| IED ID | IndEnz0002002857 |
| Enzyme Type ID | protease002857 |
| Protein Name |
Elastase EC 3.4.24.26 Neutral metalloproteinase PAE Pseudolysin Cleaved into: Pro-elastase |
| Gene Name | lasB PA3724 |
| 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 | MKKVSTLDLLFVAIMGVSPAAFAADLIDVSKLPSKAAQGAPGPVTLQAAVGAGGADELKAIRSTTLPNGKQVTRYEQFHNGVRVVGEAITEVKGPGKSVAAQRSGHFVANIAADLPGSTTAAVSAEQVLAQAKSLKAQGRKTENDKVELVIRLGENNIAQLVYNVSYLIPGEGLSRPHFVIDAKTGEVLDQWEGLAHAEAGGPGGNQKIGKYTYGSDYGPLIVNDRCEMDDGNVITVDMNSSTDDSKTTPFRFACPTNTYKQVNGAYSPLNDAHFFGGVVFKLYRDWFGTSPLTHKLYMKVHYGRSVENAYWDGTAMLFGDGATMFYPLVSLDVAAHEVSHGFTEQNSGLIYRGQSGGMNEAFSDMAGEAAEFYMRGKNDFLIGYDIKKGSGALRYMDQPSRDGRSIDNASQYYNGIDVHHSSGVYNRAFYLLANSPGWDTRKAFEVFVDANRYYWTATSNYNSGACGVIRSAQNRNYSAADVTRAFSTVGVTCPSAL |
| Enzyme Length | 498 |
| Uniprot Accession Number | P14756 |
| Absorption | |
| Active Site | ACT_SITE 338; /evidence=ECO:0000305|PubMed:1899664; ACT_SITE 420; /note=Proton donor; /evidence=ECO:0000305|PubMed:1899664 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by phosphoramidon. {ECO:0000269|PubMed:11533066}. |
| 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 elastin, collagen, IgG, and several complement components as well as endogenous pro-aminopeptidase (PubMed:11533066). Autocatalyses processing of its pro-peptide (PubMed:9642203, PubMed:1744034). Processes the pro-peptide of pro-chitin-binding protein (cbpD) (PubMed:9642203). Involved in the pathogenesis of P.aeruginosa infections. {ECO:0000269|PubMed:11533066, ECO:0000269|PubMed:1597429, ECO:0000269|PubMed:1744034, ECO:0000269|PubMed:9642203}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (14); Chain (2); Disulfide bond (2); Helix (10); Metal binding (8); Mutagenesis (1); Natural variant (8); Propeptide (1); Signal peptide (1); Site (1); Turn (3) |
| Keywords | 3D-structure;Autocatalytic cleavage;Calcium;Direct protein sequencing;Disulfide bond;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Secreted;Signal;Virulence;Zinc;Zymogen |
| Interact With | |
| Induction | INDUCTION: Optimal protein expression in vivo requires both Zn(2+) and Ca(2+) during growth (at protein level). {ECO:0000269|PubMed:1597429, ECO:0000269|PubMed:3141383}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1597429, ECO:0000269|PubMed:3141383, ECO:0000269|PubMed:9642203}. Note=Secreted in an Xcp-dependent fashion (a type II secretion pathway). {ECO:0000269|PubMed:9642203}. |
| Modified Residue | |
| Post Translational Modification | PTM: Made as a membrane-associated pre-pro-protein, which is exported to the periplasm (yielding pro-elastase) with removal of the signal peptide. Under certain conditions pro-elastase can accumulate. The pro-peptide is removed in the periplasm yielding a (mature length) 33 kDa protein, probably by autocatalysis (PubMed:1744034). The pro-peptide probably remains associated with elastase and can be secreted (PubMed:9642203). Further alterations (perhaps processing) seems to be required before secretion into the extracellular space (PubMed:1744034). {ECO:0000269|PubMed:11533066, ECO:0000269|PubMed:1744034, ECO:0000269|PubMed:3141383, ECO:0000269|PubMed:9642203}. |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000269|PubMed:1544509 |
| Structure 3D | X-ray crystallography (5) |
| Cross Reference PDB | 1EZM; 1U4G; 3DBK; 6F8B; 6FZX; |
| Mapped Pubmed ID | 17517866; 29485268; 30088919; |
| Motif | |
| Gene Encoded By | |
| Mass | 53,687 |
| Kinetics | |
| Metal Binding | METAL 333; /note="Calcium"; /evidence="ECO:0000269|PubMed:1899664, ECO:0000269|Ref.16, ECO:0000269|Ref.17"; METAL 337; /note="Zinc; catalytic"; /evidence="ECO:0000269|PubMed:1899664, ECO:0000269|Ref.16, ECO:0000269|Ref.17"; METAL 341; /note="Zinc; catalytic"; /evidence="ECO:0000269|PubMed:1899664, ECO:0000269|Ref.16, ECO:0000269|Ref.17"; METAL 361; /note="Zinc; catalytic"; /evidence="ECO:0000269|PubMed:1899664, ECO:0000269|Ref.16, ECO:0000269|Ref.17"; METAL 369; /note="Calcium"; /evidence="ECO:0000269|PubMed:1899664, ECO:0000269|Ref.16, ECO:0000269|Ref.17"; METAL 372; /note="Calcium"; /evidence="ECO:0000269|PubMed:1899664, ECO:0000269|Ref.16, ECO:0000269|Ref.17"; METAL 380; /note="Calcium"; /evidence="ECO:0000269|PubMed:1899664, ECO:0000269|Ref.16, ECO:0000269|Ref.17"; METAL 382; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:1899664, ECO:0000269|Ref.16, ECO:0000269|Ref.17" |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.26; |