P42384 · CH602_MYCPA

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.

154150100150200250300350400450500
TypeIDPosition(s)Description
Binding site29-32ATP (UniProtKB | ChEBI)
Binding site86-90ATP (UniProtKB | ChEBI)
Binding site413ATP (UniProtKB | ChEBI)
Binding site476-478ATP (UniProtKB | ChEBI)
Binding site492ATP (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcapsule
Cellular Componentcell surface
Cellular Componentcytoplasm
Cellular Componentextracellular region
Molecular FunctionATP binding
Molecular FunctionATP-dependent protein folding chaperone
Molecular Functionisomerase activity
Molecular Functionunfolded protein binding
Biological Processprotein refolding

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Chaperonin GroEL 2
  • EC number
  • Alternative names
    • 60 kDa chaperonin 2
    • 65 kDa antigen
    • Chaperonin-60 2
      (Cpn60 2
      )
    • Heat shock protein 65

Gene names

    • Name
      groEL2
    • Synonyms
      groL2
      , hsp65, mopA
    • Ordered locus names
      MAP_3936

Organism names

Accessions

  • Primary accession
    P42384

Proteomes

Subcellular Location

Keywords

Phenotypes & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variant45in strain: Linda
Natural variant481in strain: Linda
Natural variant491-492in strain: Linda
Natural variant508in strain: Linda
Natural variant525in strain: Linda
Natural variant527in strain: Linda

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 6 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for initiator methionine, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
ChainPRO_00000634422-541Chaperonin GroEL 2

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.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    541
  • Mass (Da)
    56,643
  • Last updated
    2007-01-23 v4
  • Checksum
    1D3F40031FF2F780
MAKTIAYDEEARRGLERGLNALADAVKVTLGPKGRNVVLEKKWGAPTITNDGVSIAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKSAKEVETKDQIAATAAISAGDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEGMRFDKGYISGYFVTDAERQEAVLEDPFILLVSSKVSTVKDLLPLLEKVIQAGKPLLIIAEDVEGEALSTLVVNKIRGTFKSVAVKAPGFGDRRKAMLQDMAILTGGQVISEEVGLSLESADISLLGKARKVVVTKDETTIVEGAGDSDAIAGRVAQIRTEIENSDSDYDREKLQERLAKLAGGVAVIKAGAATEVELKERKHRIEDAVRNAKAAVEEGIVAGGGVALLHAIPALDELKLEGEEATGANIVRVALEAPLKQIAFNGGLEPGVVAEKVRNSPAGTGLNAATGEYEDLLKAGIADPVKVTRSALQNAASIAGLFLTTEAVVADKPEKAAAPAGDPTGGMGGMDF

Sequence caution

The sequence AAA99670.2 differs from that shown. Reason: Erroneous initiation

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict429in Ref. 1; CAA52630
Sequence conflict446in Ref. 1 and 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X74518
EMBL· GenBank· DDBJ
CAA52630.1
EMBL· GenBank· DDBJ
Genomic DNA
U15989
EMBL· GenBank· DDBJ
AAA99670.2
EMBL· GenBank· DDBJ
Genomic DNA Different initiation
AE016958
EMBL· GenBank· DDBJ
AAS06486.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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