ID 3.4.23.43 DE prepilin peptidase. CA Typically cleaves a -Gly-|-Phe- bond to release an N-terminal, basic CA peptide of 5-8 residues from type IV prepilin, and then N-methylates the CA new N-terminal amino group, the methyl donor being S-adenosyl-L- CA methionine. CC -!- Many species of bacteria carry pili on their cell surfaces. CC -!- These are virulence determinants in pathogenic strains, and are CC assembled biosynthetically from type IV prepilin subunits. CC -!- Before assembly, the prepilin molecules require proteolytic CC processing, which is done by the prepilin peptidase. CC -!- Prepilin peptidase and its homologs play a central role not only in CC type IV pilus biogenesis but also in transport of macromolecules CC across cell membranes. CC -!- Although both peptide-bond hydrolysis and N-methylation are catalyzed CC by the same molecule, the methylation can be inhibited without CC affecting peptidase activity, and it is believed that the enzyme has CC two separate catalytic sites. CC -!- Belongs to peptidase family A24. DR P45794, LEP4_AERHY ; A2T195, LEP4_AERS4 ; P0C423, LEP4_AERSA ; DR P15378, LEP4_BACSU ; I1WFC0, LEP4_BURP2 ; P0DMK9, LEP4_BURPS ; DR P31711, LEP4_DICCH ; Q46525, LEP4_DICNO ; P25960, LEP4_ECOLI ; DR P44620, LEP4_HAEIN ; P15754, LEP4_KLEPN ; O68433, LEP4_LEGPN ; DR O30387, LEP4_MYXXD ; P33566, LEP4_NEIGO ; P31712, LEP4_PECCC ; DR P22610, LEP4_PSEAE ; P36642, LEP4_PSEPU ; Q9ZEL6, LEP4_STUST ; DR P72640, LEP4_SYNY3 ; A5F385, LEP4_VIBC3 ; P0C6D9, LEP4_VIBCH ; DR Q56740, LEP4_VIBVU ; Q56763, LEP4_XANCP ; E3PJ89, PPPA_ECOH1 ; //