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3.4.22.B64: sortase D

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

Word Map on EC 3.4.22.B64

Reaction

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. =

Synonyms

CPE0222, pilin-specific sortase D, pilus-associated sortase D, sortase D, sortase SrtD, SrtD

ECTree

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

Engineering

Engineering on EC 3.4.22.B64 - sortase D

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C207A
-
although sortase C207A is expressed at the same level as the wild-type enzyme, the mutant was unable to cleave IsdX1SS-GST substrate