O66202 · CH60_SERRU
- ProteinChaperonin GroEL
- GenegroEL
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids539 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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.
Catalytic activity
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | ATP-dependent protein folding chaperone | |
Molecular Function | isomerase activity | |
Biological Process | protein refolding |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameChaperonin GroEL
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Yersiniaceae > Serratia
Accessions
- Primary accessionO66202
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000063526 | 1-539 | Chaperonin GroEL | |||
Sequence: MAAKDVKFGNDARVKMLNGVNILADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEDKFENMGAQMVKEVASKANDAAGDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKKLSVPCSDSKAIAQVGTISANSDETVGKLIAEAMEKVGKEGVITVEEGTGLQDELDVVEGMQFDRGYLSPYFINKPETGSVELESPFILLADKKVSNIRELLPVLEAVAKAGKPLLIVAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTAGTVISEEIGMELEKATLEDLGQAKRVVINKDTTIIIDGIGDEATIQGRVAQIRQQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEEGVVAGGGVALIRVASKIAELKGDNEDQNVGIKVALRAMEAPLRQIVINAGEEASVIANSVKAGEGSYGYNAYSEEYGDMIGMGILDPTKVTRSALQYAASVAGLMITTECMVTDLPKEDKADMGAAGMGG |
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
Sequence
- Sequence statusFragment
- Length539
- Mass (Da)56,640
- Last updated1998-08-01 v1
- ChecksumCE447B657515D4F0
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 539 | |||||
Sequence: G |