Activating Compound | Comment | Organism | Structure |
---|---|---|---|
ATP | activates the enzyme activity | Escherichia coli | |
DNA | activates the enzyme activity | Escherichia coli | |
additional information | the enzyme activity of Lon can be stimulated by the presence of unfolded proteins (e.g. apomyoglobin, glucagon, and alpha-casein) as well as inorganic polyphosphate accumulated during amino acid starvation | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
K371E/K376E/R379E | site-directed mutagenesis, mutant demonstrates significantly reduced DNA binding capabilities compared to wild-type enzyme. The Lon mutant does not restore cell length in the lon-/- strain, cells remained filamentous | Escherichia coli |
additional information | generation of mutant LonDELTANP lacking the ATP domain. Deletion of Lon's ATPase domain abrogates interactions with DNA. The DNA-binding defect of Lon protease affects TrfA proteolysis. And the Lon mutants are defective in proper cellular localization, most probably due to their impaired ability to form a nucleoprotein complex | Escherichia coli |
R306E/K308E/K310E/K311E | site-directed mutagenesis, the mutant demonstrates significantly reduced DNA binding capabilities compared to wild-type enzyme. The Lon mutant does not restore cell length in the lon-/- strain, cells remained filamentous | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
alpha-casein + H2O | Escherichia coli | - |
? | - |
? | |
TrfA + H2O | Escherichia coli | - |
? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
alpha-casein + H2O | - |
Escherichia coli | ? | - |
? | |
TrfA + H2O | - |
Escherichia coli | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
hexamer | - |
Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
EcLon | - |
Escherichia coli |
EcLon protease | - |
Escherichia coli |
lon | - |
Escherichia coli |
lon protease | - |
Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | required, protein degradation by Lon is dependent on energy obtained from ATP hydrolysis, modelng of the structure of hexameric ATPase domain of EcLon protease using the comparative modeling approach, overview | Escherichia coli |
General Information | Comment | Organism |
---|---|---|
malfunction | deletion of Lon's ATPase domain abrogates interactions with DNA. Substitution of positively charged amino acids in this domain in full-length Lon with residues conferring a net negative charge disrupts binding of Lon to DNA. These changes also affect the degradation of nucleic acid binding protein substrates of Lon, intracellular localization of Lon, and cell morphology. The DNA-binding defect of Lon protease affects plasmid replication initiator protein TrfA proteolysis. And the Lon mutants are defective in proper cellular localization, most probably due to their impaired ability to form a nucleoprotein complex. The phenotype of the DNA binding-defective Lon mutants is similar to that observed for Lon-deficient strains | Escherichia coli |
physiological function | Lon-DNA interactions are essential for Lon activity in cell division control. The ability of Lon to bind DNA is determined by its ATPase domain. This binding is required for processing protein substrates in nucleoprotein complexes, and Lon may help regulate DNA replication in response to growth conditions | Escherichia coli |