A0A4R9WYG7 · A0A4R9WYG7_9HYPH

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.

154850100150200250300350400450500
TypeIDPosition(s)Description
Binding site30-33ATP (UniProtKB | ChEBI)
Binding site51ATP (UniProtKB | ChEBI)
Binding site87-91ATP (UniProtKB | ChEBI)
Binding site415ATP (UniProtKB | ChEBI)
Binding site496ATP (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
      groL
    • Synonyms
      groEL
    • ORF names
      EN859_033540

Organism names

Accessions

  • Primary accession
    A0A4R9WYG7

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

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region526-548Disordered
Compositional bias533-548Basic and acidic residues

Sequence similarities

Belongs to the chaperonin (HSP60) family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    548
  • Mass (Da)
    58,286
  • Last updated
    2019-07-31 v1
  • Checksum
    8AB00110E137B627
MSAKEIIFSFEARDRMLRGIDTLANAVRVTLGPRGRNVAIGSEHGAPRVTKDGVTVAREIELDNKFENMGAQMVREIATKTSYQAGDGTTTAVVLAHAIAREGAKAVAAGMNPMDLKRGIDLAVEAVVAELKNNATKVTSNVEIAQVGTISANGDREIGRCLADAMKRVGNDGVITVEDGTSLETELEFVEGMQFDRGYISPRFITNRAKMRVEMQDAYVLISEKKLSSLNEILPLLEKVVQAAKPLLIIAEDVEGEVIAALVVNKLRGALKVAAVKAPAYGDRRKAMLQDIALMTGGTVISEDLGLKLENVSLETLGRTKKVMIDKGNTTIVGGAGKRASIEARIAEIKIQLAETTSDYDREKLQERLARLAGGVAVIRVGGATEVEVREKKDRIDDAMNATRAAVAEGILPGGGVALLRAGRALKKLKGGNEDQQVGIAIVGKAITWPARQIAINAGLEGLVVIAGILENDDNAYGYDAQSGVYGDLVSKGIIDPAKVVRTALQGAASVAGLLIMTEAMVAEVPGPPPPELPGHEHHHHHDMDLDF

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias533-548Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
SADR02000047
EMBL· GenBank· DDBJ
TGQ29087.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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