| IED ID | IndEnz0002016085 |
| Enzyme Type ID | protease016085 |
| Protein Name |
Lysyl endopeptidase EC 3.4.21.50 Protease IV PvdS-regulated endoprotease |
| Gene Name | prpL PA14_09900 |
| Organism | Pseudomonas aeruginosa (strain UCBPP-PA14) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pseudomonadales Pseudomonadaceae Pseudomonas Pseudomonas aeruginosa group Pseudomonas aeruginosa Pseudomonas aeruginosa (strain UCBPP-PA14) |
| Enzyme Sequence | MHKRTYLNACLVLALAAGASQASAAPGASEMAGDVAVLQASPASTGHARFANPNAATSAAGIHFAAPPARRVARAAPLAPKPGTPLQVGVGLKTATPEIDLATLEWIDTPDGRHTARFPISAAGAASLRAAIRLETRSGSLPDDVLLHFAGAGKEIFEASGKDLSLNRPYWSPVIEGDTLTVELVLPANLQPGDLRLSVPQVSYFADSLYKAGYRDGFGASGSCEVDAVCATQSGTRAYDNATAAVAKMVFTSSADGGSYICTGTLLNNGNSPKRQLFWSAAHCIEDQATAATLQTIWFYNTTQCYGDASTINQSVTVLTGGANILHRDAKRDTLLLELKRTPPAGVFYQGWSATPIANGSLGHDIHHPRGDAKKYSQGNVSAVGVTYDGHTALTRVDWPSAVVEGGSSGSGLLTVAGDGSYQLRGGLYGGPSYCGAPTSQRNDYFSDFSGVYSQISRYFAP |
| Enzyme Length | 462 |
| Uniprot Accession Number | Q02SZ7 |
| Absorption | |
| Active Site | ACT_SITE 283; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q9HWK6; ACT_SITE 333; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q9HWK6; ACT_SITE 409; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q9HWK6 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Lys-|-Xaa, including Lys-|-Pro.; EC=3.4.21.50; |
| DNA Binding | |
| EC Number | 3.4.21.50 |
| Enzyme Function | FUNCTION: Lysine-specific endoprotease. Involved in corneal virulence. {ECO:0000250|UniProtKB:Q9HWK6}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (3); Modified residue (1); Propeptide (1); Signal peptide (1) |
| Keywords | Autocatalytic cleavage;Disulfide bond;Hydrolase;Phosphoprotein;Protease;Secreted;Serine protease;Signal;Virulence;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24965220}. |
| Modified Residue | MOD_RES 429; /note=Phosphotyrosine; /evidence=ECO:0000269|PubMed:24965220 |
| Post Translational Modification | PTM: Processing of pro-protein to mature protein is probably autocatalytic. {ECO:0000250|UniProtKB:Q9HWK6}. |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 48,178 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |