3.4.22.71	evolution	the enzyme is a member of the sortase cysteine transpeptidase family. Members of this enzyme superfamily are widely distributed in Gram-positive bacteria that frequently utilize multiple sortases to elaborate their peptidoglycan, and the family members have a conserved active site His-Cys-Arg triad that joins a sorting signal located at the C-terminus of their protein substrate to an amino nucleophile located on the cell surface	732174	
3.4.22.71	additional information	analysis of the substrate binding structure of the enzyme using SrtB-NPQT complexes, by computational modeling, molecular dynamics simulations, and targeted amino acid mutagenesis revealing that the backbone amide of Glu224 and the side chain of Arg233 form an oxyanion hole in sortase B that stabilizes high energy tetrahedral catalytic intermediates. A highly conserved threonine residue within the bound sorting signal substrate facilitates construction of the oxyanion hole by stabilizing the position of the active site arginine residue via hydrogen bonding	732174	
3.4.22.71	physiological function	sortase attaches hemoproteins to the cell wall	718136	
3.4.22.71	physiological function	sortase cysteine transpeptidases covalently attach proteins to the bacterial cell wall or assemble fiber-like pili that promote bacterial adhesion	732174	
3.4.22.71	physiological function	SrtB has dual functions, anchoring AbpA to the cell wall and processing AbpA into a ladder profile. Streptococci adapted to the oral environment rich in salivary amylase display a sortase/adhesion substrate system	-, 755438	
3.4.22.71	physiological function	the class B sortase is involved in pilus assembly	-, 718269