| IED ID | IndEnz0002010174 |
| Enzyme Type ID | protease010174 |
| Protein Name |
Sortase B EC 3.4.22.71 |
| Gene Name | srtB SAOUHSC_01088 |
| 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 | MRMKRFLTIVQILLVVIIIIFGYKIVQTYIEDKQERANYEKLQQKFQMLMSKHQEHVRPQFESLEKINKDIVGWIKLSGTSLNYPVLQGKTNHDYLNLDFEREHRRKGSIFMDFRNELKNLNHNTILYGHHVGDNTMFDVLEDYLKQSFYEKHKIIEFDNKYGKYQLQVFSAYKTTTKDNYIRTDFENDQDYQQFLDETKRKSVINSDVNVTVKDRIMTLSTCEDAYSETTKRIVVVAKIIKVS |
| Enzyme Length | 244 |
| Uniprot Accession Number | Q2FZE3 |
| Absorption | |
| Active Site | ACT_SITE 223; /note=Acyl-thioester intermediate; /evidence=ECO:0000305|PubMed:14725770 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by MTSET (2-(Trimethylammonium)-ethyl-methanethiosulfonate) and E64 ([n- (l-3-trans-carboxyoxirane-2-carbonyl)-l-leucyl]-amido(4-guanido)butane) (PubMed:14725770). Inhibited by coptisine (PubMed:29690584). {ECO:0000269|PubMed:14725770, ECO:0000269|PubMed:29690584}. |
| 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 NPXTN motif is cleaved between the Thr and Asn residue. The resulting threonine carboxyl end of the protein is covalently attached to a pentaglycine cross-bridge of peptidoglycan.; EC=3.4.22.71; Evidence={ECO:0000269|PubMed:24519933, ECO:0000305|PubMed:11830639, ECO:0000305|PubMed:14725770}; |
| DNA Binding | |
| EC Number | 3.4.22.71 |
| Enzyme Function | FUNCTION: Transpeptidase that anchors surface proteins to the cell wall (PubMed:11830639, PubMed:15718231, PubMed:24519933) (Probable). 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 (Probable) (PubMed:24519933). This sortase recognizes an Asn-Pro-Gln-Thr-Asn (NPQTN) motif in IsdC, which is cleaved by the sortase between the threonine and aspargine residues; may only have 1 substrate in this bacterium (Probable). May be dedicated to the process of iron acquisition during bacterial infection (Probable). {ECO:0000269|PubMed:11830639, ECO:0000269|PubMed:15718231, ECO:0000269|PubMed:24519933, ECO:0000305|PubMed:11830639, ECO:0000305|PubMed:15718231, ECO:0000305|PubMed:29690584}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (12); Chain (1); Helix (6); Mutagenesis (4); Site (1); Topological domain (2); Transmembrane (1); Turn (3) |
| Keywords | 3D-structure;Cell membrane;Hydrolase;Membrane;Reference proteome;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | INDUCTION: Not expressed in the presence of extracellular iron, repressed by fur in the presence of iron. {ECO:0000305|PubMed:11830639}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000255}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 1QWZ; 1QX6; 1QXA; 4LFD; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 29,163 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |