| IED ID | IndEnz0002007328 |
| Enzyme Type ID | protease007328 |
| Protein Name |
Archaeal Lon protease EC 3.4.21.- ATP-dependent protease La homolog |
| Gene Name | MJ1417 |
| Organism | Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) |
| Taxonomic Lineage | cellular organisms Archaea Euryarchaeota Methanomada group Methanococci Methanococcales Methanocaldococcaceae Methanocaldococcus Methanocaldococcus jannaschii Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) |
| Enzyme Sequence | MFSIKFKTTEELPEPSPRLIDQVIGQEEAVKIVLSAVKNKRNVILLGDPGVGKSMIVKAVGEILSDFGEFTPYYVIAKPNLKNMERPIVEVIDGEYKEDSKDMPKLDFKAPSSTTLLLIMIGAILLSEYLLKYLPQNYLLAAVTITALIVLIFGFVIILTSIMGASRASMPNNLNPMDLKPVLLYECKKRPLVRASAYNVTRLLGDIKHCPLGGRPPLGTPPHKRIILGAIHEAHRGILYVDEIKTMPLEVQDYILTALQDKQLPISGRNPNSSGATVETNPIPCDFILIMSGNMDDVYNLRAPLLDRIDYKIVLKNKMDNTLENRDKLLQFIVQEIKNNNLNPMTYDGCCEVVRIAQYLAGSKDKLTLRLRLLANIIKMANDVAMGKDVEELLGNFDDKGEYHPETQKDKSNKVYITAEHVRKVFDTGIYSMEKQVALNYIKNFKRYKHIVPNDEPKVGVIYGLAVLGAGGIGDVTKIIVQILESKNPGTHLLNISGDIAKHSITLASALSKKLVAEKKLPLPKKDIDLNNKEIYIQFSQSYSKIDGDSATAAVCLAIISALLDIPLKQDFAITGSLDLSGNVLAIGGVNEKIEAAKRYGFKRVIIPEANMIDVIETEGIEIIPVKTLDEIVPLVFDLDNRGGAERFN |
| Enzyme Length | 649 |
| Uniprot Accession Number | Q58812 |
| Absorption | |
| Active Site | ACT_SITE 550; /evidence=ECO:0000269|PubMed:15456757; ACT_SITE 593; /evidence=ECO:0000269|PubMed:15456757 |
| 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 47..54; /note=ATP; /evidence=ECO:0000255 |
| Features | Active site (2); Beta strand (9); Chain (1); Domain (1); Helix (6); Nucleotide binding (1); Topological domain (3); Transmembrane (2); Turn (1) |
| Keywords | 3D-structure;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:0000250}; Multi-pass membrane protein {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1XHK; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 71,918 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |