Detail Information for IndEnz0002003452
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