| IED ID | IndEnz0002009751 |
| Enzyme Type ID | protease009751 |
| Protein Name |
Staphopain A EC 3.4.22.48 Staphylococcal cysteine proteinase A Staphylopain A |
| Gene Name | sspP scpA |
| Organism | Staphylococcus aureus |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Staphylococcaceae Staphylococcus Staphylococcus aureus |
| Enzyme Sequence | MKRNFPKLIALSLIFSLSITPIANAESNSNIKAKDKRHVQVNVEDKSVPTDVRNLAQKDYLSYVTSLDKIYNKEKASYTLGEPFKIYKFNKKSDGNYYFPVLNTEGNIDYIVTISPKVTKDSSSSSKYTINVSSFLSKALNEYKDQQITILTNSKGYYVVTQNHKAKLVLKTPRLEDKKAKKTESIPTGNNVTQLKQKASVTMPTSQFKSNNYTYNEQYVNKLENFKIRETQGNNGWCAGYTMSALLNATYNTNKYHAEAVMRFLHPNLQGQQFQFTGLTPREMIYFEQTQGRSPQLLNRMTTYNEVDNLTKNNKGIAILGSRVESRNGMHAGHAMAVVGNAKLNNGQEVIIIWNPWDNGFMTQDAKNNVIPVSNGDHYQWYSSIYGY |
| Enzyme Length | 388 |
| Uniprot Accession Number | P81297 |
| 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. Also inactivated by heavy metal ions such as Hg(2+) or Ag(+), iodoacetamide, E-64 and human plasma. {ECO:0000269|PubMed:3422637}. |
| 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 (PubMed:3422637, PubMed:23235402). Proteolytic cleavage of surfactant protein A impairs bacterial phagocytosis by neutrophils while CXCR2 degradation blocks neutrophil activation and chemotaxis (PubMed:3422637, PubMed:23235402). Additionally, promotes vascular leakage by activating the plasma kallikerin/kinin system, resulting in hypotension (PubMed:15897280). {ECO:0000269|PubMed:15897280, ECO:0000269|PubMed:23235402, ECO:0000269|PubMed:3422637}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5 for elastin hydrolysis. {ECO:0000269|PubMed:3422637}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (9); Chain (1); Helix (5); Propeptide (1); Sequence conflict (1); Signal peptide (1); Site (1) |
| Keywords | 3D-structure;Direct protein sequencing;Hydrolase;Protease;Secreted;Signal;Thiol protease;Virulence;Zymogen |
| Interact With | |
| Induction | INDUCTION: Expression occurs in a growth phase-dependent manner with optimal expression at post-exponential phase. Up-regulated by Agr (accessory gene regulator) and repressed by SarA (staphylococcal accessory regulator) and sigmaB factor. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22850671}. |
| Modified Residue | |
| Post Translational Modification | PTM: Cleavage leads to the activation of ScpA probably by an auto-catalytic manner. |
| Signal Peptide | SIGNAL 1..25; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1CV8; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 44,120 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.5 mM for CBZ-Phe-Leu-Glu-pNA {ECO:0000269|PubMed:3422637}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.22.48; |