3.4.22.B64: sortase D

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For detailed information about sortase D, go to the full flat file.

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

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12	Organism
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General Information

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General Information on EC 3.4.22.B64 - sortase D

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

physiological function

Bacillus cereus

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sortase D links major pilin protein BcpA and minor tip pilin BcpB together. The enzyme cleaves related sorting signals within BcpA (LPVTG) and BcpB (IPNTG), and catalyses a transpeptidation that joins the threonine residues in each signal to the side-chain of Lys162 in BcpA (located within a pilin motif)

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