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ENZYME entry: EC

Accepted Name
prepilin peptidase.
Reaction catalysed
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
  • Many species of bacteria carry pili on their cell surfaces.
  • These are virulence determinants in pathogenic strains, and are assembled biosynthetically from type IV prepilin subunits.
  • Before assembly, the prepilin molecules require proteolytic processing, which is done by the prepilin peptidase.
  • Prepilin peptidase and its homologs play a central role not only in type IV pilus biogenesis but also in transport of macromolecules across cell membranes.
  • Although both peptide-bond hydrolysis and N-methylation are catalyzed by the same molecule, the methylation can be inhibited without affecting peptidase activity, and it is believed that the enzyme has two separate catalytic sites.
  • Belongs to peptidase family A24.
PRIAM enzyme-specific profiles3.4.23.43
KEGG Ligand Database for Enzyme Nomenclature3.4.23.43
IUBMB Enzyme Nomenclature3.4.23.43
MEDLINEFind literature relating to
Rhea expert-curated reactions3.4.23.43
P45794, LEP4_AERHY;  A2T195, LEP4_AERS4;  P0C423, LEP4_AERSA;  
P31711, LEP4_DICCH;  Q46525, LEP4_DICNO;  P25960, LEP4_ECOLI;  
P44620, LEP4_HAEIN;  P15754, LEP4_KLEPN;  O68433, LEP4_LEGPN;  
O30387, LEP4_MYXXD;  P33566, LEP4_NEIGO;  P31712, LEP4_PECCC;  
P22610, LEP4_PSEAE;  P36642, LEP4_PSEPU;  Q9ZEL6, LEP4_STUST;  
P72640, LEP4_SYNY3;  A5F385, LEP4_VIBC3;  P0C6D9, LEP4_VIBCH;  
Q56740, LEP4_VIBVU;  Q56763, LEP4_XANCP;  E3PJ89, PPPA_ECOH1;  

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