P42384 · CH602_MYCPA
- ProteinChaperonin GroEL 2
- GenegroEL2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids541 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
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
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | capsule | |
Cellular Component | cell surface | |
Cellular Component | cytoplasm | |
Cellular Component | extracellular region | |
Molecular Function | ATP binding | |
Molecular Function | ATP-dependent protein folding chaperone | |
Molecular Function | isomerase activity | |
Molecular Function | unfolded protein binding | |
Biological Process | protein refolding |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameChaperonin GroEL 2
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium > Mycobacterium avium complex (MAC)
Accessions
- Primary accessionP42384
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 45 | in strain: Linda | ||||
Sequence: A → S | ||||||
Natural variant | 481 | in strain: Linda | ||||
Sequence: E → K | ||||||
Natural variant | 491-492 | in strain: Linda | ||||
Sequence: AD → TE | ||||||
Natural variant | 508 | in strain: Linda | ||||
Sequence: A → S | ||||||
Natural variant | 525 | in strain: Linda | ||||
Sequence: A → T | ||||||
Natural variant | 527 | in strain: Linda | ||||
Sequence: A → P |
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.
PTM/Processing
Features
Showing features for initiator methionine, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000063442 | 2-541 | Chaperonin GroEL 2 | |||
Sequence: AKTIAYDEEARRGLERGLNALADAVKVTLGPKGRNVVLEKKWGAPTITNDGVSIAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKSAKEVETKDQIAATAAISAGDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEGMRFDKGYISGYFVTDAERQEAVLEDPFILLVSSKVSTVKDLLPLLEKVIQAGKPLLIIAEDVEGEALSTLVVNKIRGTFKSVAVKAPGFGDRRKAMLQDMAILTGGQVISEEVGLSLESADISLLGKARKVVVTKDETTIVEGAGDSDAIAGRVAQIRTEIENSDSDYDREKLQERLAKLAGGVAVIKAGAATEVELKERKHRIEDAVRNAKAAVEEGIVAGGGVALLHAIPALDELKLEGEEATGANIVRVALEAPLKQIAFNGGLEPGVVAEKVRNSPAGTGLNAATGEYEDLLKAGIADPVKVTRSALQNAASIAGLFLTTEAVVADKPEKAAAPAGDPTGGMGGMDF |
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 statusComplete
- Length541
- Mass (Da)56,643
- Last updated2007-01-23 v4
- Checksum1D3F40031FF2F780
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 429 | in Ref. 1; CAA52630 | ||||
Sequence: L → P | ||||||
Sequence conflict | 446 | in Ref. 1 and 2 | ||||
Sequence: A → R |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |