| IED ID | IndEnz0002003453 |
| Enzyme Type ID | protease003453 |
| Protein Name |
Extracellular cysteine protease EC 3.4.22.- Staphopain |
| Gene Name | ecpA ecp SERP2390 |
| Organism | Staphylococcus epidermidis (strain ATCC 35984 / RP62A) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Staphylococcaceae Staphylococcus Staphylococcus epidermidis Staphylococcus epidermidis (strain ATCC 35984 / RP62A) |
| Enzyme Sequence | MKKKLSYMITIMLAFTLSLALGLFFNSAHADSLPQKNGANQKTTKVTVSNKDVPDAVRKLAEEQYLSRVALLDKASNHKATSYTLGEPFKIYKFNKESDGNYYYPVLNKKGDVVYVVTISPNPSNSKASKQQNNYSINVSPFLSKILNQYKNQKITILTNTKGYFALTEDGKVTLVLKTPRNNEKTYENATESTKPKDLNDFKQTASVTKPTLEYQSTRNEMYAEYVNQLKNFRIRETQGYNSWCAGYTMSALLNATYNTNRYNAESVMRYLHPNLRGHDFQFTGLTSNEMLRFGRSQGRNTQYLNRMTSYNEVDQLTTNNQGIAVLGKRVESSDGIHAGHAMAVAGNAKVNNGQKVILIWNPWDNGLMTQDAHSNIIPVSNGDHYEWYASIYGY |
| Enzyme Length | 395 |
| Uniprot Accession Number | Q5HKF6 |
| Absorption | |
| Active Site | ACT_SITE 245; /evidence=ECO:0000255|PROSITE-ProRule:PRU10089; ACT_SITE 341; /evidence=ECO:0000255|PROSITE-ProRule:PRU10089; ACT_SITE 362; /evidence=ECO:0000255|PROSITE-ProRule:PRU10089 |
| Activity Regulation | |
| 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 (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Propeptide (1); Signal peptide (1); Site (1) |
| Keywords | Cell wall;Hydrolase;Protease;Reference proteome;Secreted;Signal;Thiol protease;Virulence;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, cell wall. Secreted {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: Proteolytically cleaved. {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..30; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 44,701 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |