| IED ID | IndEnz0002016213 |
| Enzyme Type ID | protease016213 |
| Protein Name |
Prepilin leader peptidase/N-methyltransferase Includes: Leader peptidase EC 3.4.23.43 Prepilin peptidase ; N-methyltransferase EC 2.1.1.- |
| Gene Name | pilD |
| Organism | Legionella pneumophila |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Legionellales Legionellaceae Legionella Legionella pneumophila |
| Enzyme Sequence | MINALIINYPWFMYLVVGLFSLAVGSLLNVIIYRLPIILQEEWKEQCCELFHFEQRKEKIKLNLFLPRSFCPHCKAMVKAWQNIPLLAILVLRGRCYQCDSPFSIRYPFVETLTTVLSLYASWHFGFTIQLLFALLAIWILISLVFIDLDHQLLPDSLTLGLLWIGLIANTQNVFVSLDVAVLSCAGAYLALWLFINLFYLMTCKVCMGHGDFKLFAAFGAWLGWMYLPIILLISSITGAIIGLIYLKINGKSRDTAIPFGPFLCISGLIAMFWGDSIINWYIGYWM |
| Enzyme Length | 287 |
| Uniprot Accession Number | O68433 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=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.; EC=3.4.23.43; Evidence={ECO:0000250|UniProtKB:P22610}; |
| DNA Binding | |
| EC Number | 3.4.23.43; 2.1.1.- |
| Enzyme Function | FUNCTION: Plays an essential role in type IV pili and type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha-amino group of the newly exposed N-terminal phenylalanine. {ECO:0000250|UniProtKB:P22610}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Metal binding (4); Transmembrane (6) |
| Keywords | Cell inner membrane;Cell membrane;Hydrolase;Membrane;Metal-binding;Methyltransferase;Multifunctional enzyme;Protease;S-adenosyl-L-methionine;Transferase;Transmembrane;Transmembrane helix;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250|UniProtKB:P22610}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P22610}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 32,850 |
| Kinetics | |
| Metal Binding | METAL 71; /note=Zinc; /evidence=ECO:0000250|UniProtKB:P22610; METAL 74; /note=Zinc; /evidence=ECO:0000250|UniProtKB:P22610; METAL 96; /note=Zinc; /evidence=ECO:0000250|UniProtKB:P22610; METAL 99; /note=Zinc; /evidence=ECO:0000250|UniProtKB:P22610 |
| Rhea ID | |
| Cross Reference Brenda |