| IED ID | IndEnz0002007521 |
| Enzyme Type ID | protease007521 |
| Protein Name |
Prepilin leader peptidase/N-methyltransferase Protein PilD Protein secretion protein XCPA Includes: Leader peptidase EC 3.4.23.43 Prepilin peptidase ; N-methyltransferase EC 2.1.1.- |
| Gene Name | pilD xcpA PA4528 |
| Organism | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pseudomonadales Pseudomonadaceae Pseudomonas Pseudomonas aeruginosa group Pseudomonas aeruginosa Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
| Enzyme Sequence | MPLLDYLASHPLAFVLCTILLGLLVGSFLNVVVHRLPKMMERNWKAEAREALGLEPEPKQATYNLVLPNSACPRCGHEIRPWENIPLVSYLALGGKCSSCKAAIGKRYPLVELATALLSGYVAWHFGFTWQAGAMLLLTWGLLAMSLIDADHQLLPDVLVLPLLWLGLIANHFGLFASLDDALFGAVFGYLSLWSVFWLFKLVTGKEGMGYGDFKLLAMLGAWGGWQILPLTILLSSLVGAILGVIMLRLRNAESGTPIPFGPYLAIAGWIALLWGDQITRTYLQFAGFK |
| Enzyme Length | 290 |
| Uniprot Accession Number | P22610 |
| 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:0000269|PubMed:23255525, ECO:0000269|PubMed:8096341}; |
| 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 (PubMed:8096341, PubMed:8340405, PubMed:23255525). Substrates include proteins required for pilus biogenesis PilE, PilV, PilW, and PilX as well as some components of the type II general secretory apparatus GspG, GspH, GspI and GspJ (PubMed:8331069). {ECO:0000269|PubMed:23255525, ECO:0000269|PubMed:8096341, ECO:0000269|PubMed:8331069, ECO:0000269|PubMed:8340405}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Metal binding (4); Mutagenesis (6); Natural variant (1); Transmembrane (6) |
| Keywords | Cell inner membrane;Cell membrane;Hydrolase;Membrane;Metal-binding;Methyltransferase;Multifunctional enzyme;Protease;Reference proteome;S-adenosyl-L-methionine;Transferase;Transmembrane;Transmembrane helix;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:8331069}; Multi-pass membrane protein. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 31,870 |
| Kinetics | |
| Metal Binding | METAL 72; /note=Zinc; /evidence=ECO:0000305|PubMed:23255525; METAL 75; /note=Zinc; /evidence=ECO:0000305|PubMed:23255525; METAL 97; /note=Zinc; /evidence=ECO:0000305|PubMed:23255525; METAL 100; /note=Zinc; /evidence=ECO:0000305|PubMed:23255525 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.23.43; |