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A0A0D6KM56 · A0A0D6KM56_9CYAN

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.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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.

154650100150200250300350400450500
TypeIDPosition(s)Description
Binding site29-32ATP (UniProtKB | ChEBI)
Binding site86-90ATP (UniProtKB | ChEBI)
Binding site413ATP (UniProtKB | ChEBI)
Binding site495ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular ComponentGroEL-GroES complex
Molecular FunctionATP binding
Molecular FunctionATP-dependent protein folding chaperone
Molecular Functionisomerase activity
Molecular Functionunfolded protein binding
Biological Processchaperone cofactor-dependent protein refolding
Biological Processprotein refolding
Biological Processresponse to heat

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
      FDUTEX481_08514

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • PCC 7601 / UTEX B 481
  • Taxonomic lineage
    Bacteria > Cyanobacteriota > Cyanophyceae > Nostocales > Tolypothrichaceae > Tolypothrix

Accessions

  • Primary accession
    A0A0D6KM56

Proteomes

Subcellular Location

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.

Type
IDPosition(s)Description
Coiled coil337-364
Region527-546Disordered

Sequence similarities

Belongs to the chaperonin (HSP60) family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    546
  • Mass (Da)
    57,736
  • Last updated
    2015-05-27 v1
  • MD5 Checksum
    81DA600878F9FC359D24A4DDB2EED37C
MAKRIIYNENARRALEKGIDILAEAVAVTLGPKGRNVVLEKKFGAPQIVNDGVTIAKEIELEDHVENTGVSLIRQAASKTNDAAGDGTTTATVLAHAIVKEGLRNVAAGANAIEIKRGIDKATGFLVDKIKEHARPVEDSKAIAQVAAISAGNDEVVGALIAEALDKVGREGVISLEEGKSVTTELEVTEGLNFDKGYISPYFATDAERLEAVFDEPFLLLTDKKIALVQDLVPVLEQVARAGRPLVIIAEDIEKEALATLVVNRLRGVLNVAAVKAPGFGDRRKAILEDIAILTGGQLITEDAGLRLDATKIDQLGKARRITITKDSTTLVAEGNEQAVKARVEQIRRQIEETESSYDKEKLQERLAKLAGGVAVVKVGAATETELKDRKLRLEDAINATKAAVEEGIVPGGGTTLAHLAPGLEEWAKSNLVNEELTGALIVSRALSAPLKRIAENAGQNGAVIAERVKEKEFNVGYDATTGDFVDLFEAGIVDPAKVTRSAVQNAASIAGMVLTTEAIVVDKPEPKDAAPAAPGGGGLGGDFDY

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AGCR01000051
EMBL· GenBank· DDBJ
EKF00857.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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