| IED ID | IndEnz0002006831 |
| Enzyme Type ID | protease006831 |
| Protein Name |
Archaeal Lon protease EC 3.4.21.- ATP-dependent protease La homolog |
| Gene Name | Ta1081 |
| Organism | Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) |
| Taxonomic Lineage | cellular organisms Archaea Candidatus Thermoplasmatota Thermoplasmata Thermoplasmatales Thermoplasmataceae Thermoplasma Thermoplasma acidophilum Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) |
| Enzyme Sequence | MEENIESVEEWVNKLDIETTKDIHVPKLLFDQVIGQDQAGEIVKKAALQRRHVILIGEPGTGKSMLAQSMVDFLPKSELEDILVFPNPEDPNKPKIKTVPAGKGKEIVRQYQIKAEREKRDRSRSIMFVIFSVVLLGIIAAIVLRSITLIFFAIMAAAFLYMAMAFNPVIRNERAMVPKLLVSHNPNDKPPFVDSTGAHSGALLGDVRHDPFQSGGLETPAHERVEAGNIHKAHKGVLFIDEINLLRPEDQQAILTALQEKKYPISGQSERSAGAMVQTEPVPCDFVLVAAGNYDAIRNMHPALRSRIRGYGYEVVVNDYMDDNDENRRKLVQFIAQEVEKDKKIPHFDKSAIIEVIKEAQKRSGRRNKLTLRLRELGGLVRVAGDIAVSQKKTVVTAADVIAAKNLAKPLEQQIADRSIEIKKIYKTFRTEGSVVGMVNGLAVVGADTGMSEYTGVVLPIVAEVTPAEHKGAGNIIATGKLGDIAKEAVLNVSAVFKKLTGKDISNMDIHIQFVGTYEGVEGDSASVSIATAVISAIENIPVDQSVAMTGSLSVRGDVLPVGGVTAKVEAAIEAGLNKVIVPELNYSDIILDADHVNKIEIIPAKTIEDVLRVALVNSPEKEKLFDRISNLINAAKIIKPQRPATPATTRAGNNAA |
| Enzyme Length | 657 |
| Uniprot Accession Number | Q9HJ89 |
| Absorption | |
| Active Site | ACT_SITE 525; /evidence=ECO:0000250; ACT_SITE 568; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Degrades polypeptides processively. {ECO:0000269|PubMed:15358558, ECO:0000269|PubMed:15560777}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 57..64; /note=ATP; /evidence=ECO:0000255 |
| Features | Active site (2); Chain (1); Domain (1); Mutagenesis (8); Nucleotide binding (1); Topological domain (3); Transmembrane (2) |
| Keywords | ATP-binding;Cell membrane;Hydrolase;Membrane;Nucleotide-binding;Protease;Reference proteome;Serine protease;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 71,601 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.196 mM for ATP {ECO:0000269|PubMed:15560777}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.53; |