| IED ID | IndEnz0002007329 |
| Enzyme Type ID | protease007329 |
| Protein Name |
Archaeal Lon protease EC 3.4.21.- ATP-dependent protease La homolog Cleaved into: Pho lon intein |
| Gene Name | PH0452 |
| Organism | Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) |
| Taxonomic Lineage | cellular organisms Archaea Euryarchaeota Thermococci Thermococcales Thermococcaceae Pyrococcus Pyrococcus horikoshii Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) |
| Enzyme Sequence | MLSGESEMDEERMDLGIEFETTEEIPVPERLIDQVIGQDHAVEVIKTAAKQRRHVLLIGEPGTGKSMLGQAMAELLPTEELEDILVFPNPEDENMPRIKTVPAGQGRKIVEEYRRKAKEQEGVRFYLLFFVFFIVAMAVFLSHGDPNTLLLGVFVILVALMVTANMRFKTQAMVPKLLVDNSGRKRAPFVDATGAHAGALLGDVRHDPFQCFSGEEVIIVEKGKDRKVVKLREFVEDALKEPSGEGMDGDIKVTYKDLRGEDVRILTKDGFVKLLYVNKREGKQKLRKIVNLDKDYWLAVTPDHKVFTSEGLKEAGEITEKDEIIRVPLVILDGPKIASTYGEDGKFDDYIRWKKYYEKTGNGYKRAAKELNIKESTLRWWTQGAKPNSLKMIEELEKLNLLPLTSEDSRLEKVAIILGALFSDGNIDRNFNTLSFISSERKAIERFVETLKELFGEFNYEIRDNHESLGKSILFRTWDRRIIRFFVALGAPVGNKTKVKLELPWWIKLKPSLFLAFMDGLYSGDGSVPRFARYEEGIKFNGTFEIAQLTDDVEKKLPFFEEIAWYLSFFGIKAKVRVDKTGDKYKVRLIFSQSIDNVLNFLEFIPISLSPAKREKFLREVESYLAAVPESSLAGRIEELREHFNRIKKGERRSFIETWEVVNVTYNVTTETGNLLANGLFVKNSGGLGTPAHLRVEPGMIHRAHKGVLFIDEIATLSLKMQQSLLTAMQEKKFPITGQSELSSGAMVRTEPVPCDFILVAAGNLDTIEKMHPALRSRIRGYGYEVYMRTTMPDTPENRRKLVQFVAQEVKKDGRIPHFTRDAVEEIVREAQRRAGRKGHLTLRLRDLGGVVRAAGDIAVRKGKKYVTREDVLEALKLAKPLEKQLADWYIERKKEYQVIRVEGGEIGRVNGLAIIGEQSGIVLPIEAIVAPAASKEEGKIIVTGKLGEIAKEAVLNVSAIIKRYKGEDISKYDIHVQFLQTYEGVEGDSASISVATAVISALEEIPVRQDVAMTGSLSVRGEVLPVGGVTPKIEAAIEAGIKTVIIPKSNEKDVFLSPDKRKKIKIIPVERIDEVLEVALVESEKKRELIKRVRESLPLWMEETPSGETLHEHKGGATLPLEESKA |
| Enzyme Length | 1127 |
| Uniprot Accession Number | O58221 |
| Absorption | |
| Active Site | ACT_SITE 990; /evidence=ECO:0000250; ACT_SITE 1033; /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 (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 59..66; /note=ATP; /evidence=ECO:0000255 |
| Features | Active site (2); Chain (3); Compositional bias (1); Domain (2); Nucleotide binding (1); Region (1); Topological domain (2); Transmembrane (2) |
| Keywords | ATP-binding;Autocatalytic cleavage;Cell membrane;Endonuclease;Hydrolase;Intron homing;Membrane;Nuclease;Nucleotide-binding;Protease;Protein splicing;Serine protease;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | PTM: This protein undergoes a protein self splicing that involves a post-translational excision of the intervening region (intein) followed by peptide ligation. {ECO:0000305}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 126,992 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |