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L7V3Y7 · L7V3Y7_MYCL1

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.

153950100150200250300350400450500
TypeIDPosition(s)Description
Binding site29-32ATP (UniProtKB | ChEBI)
Binding site86-90ATP (UniProtKB | ChEBI)
Binding site413ATP (UniProtKB | ChEBI)
Binding site478-480ATP (UniProtKB | ChEBI)
Binding site494ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcapsule
Cellular Componentcell surface
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
    • Ordered locus names
      MULP_01258

Organism names

Accessions

  • Primary accession
    L7V3Y7

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.

Structure

Family & Domains

Features

Showing features for region, compositional bias.

Type
IDPosition(s)Description
Region520-539Disordered
Compositional bias522-539Basic and acidic residues

Sequence similarities

Belongs to the chaperonin (HSP60) family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    539
  • Mass (Da)
    55,858
  • Last updated
    2013-04-03 v1
  • MD5 Checksum
    58418D2E2307FEFD0F4C79340E5AE414
MSKLIEYDETARRAMEAGVDKLADTVRVTLGPRGRHVVLAKSFGGPTVTNDGVTVARDIDLEDPFENLGAQLVKSVATKTNDVAGDGTTTATVLAQALVKTGLRLVAAGINPIALGSGIGKAADAVSEALLASATPVSGKDAIAQVATVSSRDQLIGDLVGEAMSKVGHDGVVSVEESSTLGTELEFTEGVGFDKGYLSAYFVTDFDAQQAVLEDPLILLHQDKISSLPDLLPLLEKVAESGKPLMIIAEDIEGEALATLVVNSIRKTLKAIAVKSPYFGDRRKAFLQDLAAVTGAEVVNPDAGLVLREVGLEVMGSARRVVVSKDDTIIVDGGGAPEAVEARVNLLRSEIDRSDSEWDREKLGERLAKLAGGVAVIKVGAATETELKKRKESVEDAVAAAKAAVEEGIVAGGGSALIQARNALKDLRASLSGDEAVGVDVFSEALAAPLYWIATNAGLDGSVVVNKVSELPAGHGLNAATLTYGDLAADGIVDPVKVTRSAVLNASSVARMVLTTETAIVDKPAEPEDDGHGHHGHAH

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias522-539Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP003899
EMBL· GenBank· DDBJ
AGC61255.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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