| IED ID | IndEnz0002008967 |
| Enzyme Type ID | protease008967 |
| Protein Name |
Staphopain B EC 3.4.22.- Staphylococcal cysteine proteinase B Staphylopain B |
| Gene Name | sspB SAOUHSC_00987 |
| Organism | Staphylococcus aureus (strain NCTC 8325 / PS 47) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Staphylococcaceae Staphylococcus Staphylococcus aureus Staphylococcus aureus (strain NCTC 8325 / PS 47) |
| Enzyme Sequence | MNSSCKSRVFNIISIIMVSMLILSLGAFANNNKAKADSHSKQLEINVKSDKVPQKVKDLAQQQFAGYAKALDKQSNAKTGKYELGEAFKIYKFNGEEDNSYYYPVIKDGKIVYTLTLSPKNKDDLNKSKEDMNYSVKISNFIAKDLDQIKDKNSNITVLTDEKGFYFEEDGKVRLVKATPLPGNVKEKESAKTVSAKLKQELKNTVTPTKVEENEAIQEDQVQYENTLKNFKIREQQFDNSWCAGFSMAALLNATKNTDTYNAHDIMRTLYPEVSEQDLPNCATFPNQMIEYGKSQGRDIHYQEGVPSYEQVDQLTKDNVGIMILAQSVSQNPNDPHLGHALAVVGNAKINDQEKLIYWNPWDTELSIQDADSSLLHLSFNRDYNWYGSMIGY |
| Enzyme Length | 393 |
| Uniprot Accession Number | Q2FZL3 |
| Absorption | |
| Active Site | ACT_SITE 243; /evidence=ECO:0000255|PROSITE-ProRule:PRU10089; ACT_SITE 340; /evidence=ECO:0000255|PROSITE-ProRule:PRU10089; ACT_SITE 360; /evidence=ECO:0000255|PROSITE-ProRule:PRU10089 |
| 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. Also inactivated by E-64 and stimulated by EDTA. {ECO:0000269|PubMed:12207024}. |
| 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. Decreases surface expression of the 'don't eat me' signal CD31 on neutrophils. Cleaves host galectin-3/LGALS3, thereby inhibiting the neutrophil-activating ability of the lectin. {ECO:0000250|UniProtKB:P0C1S6}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Propeptide (1); Signal peptide (1); Site (1) |
| Keywords | Direct protein sequencing;Hydrolase;Protease;Reference proteome;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. Environmental conditions such as degree of aeration and salt concentration are also important in control of transcription and processing of SspB. Up-regulated by agr (accessory gene regulator) and repressed by SarA (staphylococcal accessory regulator) and sigmaB factor. {ECO:0000269|PubMed:14702415}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | PTM: Proteolytically cleaved by staphylococcal serine protease (SspA). {ECO:0000269|PubMed:11119502, ECO:0000269|PubMed:12207024}. |
| Signal Peptide | SIGNAL 1..36; /evidence=ECO:0000269|PubMed:11119502 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 44,519 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.22.48; |