| IED ID | IndEnz0002011575 |
| Enzyme Type ID | protease011575 |
| Protein Name |
Protease 2 EC 3.4.21.83 Oligopeptidase B Protease II |
| Gene Name | ptrB |
| Organism | Moraxella lacunata |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Moraxellales Moraxellaceae Moraxella Moraxella lacunata |
| Enzyme Sequence | MKLPIAKRIPHPHELHGDVREDDYYWLKDRDNTEVIQYLEEENRYYHEIMRPLQEQTEQIYESMVDRVPDSEMKVPVQHGQFFYYSRLDKNKQYPIYARKQAASRALLQDATEEVVLDLNELAEEDDYLSVTVQRMTTDHSRLAYLENRDGTDRYTIYIKDLNTGELLSDRVPNVYIYGSMEWCRCGDYIFYTTVDEHQRPCQLWRHRLGSDVESDELIFEEKDDTFTLFISKSQSGKFIFVYSSSKTTSEIHMIDTDSPLSPLQLVDERRDGILYDVEHWEDDLLILTNEGALNFQLLRCPLNDLSSKVNVVEYNEERYLQEMYPFRDKLLIAGRENGLTQIWVVHDGELQQISWDEPLYTVAVLSEQSYDTNEVLIQYESLLTPKTTFGLNLQTGEKQCLQVAPVSGEYDRSQFRQEQLWATGRSGVKVPMTAVYLEGALDNGPAPLILYGYGSYGSNSDPRFDPYRLPLLEKGIVFVTAQVRGGSEMGRGWYEDGKMQNKRNTFTDFIAAAKHLIDQNYTSPTKMAARGGSAGGLLVGAVANMAGELFKVIVPAVPFVDVVTTMLDTSIPLTTLEWDEWGDPRKQEDYFYMKSYSPYDNVEAKDYPHMYITTGINDPRVGYFEPAKWVARLRAVKTDNNTLVMKTNMGAGHFGKSGRFNHLKEAAESYAFILDKLGVEAEEKVLNHR |
| Enzyme Length | 690 |
| Uniprot Accession Number | Q59536 |
| Absorption | |
| Active Site | ACT_SITE 534; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10084; ACT_SITE 619; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10084; ACT_SITE 654; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10084 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of -Arg-|-Xaa- and -Lys-|-Xaa- bonds in oligopeptides, even when P1' residue is proline.; EC=3.4.21.83; |
| DNA Binding | |
| EC Number | 3.4.21.83 |
| Enzyme Function | FUNCTION: Cleaves peptide bonds on the C-terminal side of lysyl and argininyl residues. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1) |
| Keywords | Hydrolase;Protease;Serine protease |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 79,507 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.83; |