| IED ID | IndEnz0002009568 |
| Enzyme Type ID | protease009568 |
| Protein Name |
Staphopain B EC 3.4.22.- Staphylococcal cysteine proteinase B Staphylopain B |
| Gene Name | sspB |
| Organism | Staphylococcus aureus |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Staphylococcaceae Staphylococcus Staphylococcus aureus |
| Enzyme Sequence | MNSSCKTRVFNIISIIMVSMLILSLGAFANNNKAKADSHSKQLEINVKSDKVPQKVKDLAQQQFAGYAKALDKQSNAKTGKYELGEAFKIYKFNGEEDNSYYYPVIKDGKIVYTLTLSPKNKDDLNKSKEDMNYSVKISNFIAKDLDQIKDKNSNITVLTDEKGFYFEEDGKVRLVKATPLANNIKEKESAKTVSPQLKQELKTTVTPTKVEENEAIQEDQVQYENTLKNFKIREQQFDNSWCAGFSMAALLNATKNTDTYNAHDIMRTLYPEVSEQDLPNCATFPNQMIEYGKSQGRDIHYQEGVPSYNQVDQLTKDNVGIMILAQSVSQNPNDPHLGHALAVVGNAKINDQEKLIYWNPWDTELSIQDADSSLLHLSFNRDYNWYGSMIGY |
| Enzyme Length | 393 |
| Uniprot Accession Number | P0C1S6 |
| Absorption | |
| Active Site | ACT_SITE 243; /evidence=ECO:0000269|PubMed:15644332; ACT_SITE 340; /evidence=ECO:0000269|PubMed:15644332; ACT_SITE 360; /evidence=ECO:0000269|PubMed:15644332 |
| Activity Regulation | ACTIVITY REGULATION: Prematurely activated/folded staphopain B is inhibited by staphostatin B (SspC), which is probably required to protect staphylococcal cytoplasmic proteins from degradation by SspB. {ECO:0000250}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.22.- |
| Enzyme Function | FUNCTION: Cysteine protease that plays an important role in the inhibition of host innate immune response. Degrades host elastin, fibrogen, fibronectin and kininogen. Blocks phagocytosis of opsonised S. aureus by neutrophils and monocytes by inducing their death in a proteolytic activity-dependent manner (PubMed:20375568, PubMed:19284294). Decreases surface expression of the 'don't eat me' signal CD31 on neutrophils (PubMed:19284294). Cleaves host galectin-3/LGALS3, thereby inhibiting the neutrophil-activating ability of the lectin (PubMed:28438975). {ECO:0000269|PubMed:19284294, ECO:0000269|PubMed:20375568, ECO:0000269|PubMed:28438975}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (20); Chain (1); Helix (10); Mutagenesis (1); Propeptide (1); Sequence conflict (7); Signal peptide (1); Site (1); Turn (3) |
| Keywords | 3D-structure;Hydrolase;Protease;Secreted;Signal;Thiol protease;Virulence;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: Proteolytically cleaved by staphylococcal serine protease (SspA). {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..36 |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 1PXV; 1X9Y; 1Y4H; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 44,576 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.22.48; |