| IED ID | IndEnz0002010337 |
| Enzyme Type ID | protease010337 |
| Protein Name |
Elastase EC 3.4.24.26 Cleaved into: Pro-elastase |
| Gene Name | lasB PA14_16250 |
| 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 | MKKVSTLDLLFVAIMGVSPAAFAADLIDVSKLPSKAAQGAPGPVTLQAAVGAGGADELKAIRSTTLPNGKQVTRYEQFHNGVRVVGEAITEVKGPGKSVAARRSGHFVANIAADLPGSTTAAVSAEQVLAQAKSLKAQGRKTENDKVELVIRLGENNIAQLVYNVSYLIPGEGLSRPHFVIDAKTGEVLDQWEGLAHAEAGGPGGNQKIGKYTYGSDYGPLIVNDRCEMDDGNVITVDMNGSTNDSKTTPFRFACPTNTYKQVNGAYSPLNDAHFFGGVVFNLYRDWFGTSPLTHKLYMKVHYGRSVENAYWDGTAMLFGDGATMFYPLVSLDVAAHEVSHGFTEQNSGLIYRGQSGGMNEAFSDMAGEAAEFYMRGKNDFLIGYDIKKGSGALRYMDQPSRDGRSIDNASQYYNGIDVHHSSGVYNRAFYLLANSPGWDTRKAFEVFVDANRYYWTATSNYNSGACGVISSAQNRNYSAADVTRAFSTVGVTCPSAL |
| Enzyme Length | 498 |
| Uniprot Accession Number | Q02RJ6 |
| Absorption | |
| Active Site | ACT_SITE 338; /evidence=ECO:0000250|UniProtKB:P14756; ACT_SITE 420; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P14756 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins including elastin, collagen types III and IV, fibronectin and immunoglobulin A, generally with bulky hydrophobic group at P1'. Insulin B chain cleavage pattern identical to that of thermolysin, but specificity differs in other respects.; EC=3.4.24.26; |
| DNA Binding | |
| EC Number | 3.4.24.26 |
| Enzyme Function | FUNCTION: Cleaves host elastase, collagen, IgI and several complement components as well as endogenous pro-aminopeptidase, pro-chitin-binding protein (cbpD). Cleaves its own pro-peptide. Involved in the pathogenesis of P.aeruginosa infections. {ECO:0000250|UniProtKB:P14756}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (2); Disulfide bond (2); Metal binding (8); Modified residue (1); Propeptide (1); Signal peptide (1); Site (1) |
| Keywords | Autocatalytic cleavage;Calcium;Disulfide bond;Hydrolase;Metal-binding;Metalloprotease;Phosphoprotein;Protease;Secreted;Signal;Virulence;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24965220}. |
| Modified Residue | MOD_RES 236; /note=Phosphothreonine; /evidence=ECO:0000269|PubMed:24965220 |
| Post Translational Modification | PTM: Made as a pre-pro-protein which is exported to the periplasm. Probably autocatalyzes cleavage of its pro-peptide. The pro-peptide can be secreted with mature elastase. {ECO:0000250|UniProtKB:P14756}. |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 53,601 |
| Kinetics | |
| Metal Binding | METAL 333; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P14756; METAL 337; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P14756; METAL 341; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P14756; METAL 361; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P14756; METAL 369; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P14756; METAL 372; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P14756; METAL 380; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P14756; METAL 382; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P14756 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.26; |