IED ID | IndEnz0002015769 |
Enzyme Type ID | protease015769 |
Protein Name |
Lon protease 2 EC 3.4.21.53 ATP-dependent protease La 2 |
Gene Name | lon2 lonB ysxF BSU28210 |
Organism | Bacillus subtilis (strain 168) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168) |
Enzyme Sequence | MSWTGIALFIQLFFGIIIGLYFWNLLKNQRTQKVTIDKESKKEMEQLRKMRAISLSEPLSEKVRPKSFKDIVGQEDGIKALKAALCGPNPQHVIVYGPPGVGKTAAARLVLEEAKKHKQSPFKEQAVFVELDATTARFDERGIADPLIGSVHDPIYQGAGAMGQAGIPQPKQGAVTHAHGGVLFIDEIGELHPIQMNKMLKVLEDRKVFLDSAYYSEENTQIPNHIHDIFQNGLPADFRLIGATTRMPNEIPPAIRSRCLEVFFRELEKDELKTVAKTAADKIEKNISEEGLDLLTSYTRNGREAVNMIQIAAGMAVTENRKDITIEDIEWVIHSSQLTPKHEQKIGVEPQVGIVNGLAVYGPNSGSLLEIEVSVTAAQDKGSINITGIAEEESIGSQSKSIRRKSMAKGSVENVLTVLRTMGMKPSDYDIHINFPGGIPIDGPSAGIAMAAGIFSAIHKIPIDNTVAMTGEISLNGLVKPIGGVIPKIKAAKQSGAKKVIIPYENQQAILKQIDGIEIIAVKTFQEVLDEILVNPPTEQKPFHIEINKESV |
Enzyme Length | 552 |
Uniprot Accession Number | P42425 |
Absorption | |
Active Site | ACT_SITE 445; /evidence=ECO:0000255|PROSITE-ProRule:PRU10087; ACT_SITE 488; /evidence=ECO:0000255|PROSITE-ProRule:PRU10087 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53; Evidence={ECO:0000255|PROSITE-ProRule:PRU10087}; |
DNA Binding | |
EC Number | 3.4.21.53 |
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. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner (By similarity). {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | NP_BIND 97..104; /note=ATP; /evidence=ECO:0000250 |
Features | Active site (2); Chain (1); Domain (1); Nucleotide binding (1); Sequence conflict (1) |
Keywords | ATP-binding;Cytoplasm;Hydrolase;Nucleotide-binding;Protease;Reference proteome;Serine protease;Stress response |
Interact With | |
Induction | INDUCTION: By heat shock. {ECO:0000250}. |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 60,429 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |