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ENZYME entry: EC 188.8.131.52
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|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 profiles||184.108.40.206|
|KEGG Ligand Database for Enzyme Nomenclature||220.127.116.11|
|IUBMB Enzyme Nomenclature||18.104.22.168|
|MEDLINE||Find literature relating to 22.214.171.124|
|P45794, LEP4_AERHY; ||A2T195, LEP4_AERS4; ||P0C423, LEP4_AERSA; |
|P15378, LEP4_BACSU; ||I1WFC0, LEP4_BURP2; ||P0DMK9, LEP4_BURPS; |
|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_PSEST; |
|P72640, LEP4_SYNY3; ||A5F385, LEP4_VIBC3; ||P0C6D9, LEP4_VIBCH; |
|Q56740, LEP4_VIBVU; ||Q56763, LEP4_XANCP; |
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entries corresponding to 3.4.23.-
entries corresponding to 3.4.-.-
entries corresponding to 3.-.-.-