVEESSTLATELVITEGVQFDKGYISAHFATDAEAQEAVLEDAYILLFREKISALADLLPILEKIVQASKPVLIIAEDIEGEALSTLVVNSARKTIKAVAVKAPFFGDRRKAFLDDLAFVTGGQVVSSEIGMKLAEVGLDVLGSARRIVVTKDETTIIEGKGDKAEVQARVEQLRKEIEASDSDWDREKLQERLAKLAGGVAVIRVGAATETELTERKHRIEDAVAATKAAVEEGIVPGGGSAIVHAAKELEGNLGLTGDEATGVAIVREALAAPLHWIASNAGLEGAVVVHRVREADWGHGLNAAKLTYGDLVAEGIIDPVKVTRSAVTNAASIARMVLTTESSVVEKKEEEPPAAGHGHGHGHGH

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias517-533Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP012752
EMBL· GenBank· DDBJ
ALG13810.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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