A0A6N8H3S7 · A0A6N8H3S7_9FIRM

  • Protein
    Chaperonin GroEL
  • Gene
    groL
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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.

154350100150200250300350400450500
TypeIDPosition(s)Description
Binding site29-32ATP (UniProtKB | ChEBI)
Binding site86-90ATP (UniProtKB | ChEBI)
Binding site414ATP (UniProtKB | ChEBI)
Binding site497ATP (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
      EP147_05730

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • P1-4
  • Taxonomic lineage
    Bacteria > Bacillota > Clostridia > Eubacteriales > Oscillospiraceae > Subdoligranulum

Accessions

  • Primary accession
    A0A6N8H3S7

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
    543
  • Mass (Da)
    57,455
  • Last updated
    2020-10-07 v1
  • Checksum
    D24A13B9E3FC45D4
MAKQIKQGEDARKALCAGIDQLADTVKVTLGPKGRNVVLSKKFGSPLITNDGVTIAKEIELKDEFENMGAQLVREVATKTNDAAGDGTTTATVLAQALVTEGMKNVTAGANPMDIKRGMQKAVAAAVASVKEHSQKVNGSKDIARVGTVSAGDAEIGQLIADAMEKVTADGVITIEENKTTAETYTEVVEGMQFDRGYVTPYMVTDTEKMETVYDDCSVLITDKKISVFQDVVPLLEQVIQSGRKLLIIAEDVEGDALSNLIINRLRGGLNVVAVKAPGFGDRRKEMLQDIAILTGGTVISSDLGYELKDATMQLLGTARQVKVTKENTTIVGGAGDKQAIADRVAQIRSQIVSATSDFDREKLQERLAKMAGGVAVIKVGAATEVEMKDKKLRIEDALNATKAAVEEGIVAGGGTATINAIPAVDKVVNELEGDERTGAKIVRKALEAPLRQIAKNAGLEGSVIIDNILKANKANYGFDAQKEEYVEDMIEAGIVDPTKVTRSALENAASVAAMVLTTESLVADLPEPPAPAAPNPDMGGMY

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
SCPH01000001
EMBL· GenBank· DDBJ
MUT95367.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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