| IED ID | IndEnz0002009569 |
| Enzyme Type ID | protease009569 |
| Protein Name |
Glutamyl endopeptidase EC 3.4.21.19 Endoproteinase Glu-C Staphylococcal serine proteinase V8 protease V8 proteinase |
| Gene Name | sspA SAOUHSC_00988 |
| 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 | MKGKFLKVSSLFVATLTTATLVSSPAANALSSKAMDNHPQQTQSSKQQTPKIQKGGNLKPLEQREHANVILPNNDRHQITDTTNGHYAPVTYIQVEAPTGTFIASGVVVGKDTLLTNKHVVDATHGDPHALKAFPSAINQDNYPNGGFTAEQITKYSGEGDLAIVKFSPNEQNKHIGEVVKPATMSNNAETQVNQNITVTGYPGDKPVATMWESKGKITYLKGEAMQYDLSTTGGNSGSPVFNEKNEVIGIHWGGVPNEFNGAVFINENVRNFLKQNIEDIHFANDDQPNNPDNPDNPNNPDNPNNPDEPNNPDNPNNPDNPDNGDNNNSDNPDAA |
| Enzyme Length | 336 |
| Uniprot Accession Number | Q2FZL2 |
| Absorption | |
| Active Site | ACT_SITE 119; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10083; ACT_SITE 161; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10083; ACT_SITE 237; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10083 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Glu-|-Xaa, Asp-|-Xaa.; EC=3.4.21.19; Evidence={ECO:0000255|PROSITE-ProRule:PRU10083}; |
| DNA Binding | |
| EC Number | 3.4.21.19 |
| Enzyme Function | FUNCTION: Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. It is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. May also protect bacteria against host defense mechanism by cleaving the immunoglobulin classes IgG, IgA and IgM. May be involved in the stability of secreted lipases. {ECO:0000269|PubMed:11119502, ECO:0000269|PubMed:11447146, ECO:0000269|PubMed:12207024, ECO:0000269|PubMed:14702415}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Compositional bias (3); Propeptide (1); Region (3); Repeat (11); Signal peptide (1); Site (1) |
| Keywords | Direct protein sequencing;Hydrolase;Protease;Reference proteome;Repeat;Secreted;Serine protease;Signal;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 SspA. Up-regulated by Agr (accessory gene regulator) and repressed by sigmaB factor and SarA. {ECO:0000269|PubMed:12117932, ECO:0000269|PubMed:14702415}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: Proteolytically cleaved by aureolysin (aur). This cleavage leads to the activation of SspA. |
| Signal Peptide | SIGNAL 1..29; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 36,326 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.19;3.4.24.29; |