| IED ID | IndEnz0002012700 |
| Enzyme Type ID | protease012700 |
| Protein Name |
Prepilin leader peptidase/N-methyltransferase Late competence protein ComC Includes: Leader peptidase EC 3.4.23.43 Prepilin peptidase ; N-methyltransferase EC 2.1.1.- |
| Gene Name | comC BSU28070 |
| Organism | Bacillus subtilis (strain 168) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168) |
| Enzyme Sequence | MLSILFIFGLILGSFYYTAGCRIPLHLSIIAPRSSCPFCRRTLTPAELIPILSFLFQKGKCKSCGHRISFMYPAAELVTACLFAAAGIRFGISLELFPAVVFISLLIIVAVTDIHFMLIPNRILIFFLPFLAAARLISPLDSWYAGLLGAAAGFLFLAVIAAITHGGVGGGDIKLFAVIGFVLGVKMLAAAFFFSVLIGALYGAAAVLTGRLAKRQPLPFAPAIAAGSILAYLYGDSIISFYIKMALG |
| Enzyme Length | 248 |
| Uniprot Accession Number | P15378 |
| 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:P25960}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Metal binding (4); Sequence conflict (2); Transmembrane (7) |
| Keywords | Cell membrane;Competence;Hydrolase;Membrane;Metal-binding;Methyltransferase;Multifunctional enzyme;Protease;Reference proteome;S-adenosyl-L-methionine;Sporulation;Transferase;Transmembrane;Transmembrane helix;Zinc |
| Interact With | |
| Induction | INDUCTION: By several proteins including Spo0A, Spo0H, Sin, AbrB, DegS, DegU, ComA, ComB and ComK. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell 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 | 26,435 |
| Kinetics | |
| Metal Binding | METAL 36; /note=Zinc; /evidence=ECO:0000250|UniProtKB:P22610; METAL 39; /note=Zinc; /evidence=ECO:0000250|UniProtKB:P22610; METAL 61; /note=Zinc; /evidence=ECO:0000250|UniProtKB:P22610; METAL 64; /note=Zinc; /evidence=ECO:0000250|UniProtKB:P22610 |
| Rhea ID | |
| Cross Reference Brenda |