O66202 · CH60_SERRU

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.

153950100150200250300350400450500
TypeIDPosition(s)Description
Binding site30-33ATP (UniProtKB | ChEBI)
Binding site51ATP (UniProtKB | ChEBI)
Binding site87-91ATP (UniProtKB | ChEBI)
Binding site415ATP (UniProtKB | ChEBI)
Binding site495ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular FunctionATP-dependent protein folding chaperone
Molecular Functionisomerase activity
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
      , mopA

Organism names

Accessions

  • Primary accession
    O66202

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000635261-539Chaperonin GroEL

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

Structure

Family & Domains

Sequence similarities

Belongs to the chaperonin (HSP60) family.

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    539
  • Mass (Da)
    56,640
  • Last updated
    1998-08-01 v1
  • Checksum
    CE447B657515D4F0
MAAKDVKFGNDARVKMLNGVNILADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEDKFENMGAQMVKEVASKANDAAGDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKKLSVPCSDSKAIAQVGTISANSDETVGKLIAEAMEKVGKEGVITVEEGTGLQDELDVVEGMQFDRGYLSPYFINKPETGSVELESPFILLADKKVSNIRELLPVLEAVAKAGKPLLIVAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTAGTVISEEIGMELEKATLEDLGQAKRVVINKDTTIIIDGIGDEATIQGRVAQIRQQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEEGVVAGGGVALIRVASKIAELKGDNEDQNVGIKVALRAMEAPLRQIVINAGEEASVIANSVKAGEGSYGYNAYSEEYGDMIGMGILDPTKVTRSALQYAASVAGLMITTECMVTDLPKEDKADMGAAGMGG

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue539

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB008143
EMBL· GenBank· DDBJ
BAA25219.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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