| IED ID | IndEnz0002002996 |
| Enzyme Type ID | protease002996 |
| Protein Name |
Protease LasA EC 3.4.24.- Staphylolytic protease |
| Gene Name | lasA PA14_40290 |
| 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 | MQHKRSRALASPRSPFLFALLALAVGGTANAHDDGLPAFRYSAELLGQLQLPSVALPLNDELFLYGRDAEAFDLEAYLALNAPALRDKSEYLEHWSGYYSINPKVLLTLMVMQSGPLGAPDERALAAPLGRLSAKRGFDAQVRDVLQQLSRRYYGFEEYQLRQAAARKAVGEDGLNAASAALLGLLREGAKASAVQGGNPLGAYAQTFQRLFGTPAAELLQPRNRVARQLQAKAALAPPSNLMQLPWRQGYSWQPNGAHSNTGSGYPYSSFDASYDWPRWGSATYSVVAAHAGTVRVLSRCQVRVTHPSGWATNYYHMDQIQVSNGQQVSADTKLGVYASNINTALCEGGSSTGPHLHFSLLYNGAFVSLQGASFGPYRINVGTSNYDNDCRRYYFYNQSAGTTHCAFRPLYNPGLAL |
| Enzyme Length | 418 |
| Uniprot Accession Number | Q02L18 |
| Absorption | |
| Active Site | ACT_SITE 317; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:P14789; ACT_SITE 356; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:P14789 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Involved in proteolysis and elastolysis (degradation of the host protein elastin). Has staphylolytic activity (degrades pentaglycine cross-links in cell wall peptidogylcan), preferring Gly-Gly-|-X substrates where X is Ala or Gly. Enhances the elastolytic but not proteolytic activity of elastase (lasB) and elastolytic activity of other proteases. Degradation of elastin is likely to contribute to the pathogenicity of P.aeruginosa. {ECO:0000250|UniProtKB:P14789}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Disulfide bond (2); Metal binding (3); Propeptide (1); Signal peptide (1) |
| Keywords | Disulfide bond;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Signal;Virulence;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24965220}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..31; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 45,556 |
| Kinetics | |
| Metal Binding | METAL 259; /note=Zinc; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:P14789; METAL 272; /note=Zinc; /evidence=ECO:0000250|UniProtKB:P14789; METAL 358; /note=Zinc; via pros nitrogen; /evidence=ECO:0000250|UniProtKB:P14789 |
| Rhea ID | |
| Cross Reference Brenda |