Sortase D
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.22 Cysteine endopeptidases > 3.4.22.B64 sortase D
Sortase D is a bacterial transpeptidase found in viruses and cellular organisms. It cleaves the major pilin BcpA precursor between Thr and Gly of its LPXTG sorting signal and catalyzes an amide bond between the Thr of the signal and a Lys in the YPKN motif of another BcpA subunit; the acyl-enzyme intermediate acts as an assembly platform for pilus capture. In Gram-positive bacteria it builds pili. It features a cysteine-transpeptidase fold.
Sortase D is a bacterial transpeptidase found in viruses and cellular organisms. It cleaves the major pilin BcpA precursor between Thr and Gly of its LPXTG sorting signal and catalyzes an amide bond between the Thr of the signal and a Lys in the YPKN motif of another BcpA subunit; the acyl-enzyme intermediate acts as an assembly platform for pilus capture. In Gram-positive bacteria it builds pili. It features a cysteine-transpeptidase fold.
References:
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