EC Number   |
Natural Substrates |
|---|
   3.4.22.71 | IsdC + H2O |
the enzyme cleaves the C-terminal sorting signal of IsdC at the NPQTN motif and rethers the polypeptide to the pentaglycine cell wall cross-bridge. During catalysis, the active site cysteine of sortase and the cleaved substrate form an acyl intermediate, which is then resolved by the amino group of pentaglycine cross-bridges |
| 3.4.22.71 | IsdC + H2O |
the enzyme anchors the IsdC precursor with a C-terminal NPQTN motif sorting sognal, to the cell wall envelope. The sorting signal of IsdC is cleaved between threonine and asparagine of the NPQTN motif, and the carboxyl group of the thrteonine is amide-linked to the amino group of pentaglycine cross-bridges |
| 3.4.22.71 | more |
gram-positive pathogenic bacteria display proteins on their surface that play important roles during infection. In Staphylococcus aureus these surface proteins are anchored to the cell wall by two sortases, sortase A and sortaseB that recognize specific surface protein sorting signals. Sortase B plays a contributing role during the pathogenesis of staphylococcal infections |
| 3.4.22.71 | more |
anchoring of SvpA to the bacterial cell wall is specifically mediated by SrzB. The enzyme is involved in the attachment of a subset of proteins to the cell wall, most likely by recognizing an NXZTN sorting motif. SrtB-mediated anchoring can be required to anchor surface proteins involved in the adaption of this microorganism to different environmental conditions |
| 3.4.22.71 | more |
the svpA-srtB locus is regulated by iron availability, mediated by Fur |
| 3.4.22.71 | more |
surface protein IsdC and sortase B are required for heme-iron scavenging of Bacillus anthracis |
| 3.4.22.71 | SvpA + H2O |
anchoring of SvpA to the bacterial cell wall is specifically mediated by SrzB |
