P49464 · CH60_TRICV

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.

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.

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TypeIDPosition(s)Description
Binding site29-32ATP (UniProtKB | ChEBI)
Binding site86-90ATP (UniProtKB | ChEBI)
Binding site415ATP (UniProtKB | ChEBI)
Binding site481-483ATP (UniProtKB | ChEBI)
Binding site497ATP (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 Componentchloroplast
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, chloroplastic
  • EC number
  • Alternative names
    • 60 kDa chaperonin
    • Chaperonin-60
      (Cpn60
      )

Gene names

    • Name
      groEL
    • Synonyms
      groL

Encoded on

  • Chloroplast

Organism names

Accessions

  • Primary accession
    P49464

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000636261-528Chaperonin GroEL, chloroplastic

Interaction

Subunit

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

Structure

Family & Domains

Sequence similarities

Belongs to the chaperonin (HSP60) family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    528
  • Mass (Da)
    57,128
  • Last updated
    1996-02-01 v1
  • Checksum
    E04317FEC9EF2EE8
MAKKILYQDNARRALERGMEIMVEAVSVTLGPKGRNVVLEKPYGSPQIVNDGVTIAKEINLEDHIENTGVALIRQAASKTNDVAGDGTTTATVLAYAMVKEGLKNVTAGANPISIKLGMEKATQYLVTQINEFAQPVEDIQSIEQVASISAGNDNLIGSLIADALSKVGKEGVISLEEGKGIITELEITEGMKLEKGFISPYFITNTEKMEVSYENPFILLTDKRITLVQQDLLPILEQITKTKRPLLLIAEDVEKEALATLILNKLRGIVNVVAVRAPGFGELRKQMLEDIAVLTGGTVITQDAGLSLENIQVNLLGQARRIIVNKDSTTIVGDGLEIEQIKARCEQLRKQVNIADTGYEKEKLQDRIAKLSGGIAVIRVGAVTETEMKDKKLRLEDAINATRAAVEEGIVPGGGATLAHLAENLLTWAKINLKEDELIGAMIISRAIVAPLKRIAENAGINGPVIIEKVQQQEFEIGYNAAKNVFGNMYDEGIVDPAKVTRSGLQNATSIASMILTTECIIVDETD

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
Z67753
EMBL· GenBank· DDBJ
CAA91651.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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