| IED ID | IndEnz0002013394 |
| Enzyme Type ID | protease013394 |
| Protein Name |
Tripeptidyl aminopeptidase Tap EC 3.4.14.- |
| Gene Name | tap SCO1230 2SCG1.05c |
| Organism | Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Streptomycetales Streptomycetaceae Streptomyces Streptomyces albidoflavus group Streptomyces coelicolor Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) |
| Enzyme Sequence | MRKSSIRRRATAFGTAGALVTATLIAGAVSAPAASAAPADGHGHGHGHGRSWDREARGAAIAAARAARAGIDWEDCAADWNLPKPIQCGYVTVPMDYAKPYGKQIRLAVDRIGNTGTRSERQGALIYNPGGPGGSGLRFPARVTSKSAVWANTAKAYDFVGFDPRGVGHSAPISCVDPQEFVKAPKADPVPGSEADKRAQRKLAREYAEGCFERSGEMLPHMTTPNTARDLDVIRAALGEKKLNYLGVSYGTYLGAVYGTLFPDHVRRMVVDSVVNPSRDKIWYQANLDQDVAFEGRWKDWQDWVAANDAAYHLGDTRAEVQDQWLKLRAAAAKKPLGGVVGPAELISFFQSAPYYDSAWAPTAEIFSKYVAGDTQALVDAAAPDLSDTAGNASAENGNAVYTAVECTDAKWPANWRTWDRDNTRLHRDHPFMTWANAWMNLPCATWPVKQQTPLNVKTGKGLPPVLIVQSERDAATPYEGAVELHQRFRGSRLITERDAGSHGVTGLVNPCINDRVDTYLLTGGTDARDVTCAPHATPRP |
| Enzyme Length | 541 |
| Uniprot Accession Number | Q9FCD7 |
| Absorption | |
| Active Site | ACT_SITE 249; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 474; /evidence=ECO:0000250; ACT_SITE 503; /note=Proton donor; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.14.- |
| Enzyme Function | FUNCTION: Cleaves tripeptides from the N-termini of proteins. Does not cleave mono- or dipeptides, or N-terminally blocked peptides (By similarity). {ECO:0000250|UniProtKB:Q54410}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Domain (1); Propeptide (1); Signal peptide (1) |
| Keywords | Aminopeptidase;Hydrolase;Protease;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q54410}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..36; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 58,536 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |