IED ID | IndEnz0002016346 |
Enzyme Type ID | protease016346 |
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 | hofD hopD HI_0296 |
Organism | Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pasteurellales Pasteurellaceae Haemophilus Haemophilus influenzae Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) |
Enzyme Sequence | MIYFTMFLLGGILGIALWFYLSGFITRLQQNIYAIYVELFPQNRSPFQPHFASIQQKKCGHILRYFFSIGVGFIFLQIAFKDSIFTVWIGLTLIILWTISYLDWHYQLISTTPCLWLLTLGLFGADNNFSLLTLSESIKSAASFFIVFYVIYWLAKFYYGKEAFGRGDYWLAMALGSFIHLETLPHFLLLASVLGICFSLIHRKKKEFLPFAPFMNLSAVIIYFVKYYGY |
Enzyme Length | 230 |
Uniprot Accession Number | P44620 |
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 a role in 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. Substrates include proteins required for biogenesis of the type II general secretory apparatus. {ECO:0000250|UniProtKB:P22610}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Transmembrane (7) |
Keywords | Cell inner membrane;Cell membrane;Hydrolase;Membrane;Protease;Reference proteome;S-adenosyl-L-methionine;Transferase;Transmembrane;Transmembrane helix;Transport |
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 | 26,789 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |