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ENZYME

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ENZYME entry: EC 3.4.23.43

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
Comment(s)
  • 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.
Cross-references
BRENDA3.4.23.43
EC2PDB3.4.23.43
ExplorEnz3.4.23.43
PRIAM enzyme-specific profiles3.4.23.43
KEGG Ligand Database for Enzyme Nomenclature3.4.23.43
IUBMB Enzyme Nomenclature3.4.23.43
IntEnz3.4.23.43
MEDLINEFind literature relating to 3.4.23.43
MetaCyc3.4.23.43
Rhea expert-curated reactions3.4.23.43
UniProtKB/Swiss-Prot
P45794, LEP4_AERHYA2T195, LEP4_AERS4P0C423, LEP4_AERSA
P15378, LEP4_BACSUI1WFC0, LEP4_BURP2P0DMK9, LEP4_BURPS
P31711, LEP4_DICCHQ46525, LEP4_DICNOP25960, LEP4_ECOLI
P44620, LEP4_HAEINP15754, LEP4_KLEPNO68433, LEP4_LEGPN
O30387, LEP4_MYXXDP33566, LEP4_NEIGOP31712, LEP4_PECCC
P22610, LEP4_PSEAEP36642, LEP4_PSEPUQ9ZEL6, LEP4_STUST
P72640, LEP4_SYNY3A5F385, LEP4_VIBC3P0C6D9, LEP4_VIBCH
Q56740, LEP4_VIBVUQ56763, LEP4_XANCPE3PJ89, PPPA_ECOH1

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.4.23.-
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