3.4.22.B64: sortase D

This is an abbreviated version, for detailed information about sortase D, go to the full flat file.


Sortase D cleaves major pilin protein (BcpA) precursor between the threonine and the glycine residues of its LPXTG sorting signal and catalyzes formation of an amide bond between threonine of the sorting signal and lysine in the YPKN motif of another BcpA subunit. BcpA cleavage by SrtD leads to the assembly of pili. The acyl enzyme of SrtD can be viewed as an assembly platform for the capture of polymerized pili via thioester linked intermediates with the C-terminal threonine of the last pilin subunit. =


pilin-specific sortase D, pilus-associated sortase D, sortase D, sortase SrtD, SrtD


     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.B64 sortase D