| IED ID | IndEnz0002001527 |
| Enzyme Type ID | protease001527 |
| Protein Name |
Sortase A EC 3.4.22.70 Surface protein sorting A |
| Gene Name | srtA SAOUHSC_02834 |
| 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 | MKKWTNRLMTIAGVVLILVAAYLFAKPHIDNYLHDKDKDEKIEQYDKNVKEQASKDKKQQAKPQIPKDKSKVAGYIEIPDADIKEPVYPGPATPEQLNRGVSFAEENESLDDQNISIAGHTFIDRPNYQFTNLKAAKKGSMVYFKVGNETRKYKMTSIRDVKPTDVGVLDEQKGKDKQLTLITCDDYNEKTGVWEKRKIFVATEVK |
| Enzyme Length | 206 |
| Uniprot Accession Number | Q2FV99 |
| Absorption | |
| Active Site | ACT_SITE 120; /note="Proton donor/acceptor"; /evidence="ECO:0000305|PubMed:11371637, ECO:0000305|PubMed:11714722, ECO:0000305|PubMed:15117963, ECO:0000305|PubMed:15247224, ECO:0000305|PubMed:17518446"; ACT_SITE 184; /note="Acyl-thioester intermediate"; /evidence="ECO:0000305|PubMed:11371637, ECO:0000305|PubMed:11714722, ECO:0000305|PubMed:15117963, ECO:0000305|PubMed:15247224, ECO:0000305|PubMed:17518446" |
| Activity Regulation | ACTIVITY REGULATION: Sortase activity is regulated by monomer-homodimer equilibrium. Mutant cells with monomeric SrtA display more adhesive proteins on the cell surface and are more invasive than wild-type cells, which have majority of SrtA in dimeric form. Dimerization may suppress the enzymatic activity on cell membranes (PubMed:26129884). Stimulated by calcium ions, which promote substrate binding (PubMed:11371637, PubMed:16269411). Calcium ions bind to SrtA and modulate both the structure and dynamics of a large active site loop (PubMed:16269411). Can also be stimulated, to a lesser extent, by Mg(2+) and Mn(2+) (PubMed:11371637). Inhibited by sulfhydryl-modifying reagents (PubMed:10535938, PubMed:10446208). {ECO:0000269|PubMed:10446208, ECO:0000269|PubMed:10535938, ECO:0000269|PubMed:11371637, ECO:0000269|PubMed:16269411, ECO:0000269|PubMed:26129884}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=The enzyme catalyzes a cell wall sorting reaction in which a surface protein with a sorting signal containing a LPXTG motif is cleaved between the Thr and Gly residue. The resulting threonine carboxyl end of the protein is covalently attached to a pentaglycine cross-bridge of peptidoglycan.; EC=3.4.22.70; Evidence={ECO:0000269|PubMed:10535938, ECO:0000269|PubMed:11371637, ECO:0000269|PubMed:14503881, ECO:0000269|PubMed:14769030, ECO:0000269|PubMed:15247224, ECO:0000269|PubMed:16269411, ECO:0000269|PubMed:17518446}; |
| DNA Binding | |
| EC Number | 3.4.22.70 |
| Enzyme Function | FUNCTION: Transpeptidase that anchors surface proteins to the cell wall (PubMed:10427003, PubMed:10446208, PubMed:10535938, PubMed:11714722, PubMed:14769030, PubMed:15247224). Recognizes and modifies its substrate by proteolytic cleavage of a C-terminal sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the sortase and its substrate, which is then transferred and covalently attached to the cell wall (PubMed:10446208, PubMed:10535938, PubMed:11714722, PubMed:14769030, PubMed:15247224). This sortase recognizes a Leu-Pro-x-Thr-Gly (LPXTG) motif, which is cleaved by the sortase between the threonine and glycine residues (PubMed:10535938, PubMed:11714722, PubMed:14769030, PubMed:15247224). Utilizes lipid II as the peptidoglycan substrate for the sorting reaction (PubMed:10446208, PubMed:11856734). Responsible for the display of important virulence factors (PubMed:14769030). Important for interactions with the host and host colonization during infection (PubMed:10805806, PubMed:14769030). {ECO:0000269|PubMed:10427003, ECO:0000269|PubMed:10446208, ECO:0000269|PubMed:10535938, ECO:0000269|PubMed:10805806, ECO:0000269|PubMed:11714722, ECO:0000269|PubMed:11856734, ECO:0000269|PubMed:14769030, ECO:0000269|PubMed:15247224}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (12); Chain (1); Compositional bias (1); Helix (3); Metal binding (5); Mutagenesis (26); Region (1); Site (1); Topological domain (2); Transmembrane (1); Turn (1) |
| Keywords | 3D-structure;Cell membrane;Hydrolase;Membrane;Metal-binding;Protease;Reference proteome;Thiol protease;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26129884, ECO:0000305|PubMed:11371637}; Single-pass type II membrane protein {ECO:0000305|PubMed:11371637}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (3); X-ray crystallography (3) |
| Cross Reference PDB | 1IJA; 1T2O; 1T2P; 1T2W; 2KID; 6R1V; |
| Mapped Pubmed ID | 31724850; |
| Motif | |
| Gene Encoded By | |
| Mass | 23,541 |
| Kinetics | |
| Metal Binding | METAL 105; /note="Calcium"; /evidence="ECO:0000269|PubMed:19592495, ECO:0000305|PubMed:16269411"; METAL 108; /note="Calcium"; /evidence="ECO:0000269|PubMed:19592495, ECO:0000305|PubMed:16269411"; METAL 112; /note="Calcium"; /evidence="ECO:0000269|PubMed:19592495, ECO:0000305|PubMed:16269411"; METAL 114; /note="Calcium"; /evidence="ECO:0000269|PubMed:19592495, ECO:0000305|PubMed:16269411"; METAL 171; /note="Calcium"; /evidence="ECO:0000269|PubMed:19592495, ECO:0000305|PubMed:16269411" |
| Rhea ID | |
| Cross Reference Brenda |