| IED ID | IndEnz0002006652 |
| Enzyme Type ID | protease006652 |
| Protein Name |
Protease LasA EC 3.4.24.- Staphylolytic protease |
| Gene Name | lasA PA1871 |
| 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 | MQHKRSRAMASPRSPFLFVLLALAVGGTANAHDDGLPAFRYSAELLGQLQLPSVALPLNDDLFLYGRDAEAFDLEAYLALNAPALRDKSEYLEHWSGYYSINPKVLLTLMVMQSGPLGAPDERALAAPLGRLSAKRGFDAQVRDVLQQLSRRYYGFEEYQLRQAAARKAVGEDGLNAASAALLGLLREGAKVSAVQGGNPLGAYAQTFQRLFGTPAAELLQPSNRVARQLQAKAALAPPSNLMQLPWRQGYSWQPNGAHSNTGSGYPYSSFDASYDWPRWGSATYSVVAAHAGTVRVLSRCQVRVTHPSGWATNYYHMDQIQVSNGQQVSADTKLGVYAGNINTALCEGGSSTGPHLHFSLLYNGAFVSLQGASFGPYRINVGTSNYDNDCRRYYFYNQSAGTTHCAFRPLYNPGLAL |
| Enzyme Length | 418 |
| Uniprot Accession Number | P14789 |
| Absorption | |
| Active Site | ACT_SITE 317; /note=Proton donor/acceptor; /evidence=ECO:0000305|PubMed:20026068; ACT_SITE 356; /note=Proton donor/acceptor; /evidence=ECO:0000305|PubMed:20026068 |
| 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 (PubMed:11179971). Enhances the elastolytic but not proteolytic activity of elastase (lasB) and elastolytic activity of other proteases (PubMed:2110137). Degradation of host elastin is likely to contribute to the pathogenicity of P.aeruginosa. While either His-317 or His-356 can abstract a proton in the hydrolysis reaction, the same residue performs both functions in a given catalytic cycle, with the other stabilizing the catalytic intermediate (PubMed:20026068). {ECO:0000269|PubMed:11179971, ECO:0000269|PubMed:1597429, ECO:0000269|PubMed:20026068, ECO:0000269|PubMed:2110137, ECO:0000269|PubMed:8932318}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8-9, inactive at pH 6 and below. {ECO:0000269|PubMed:20026068}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (12); Chain (1); Disulfide bond (2); Erroneous initiation (1); Erroneous termination (1); Frameshift (1); Helix (1); Metal binding (3); Mutagenesis (1); Propeptide (1); Sequence conflict (6); Signal peptide (1); Turn (4) |
| Keywords | 3D-structure;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}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11179971, ECO:0000269|PubMed:1597429, ECO:0000269|PubMed:2110137, 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: Processing of pro-LasA can occur extracellularly and requires elastase (lasB) (PubMed:9642203). Secretion and processing may be linked (PubMed:8932318). {ECO:0000269|PubMed:8932318, ECO:0000269|PubMed:9642203}. |
| Signal Peptide | SIGNAL 1..31; /evidence=ECO:0000303|PubMed:8932318 |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 3IT5; 3IT7; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 45,517 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=58 uM for Dabsyl-Leu-Gly-Gly-Gly-Ala-Edans at pH 9 {ECO:0000269|PubMed:20026068}; KM=61 uM for Dabsyl-Leu-Gly-Gly-Gly-Ala-Edans at pH 8 {ECO:0000269|PubMed:20026068}; KM=105 uM for Dabsyl-Leu-Gly-Gly-Gly-Ala-Edans at pH 7 {ECO:0000269|PubMed:20026068}; Note=kcat is 5.1 sec(-1), 5.3 sec(-1), 1.7 sec(-1) at pH 9, 8 and 7 respectively. {ECO:0000269|PubMed:20026068}; |
| Metal Binding | METAL 259; /note=Zinc; via tele nitrogen; /evidence=ECO:0000269|PubMed:20026068; METAL 272; /note=Zinc; /evidence=ECO:0000269|PubMed:20026068; METAL 358; /note=Zinc; via pros nitrogen; /evidence=ECO:0000269|PubMed:20026068 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.B16; |