A0A0G0H5A4 · A0A0G0H5A4_9BACT

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.

155350100150200250300350400450500550
TypeIDPosition(s)Description
Binding site29-32ATP (UniProtKB | ChEBI)
Binding site86-90ATP (UniProtKB | ChEBI)
Binding site412ATP (UniProtKB | ChEBI)
Binding site503ATP (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
      US55_C0006G0018

Organism names

Accessions

  • Primary accession
    A0A0G0H5A4

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.

Family & Domains

Sequence similarities

Belongs to the chaperonin (HSP60) family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    553
  • Mass (Da)
    59,236
  • Last updated
    2015-07-22 v1
  • Checksum
    FD2A95A0EC3BBFE8
MAKQIKYAEEARQELMAGVNQLADAVVTTFGPKGRNVALDKKWGSPSVINDGVSVAKEIELKDPFQNMGAQLVKEAASKTADIAGDGTTTATVLAREIVSEGIKMITAKANPILMRKGLEKASEHVASELKKMSKVLKSTDWANVAIVSSGDVELGNLIAEALKKVGKDGVVTVEEGKGLSTEIEYKEGMEFDKGYASAYMVTNSDRMEAEIEDPYILITDKKISALNELLPFLENLVKVSKNLVIIADEIDGEALATLVVNKLRGTFNALAIKAPGFGDRRKEMLEDIAILTGGTVISDDTGRKFDSVTIEDCGRADKVWADKDNSRIIGGKGIKTKIASRITQIRKTIEASTSDFDKEKLQERLAKLSGGVAVINVGAATEIEMKDRKERVNDAVAATKAALEEGIVPGGAVALLDISRKMDVKDLEKAGENKDVIIGFEIVKRALESPFVQLMKNSGLDAGQLIAKAREVSAYGQGFDIMKTDSVEKAVPVDMLKAGIIDPVKVVRTAVQNAISVATMILVTEALVTDIKEPDKSMSGGMPPGGMGGMDY

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LBTK01000006
EMBL· GenBank· DDBJ
KKQ38463.1
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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