D6YRQ1 · D6YRQ1_WADCW

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.

153150100150200250300350400450500
TypeIDPosition(s)Description
Binding site31-34ATP (UniProtKB | ChEBI)
Binding site88-92ATP (UniProtKB | ChEBI)
Binding site416ATP (UniProtKB | ChEBI)
Binding site479-481ATP (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 Functionoxidoreductase 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
      hspB
    • Synonyms
      groEL
      , groL
    • Ordered locus names
      wcw_1396

Organism names

Accessions

  • Primary accession
    D6YRQ1

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.

TypeIDPosition(s)Description
Coiled coil340-367

Sequence similarities

Belongs to the chaperonin (HSP60) family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    531
  • Mass (Da)
    56,044
  • Last updated
    2010-08-10 v1
  • Checksum
    17A10B9633446EC8
MTSPKEIIFEEEARNKLLDGIVQLADIVAFTLGPKGRNVGLEKSWGAPTITNDGSSIVKDIHLKDPCSNMGVAMAQEVVQKIKEKCGDGTTTGTLLLKALVEEGIKQIAAGHSPIGVKRGIDKAVEAIVAAVEKSAIPIKTAQEIKNIATVSASGNETIGSMISEAMEKVGKNGVITIEEGKGTETVIDLVEGMEFDRGYLSAYFCTDLEKMQTTMNNAQILLVDKKIANIHEILPILQAVAASSRELLIIAEDLEGDALSTLVVNRLRGALKVAAVKAPGFGDRRKAMMQDIAILTGGTLITEETGMSLKDAGPEVLGSAEQITITKDRTTIVKGGGSSEAIKARISQLENEISEASSSYDKEKLEERKAKLSGGVAVIRVGAATEPEMKQKKQIFEDSLSSTKAAIEEGIVPGGGVALLRAKKSLESLKLENDEAVGSQIVAKACGTPLKQIAANTGFDGSVILMEVENADTNCGFNVLTEKVEDLVKAGVVDPAKVVINSLIHAASVAGIVLISEALITDAEEDEETE

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP001928
EMBL· GenBank· DDBJ
ADI38746.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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