Prepilin peptidase

Prepilin peptidase (EC 3.4.23.43) is an enzyme found in Type IV filament systems responsible for the maturation of the pilin.^[1][2] This enzyme catalyses the following chemical reaction

Typically cleaves a -Gly-Phe- bond to release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N-methylates the new N-terminal amino group, the methyl donor being S-adenosyl-L-methionine.

Prepilin peptidase
Identifiers
EC no.	3.4.23.43
CAS no.	202833-59-8
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Search PMC articles PubMed articles NCBI proteins

Type IV leader peptidase family (A24)
Identifiers
Symbol	Peptidase_A24
Pfam	PF01478
InterPro	IPR000045
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

This enzyme is present on the surface of many species of bacteria. All known enzymes with this activity are of the MEROPS family A24.