A0A1G2UWQ5 · A0A1G2UWQ5_9BACT
- ProteinATP-dependent Clp protease proteolytic subunit
- GeneclpP
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids189 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
function
Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic activity
- Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 97 | |||||
Sequence: S | ||||||
Active site | 97 | Nucleophile | ||||
Sequence: S | ||||||
Active site | 122 | |||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP-dependent peptidase activity | |
Molecular Function | serine-type endopeptidase activity | |
Biological Process | proteolysis |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameATP-dependent Clp protease proteolytic subunit
- EC number
- Alternative names
Gene names
Organism names
- Taxonomic lineageBacteria > Candidatus Zambryskibacteria
Accessions
- Primary accessionA0A1G2UWQ5
Proteomes
Subcellular Location
Interaction
Subunit
Fourteen ClpP subunits assemble into 2 heptameric rings which stack back to back to give a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes.
Structure
Sequence
- Sequence statusComplete
- Length189
- Mass (Da)20,576
- Last updated2017-02-15 v1
- ChecksumDE57C7EF4B9D3EDA