| IED ID | IndEnz0002004675 |
| Enzyme Type ID | protease004675 |
| Protein Name |
Lysyl endopeptidase EC 3.4.21.50 Protease IV PvdS-regulated endoprotease |
| Gene Name | prpL PA4175 |
| Organism | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pseudomonadales Pseudomonadaceae Pseudomonas Pseudomonas aeruginosa group Pseudomonas aeruginosa Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
| Enzyme Sequence | MHKRTYLNACLVLALAAGASQALAAPGASEMAGDVAVLQASPASTGHARFANPNAAISAAGIHFAAPPARRVARAAPLAPKPGTPLQVGVGLKTATPEIDLTTLEWIDTPDGRHTARFPISAAGAASLRAAIRLETHSGSLPDDVLLHFAGAGKEIFEASGKDLSVNRPYWSPVIEGDTLTVELVLPANLQPGDLRLSVPQVSYFADSLYKAGYRDGFGASGSCEVDAVCATQSGTRAYDNATAAVAKMVFTSSADGGSYICTGTLLNNGNSPKRQLFWSAAHCIEDQATAATLQTIWFYNTTQCYGDASTINQSVTVLTGGANILHRDAKRDTLLLELKRTPPAGVFYQGWSATPIANGSLGHDIHHPRGDAKKYSQGNVSAVGVTYDGHTALTRVDWPSAVVEGGSSGSGLLTVAGDGSYQLRGGLYGGPSYCGAPTSQRNDYFSDFSGVYSQISRYFAP |
| Enzyme Length | 462 |
| Uniprot Accession Number | Q9HWK6 |
| Absorption | |
| Active Site | ACT_SITE 283; /note=Charge relay system; /evidence=ECO:0000305|PubMed:12419815; ACT_SITE 333; /note=Charge relay system; /evidence=ECO:0000305|PubMed:12419815; ACT_SITE 409; /note=Charge relay system; /evidence=ECO:0000305|PubMed:12419815 |
| 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 (PubMed:12419815). Involved in corneal virulence. {ECO:0000305|PubMed:12419815}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (3); Mutagenesis (6); Propeptide (1); Sequence conflict (5); Signal peptide (1) |
| Keywords | Autocatalytic cleavage;Direct protein sequencing;Disulfide bond;Hydrolase;Protease;Reference proteome;Secreted;Serine protease;Signal;Virulence;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12419815}. Note=Experiments performed in E.coli. |
| Modified Residue | |
| Post Translational Modification | PTM: Experiments performed in E.coli. Processing of pro-endopeptidase to mature endopeptidase is probably autocatalytic, as mutations in the probable active site residues prevent processing, and purified inactive pro-endopeptidase disappears in the presence of active endopeptidase. {ECO:0000305|PubMed:12419815}. |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 48,213 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |