Detail Information for IndEnz0002010817
IED ID IndEnz0002010817
Enzyme Type ID protease010817
Protein Name Staphopain A
EC 3.4.22.48
Staphylococcal cysteine proteinase A
Staphylopain A
Gene Name sspP scpA SA1725
Organism Staphylococcus aureus (strain N315)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Staphylococcaceae Staphylococcus Staphylococcus aureus Staphylococcus aureus (strain N315)
Enzyme Sequence MKRNFPKLIALSLIFSLSVTPIANAESNSNIKAKDKKHVQVNVEDKSVPTDVRNLAQKDYLSYVTSLDKIYNKEKASYTLGEPFKIYKFNKKSDGNYYFPVLNTEGNIDYIVTISPKITKYSSSSSKYTINVSPFLSKVLNQYKDQQITILTNSKGYYVVTQNHKAKLVLKTPRLEDKKLKKTESIPTGNNVTQLKQKASVTMPTSQFKSNNYTYNEQYINKLENFKIRETQGNNGWCAGYTMSALLNATYNTNKYHAEAVMRFLHPNLQGQRFQFTGLTPREMIYFGQTQGRSPQLLNRMTTYNEVDNLTKNNKGIAVLGSRVESRNGMHAGHAMAVVGNAKLDNGQEVIIIWNPWDNGFMTQDAKNNVIPVSNGDHYRWYSSIYGY
Enzyme Length 388
Uniprot Accession Number P65826
Absorption
Active Site ACT_SITE 238; /evidence=ECO:0000255|PROSITE-ProRule:PRU10089; ACT_SITE 334; /evidence=ECO:0000255|PROSITE-ProRule:PRU10089; ACT_SITE 355; /evidence=ECO:0000255|PROSITE-ProRule:PRU10089
Activity Regulation ACTIVITY REGULATION: Prematurely activated/folded staphopain A is inhibited by staphostatin A (ScpB), which is probably required to protect staphylococcal cytoplasmic proteins from degradation by ScpA. {ECO:0000250}.
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Broad endopeptidase action on proteins including elastin, but rather limited hydrolysis of small-molecule substrates. Assays are conveniently made with hemoglobin, casein or Z-Phe-Arg-NHMec as substrate.; EC=3.4.22.48;
DNA Binding
EC Number 3.4.22.48
Enzyme Function FUNCTION: Cysteine protease that plays an important role in the inhibition of host innate immune response. Cleaves host elastins found in connective tissues, pulmonary surfactant protein A in the lungs, and the chemokine receptor CXCR2 on leukocytes. Proteolytic cleavage of surfactant protein A impairs bacterial phagocytosis by neutrophils while CXCR2 degradation blocks neutrophil activation and chemotaxis. Additionally, promotes vascular leakage by activating the plasma kallikerin/kinin system, resulting in hypotension. {ECO:0000250|UniProtKB:P81297}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Propeptide (1); Signal peptide (1); Site (1)
Keywords Hydrolase;Protease;Secreted;Signal;Thiol protease;Virulence;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P81297}.
Modified Residue
Post Translational Modification PTM: Cleavage leads to the activation of ScpA probably by an auto-catalytic manner. {ECO:0000250}.
Signal Peptide SIGNAL 1..25; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 44,204
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda