| IED ID | IndEnz0002015711 |
| Enzyme Type ID | protease015711 |
| Protein Name |
Archaeal Lon protease EC 3.4.21.- LonTk |
| Gene Name | lon TK1264 |
| Organism | Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1)) |
| Taxonomic Lineage | cellular organisms Archaea Euryarchaeota Thermococci Thermococcales Thermococcaceae Thermococcus Thermococcus kodakarensis Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1)) |
| Enzyme Sequence | MDEESTKERLIPREYGESLDLGIDFKTTEEIPVPEKLIDQVIGQEHAVEVIKTAANQRRHVLLIGEPGTGKSMLGQAMAELLPTENLEDILVFPNPEDENMPKIKTVPACQGRRIVENYRRKAKEQEGIKNYLLMFVIFTVILAIIMEPTATTLLMGMFVVLLSMMVLSNMRFRNTVLVPKLLVDNCGRKKAPFVDATGAHAGALLGDVRHDPFQSGGLGTPAHERVEPGMIHRAHKGVLFIDEIATLSLKMQQSLLTAMQEKKFPITGQSEMSSGAMVRTEPVPCDFILVAAGNLDTIDKMHPALRSRIRGYGYEVYMRTTMPDTIENRRKLVQFVAQEVKRDGKIPHFTREAVEEIVREAQKRAGRKGHLTLRLRDLGGIVRAAGDIAIKKGKKYVEREDVLEAMRMAKPLEKQLADWYIENKKEYQVIKTEGGEIGRVNGLAVIGEQSGIVLPIEAVVAPAASKEEGKIIVTGKLGEIAKEAVQNVSAIIKRYKGEDISRYDIHVQFLQTYEGVEGDSASISVATAVISALENIPIRQDVAMTGSLSVRGEVLPIGGATPKIEAAIEAGIKKVIIPKANEKDVFLSPDKAEKIEIYPVETIDQVLEIALQDGPEKDELLRRIREALPLYGSS |
| Enzyme Length | 635 |
| Uniprot Accession Number | Q8NKS6 |
| Absorption | |
| Active Site | ACT_SITE 521; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 564; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: ADP inhibits the peptide cleavage activity of LonTk, but the enzyme retains 57% activity in comparison to the condition with the addition of ATP. {ECO:0000269|PubMed:12057965}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Serine protease that displays ATP-independent proteolytic activity towards peptides and unfolded proteins and ATP-dependent activity for the cleavage of folded proteins. {ECO:0000269|PubMed:12057965}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 70 degrees Celsius for the ATP-independent peptide cleavage activity, and 95 degrees Celsius for ATPase activity. {ECO:0000269|PubMed:12057965}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9 for the ATP-independent peptide cleavage activity and for ATPase activity. {ECO:0000269|PubMed:12057965}; |
| Pathway | |
| nucleotide Binding | NP_BIND 65..72; /note=ATP; /evidence=ECO:0000255 |
| Features | Active site (2); Chain (1); Domain (1); Nucleotide binding (1); Topological domain (2); Transmembrane (2) |
| Keywords | ATP-binding;Cell membrane;Direct protein sequencing;Hydrolase;Magnesium;Membrane;Nucleotide-binding;Protease;Reference proteome;Serine protease;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12057965}; Multi-pass membrane protein {ECO:0000269|PubMed:12057965}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 70,258 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.53; |