A0A2G5X131 · A0A2G5X131_9BACL
- ProteinPeptidase T
- GenepepT
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids408 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Cleaves the N-terminal amino acid of tripeptides.
Catalytic activity
Cofactor
Note: Binds 2 Zn2+ ions per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 79 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Active site | 81 | ||||
Binding site | 140 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 140 | Zn2+ 2 (UniProtKB | ChEBI) | |||
Active site | 174 | Proton acceptor | |||
Binding site | 175 | Zn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 197 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 379 | Zn2+ 2 (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | metallopeptidase activity | |
Molecular Function | tripeptide aminopeptidase activity | |
Molecular Function | zinc ion binding | |
Biological Process | peptide catabolic process | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePeptidase T
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Planococcaceae > Sporosarcina
Accessions
- Primary accessionA0A2G5X131
Proteomes
Subcellular Location
Structure
Family & Domains
Sequence
- Sequence statusComplete
- Length408
- Mass (Da)45,465
- Last updated2018-01-31 v1
- Checksum59C1F13D48F0E2F5
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
PDYO01000008 EMBL· GenBank· DDBJ | PIC69989.1 EMBL· GenBank· DDBJ | Genomic DNA |