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 |