IED ID | IndEnz0002010520 |
Enzyme Type ID | protease010520 |
Protein Name |
Thiol protease EC 3.4.22.- |
Gene Name | tpr PG_1055 |
Organism | Porphyromonas gingivalis (strain ATCC BAA-308 / W83) |
Taxonomic Lineage | cellular organisms Bacteria FCB group Bacteroidetes/Chlorobi group Bacteroidetes Bacteroidia Bacteroidales Porphyromonadaceae Porphyromonas Porphyromonas gingivalis Porphyromonas gingivalis (strain ATCC BAA-308 / W83) |
Enzyme Sequence | MEKKLVPQSISKERLQKLEAQATLTPQQEEAKARKIEREKARLKELNIPTESKESKDCSPAGMINPYALTEVILERPLDWSNPRTTDIVERVLGSSMQDLSKGDSVLRAGRDQNAEVKIVDSVLTKTQRGQDGLERILESFNDYDMPPEEKEEAAPKAKKAAQKLDIDDLREQALSSTTITKEISKIILPTKNLRDDNNTVHQYREVGFQSNGAHNLWDTVVQGIAGDCYMLAALSAIAWVWPALLNMDVDIMSNQDEWRLYRYFIGRSKQTYARPSGSGTSTNEILQEGYYKVPIFARSRYWFNGEYWPALFEQAYANWKFPNDSKYNAILQIGGGWPEEALCELSGDSWFTSSGKLMLSSFTDLSLLNFMKSMCYSWKTIKPMVIVTPCWEPLPPMMPGIAAYHAYTVLGYTVSNGAYYLIIRNPWGVTEPTGDGVLSKRDWVIHFDNMKWFNLSKDDGIFALRLDKVRENFWYIAYMY |
Enzyme Length | 481 |
Uniprot Accession Number | P25806 |
Absorption | |
Active Site | ACT_SITE 229; /evidence=ECO:0000250; ACT_SITE 406; /evidence=ECO:0000250; ACT_SITE 426; /evidence=ECO:0000250 |
Activity Regulation | ACTIVITY REGULATION: Inactive below 20 degrees Celsius and pH 6.0. Inhibited by divalent cations. |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.22.- |
Enzyme Function | FUNCTION: Thiol protease. Probably an important virulence factor. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (1); Domain (1); Sequence conflict (1) |
Keywords | Hydrolase;Protease;Reference proteome;Thiol protease;Virulence |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 54,991 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.4.22.B8; |