IED ID | IndEnz0002003452 |
Enzyme Type ID | protease003452 |
Protein Name |
Extracellular cysteine protease EC 3.4.22.- Staphopain |
Gene Name | ecpA ecp |
Organism | Staphylococcus epidermidis |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Staphylococcaceae Staphylococcus Staphylococcus epidermidis |
Enzyme Sequence | MYAEYVNQLKNFRIRETQGYNSWCAGYTMSALLNATYNTNRYNAESVMRYLHPNLRGHDFQFTGLTSNEMLRFGRSQGRNTQYLNRMTSYNEVDQLTTNNQGIAVLGKRVESSDGIHAGHAMAVAGNAKVNNGQKVILIWNPWDNGLMTQDAHSNIIPVSNGDHYEWYASIYGY |
Enzyme Length | 174 |
Uniprot Accession Number | P0C0P9 |
Absorption | |
Active Site | ACT_SITE 24; /evidence=ECO:0000255|PROSITE-ProRule:PRU10089; ACT_SITE 120; /evidence=ECO:0000255|PROSITE-ProRule:PRU10089; ACT_SITE 141; /evidence=ECO:0000255|PROSITE-ProRule:PRU10089 |
Activity Regulation | ACTIVITY REGULATION: Inhibited by heavy metal ions such as Zn(2+) or Ni(2+), iodoacetamide, N-ethylmaleimide, leupeptin, SDS and E-64. Also inhibited by chloromethylketones TPCK and TLCK and by human plasma inhibitor alpha-2-macroglobulin. Stimulated by L-cysteine. {ECO:0000269|PubMed:11767947}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.22.- |
Enzyme Function | FUNCTION: Cysteine protease able to cleave elastin, insulin, myoglobin, fibronectin, fibrinogen, HMW-kininogen, alpha-1-protease inhibitor and alpha-1-antitrypsin. Along with other extracellular proteases may contribute to the colonization and infection of human tissues. {ECO:0000269|PubMed:11767947, ECO:0000269|PubMed:15255185}. |
Temperature Dependency | |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0 for elastin hydrolysis.; |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (1) |
Keywords | Cell wall;Direct protein sequencing;Hydrolase;Protease;Secreted;Thiol protease;Virulence;Zymogen |
Interact With | |
Induction | INDUCTION: Expression occurs in a growth-phase-dependent manner with optimal expression at post-exponential phase. {ECO:0000269|PubMed:15255185}. |
Subcellular Location | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:15255185}. Secreted {ECO:0000269|PubMed:15255185}. |
Modified Residue | |
Post Translational Modification | PTM: Proteolytically cleaved. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 19,832 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |