| IED ID | IndEnz0002009685 |
| Enzyme Type ID | protease009685 |
| Protein Name |
Prolyl tripeptidyl peptidase PTP EC 3.4.14.12 Prolyl tripeptidyl peptidase 81.8 kDa form Prolyl tripeptidyl peptidase A Cleaved into: Prolyl tripeptidyl peptidase 75.8 kDa form |
| Gene Name | ptpA PG_1361 |
| 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 | MKKTIFQQLFLSVCALTVALPCSAQSPETSGKEFTLEQLMPGGKEFYNFYPEYVVGLQWMGDNYVFIEGDDLVFNKANGKSAQTTRFSAADLNALMPEGCKFQTTDAFPSFRTLDAGRGLVVLFTQGGLVGFDMLARKVTYLFDTNEETASLDFSPVGDRVAYVRNHNLYIARGGKLGEGMSRAIAVTIDGTETLVYGQAVHQREFGIEKGTFWSPKGSCLAFYRMDQSMVKPTPIVDYHPLEAESKPLYYPMAGTPSHHVTVGIYHLATGKTVYLQTGEPKEKFLTNLSWSPDENILYVAEVNRAQNECKVNAYDAETGRFVRTLFVETDKHYVEPLHPLTFLPGSNNQFIWQSRRDGWNHLYLYDTTGRLIRQVTKGEWEVTNFAGFDPKGTRLYFESTEASPLERHFYCIDIKGGKTKDLTPESGMHRTQLSPDGSAIIDIFQSPTVPRKVTVTNIGKGSHTLLEAKNPDTGYAMPEIRTGTIMAADGQTPLYYKLTMPLHFDPAKKYPVIVYVYGGPHAQLVTKTWRSSVGGWDIYMAQKGYAVFTVDSRGSANRGAAFEQVIHRRLGQTEMADQMCGVDFLKSQSWVDADRIGVHGWSYGGFMTTNLMLTHGDVFKVGVAGGPVIDWNRYEIMYGERYFDAPQENPEGYDAANLLKRAGDLKGRLMLIHGAIDPVVVWQHSLLFLDACVKARTYPDYYVYPSHEHNVMGPDRVHLYETITRYFTDHL |
| Enzyme Length | 732 |
| Uniprot Accession Number | Q7MUW6 |
| Absorption | |
| Active Site | ACT_SITE 603; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q12884; ACT_SITE 678; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q12884; ACT_SITE 710; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q12884 |
| Activity Regulation | ACTIVITY REGULATION: Strongly inhibited by diisopropyl fluorophosphate and Pefabloc. Weakly inhibited by 3,4-dichloroisocumarin. Not inhibited by phenylmethylsulfonyl fluoride, leupeptin, antipain or prolinal. Activated by iodoacetamide. {ECO:0000269|PubMed:10092598}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of Xaa-Xaa-Pro-|-Yaa- releasing the N-terminal tripeptide of a peptide with Pro as the third residue (position P1) and where Yaa is not proline.; EC=3.4.14.12; Evidence={ECO:0000269|PubMed:10092598}; |
| DNA Binding | |
| EC Number | 3.4.14.12 |
| Enzyme Function | FUNCTION: Serine proteinase. Releases tripeptides from the free amino terminus of proteins. Has a requirement for Pro in the P1 position, but is inactivated by Pro in the P1' position. {ECO:0000269|PubMed:10092598}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Stable for at least 12 hours at 25 or 37 degrees Celsius (at pH 7.6). {ECO:0000269|PubMed:10092598}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6-8. {ECO:0000269|PubMed:10092598}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (46); Chain (2); Helix (12); Mutagenesis (2); Signal peptide (1); Turn (8) |
| Keywords | 3D-structure;Aminopeptidase;Direct protein sequencing;Hydrolase;Protease;Reference proteome;Serine protease;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | PTM: The N-terminus is blocked. {ECO:0000269|PubMed:10092598}. |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (5) |
| Cross Reference PDB | 2D5L; 2DCM; 2EEP; 2Z3W; 2Z3Z; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 82,266 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.14.12; |