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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 |
BRENDA | 3.4.23.43 |
EC2PDB | 3.4.23.43 |
ExplorEnz | 3.4.23.43 |
PRIAM enzyme-specific profiles | 3.4.23.43 |
KEGG Ligand Database for Enzyme Nomenclature | 3.4.23.43 |
IUBMB Enzyme Nomenclature | 3.4.23.43 |
IntEnz | 3.4.23.43 |
MEDLINE | Find literature relating to 3.4.23.43 |
MetaCyc | 3.4.23.43 |
Rhea expert-curated reactions | 3.4.23.43 |
UniProtKB/Swiss-Prot |
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_STUST; |
P72640, LEP4_SYNY3; | A5F385, LEP4_VIBC3; | P0C6D9, LEP4_VIBCH; |
Q56740, LEP4_VIBVU; | Q56763, LEP4_XANCP; | E3PJ89, PPPA_ECOH1; |
|
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ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 3.4.23.-
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