Prepilin peptidase
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.23 Aspartic endopeptidases > 3.4.23.43 prepilin peptidase
Prepilin peptidase is an aspartic endopeptidase that processes type IV prepilin subunits before their assembly into pili, which are virulence determinants in pathogenic bacteria and also required for macromolecular transport across membranes. The same molecule catalyzes both peptide-bond hydrolysis and N-methylation, and methylation can be inhibited without affecting proteolysis. It typically cleaves a -Gly-/-Phe- bond to release an N-terminal basic peptide of 5-8 residues from type IV prepilin, then N-methylates the new N-terminal amino group using S-adenosyl-L-methionine as methyl donor. In bacteria it builds type IV pili and secretion systems. It features an aspartic-protease active site embedded in the inner membrane.
Prepilin peptidase is an aspartic endopeptidase that processes type IV prepilin subunits before their assembly into pili, which are virulence determinants in pathogenic bacteria and also required for macromolecular transport across membranes. The same molecule catalyzes both peptide-bond hydrolysis and N-methylation, and methylation can be inhibited without affecting proteolysis. It typically cleaves a -Gly-/-Phe- bond to release an N-terminal basic peptide of 5-8 residues from type IV prepilin, then N-methylates the new N-terminal amino group using S-adenosyl-L-methionine as methyl donor. In bacteria it builds type IV pili and secretion systems. It features an aspartic-protease active site embedded in the inner membrane.
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