EC Number | Cloned (Comment) | Organism |
---|---|---|
2.7.13.3 | gene CC_0285, recombinant expression of His-tagged wild-type enzyme, enzyme fragments, and mutant C70A enzyme in Escherichia coli strain Rosetta(DE3)pLysS | Caulobacter vibrioides |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.7.13.3 | C70A | site-directed mutagenesis | Caulobacter vibrioides |
EC Number | General Stability | Organism |
---|---|---|
2.7.13.3 | photoexcitation destabilizes the LOV-HK linker sequence | Caulobacter vibrioides |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.13.3 | ATP + protein L-histidine | Caulobacter vibrioides | - |
ADP + protein N-phospho-L-histidine | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.7.13.3 | Caulobacter vibrioides | Q9ABE3 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.7.13.3 | recombinant His-tagged wild-type enzyme, enzyme fragments, and mutant C70A enzyme from Escherichia coli strain Rosetta(DE3)pLysS by nickel affinity chromatography, ultrafiltration, and gel filtration | Caulobacter vibrioides |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.13.3 | ATP + protein L-histidine | - |
Caulobacter vibrioides | ADP + protein N-phospho-L-histidine | - |
? | |
2.7.13.3 | additional information | measurement of the enzyme's ATPase activity | Caulobacter vibrioides | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.7.13.3 | More | LovK trypsin peptide mapping | Caulobacter vibrioides |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.7.13.3 | CC_0285 | - |
Caulobacter vibrioides |
2.7.13.3 | LovK | - |
Caulobacter vibrioides |
2.7.13.3 | sensor histidine kinase | - |
Caulobacter vibrioides |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.7.13.3 | 22 | - |
assay at room temperature | Caulobacter vibrioides |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.7.13.3 | 7.6 | - |
assay at | Caulobacter vibrioides |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
2.7.13.3 | ATP | - |
Caulobacter vibrioides | |
2.7.13.3 | FMN | bound to the LovK histidine kinase | Caulobacter vibrioides | |
2.7.13.3 | additional information | no FAD | Caulobacter vibrioides |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.7.13.3 | additional information | effect of the nonconserved flanking sequence on the signaling lifetime of LovK, the effects of structure outside the LOV core on its signaling lifetime do not combine in a simple, additive way. Kinetics of recovery from the adduct state depend not only on the buffer environment but also on the structural context in which the LOV domain is contained. Full-length LovK (residues 1-368) has a long recovery, with a half-life of 2 h, the isolated LOV core (residues 25-138) recovers more quickly, with a half-life of 37 min. LovK (25-163), which contains the LOV core and the nonconserved linker sequence at its C-terminus, has a recovery half-life of 28 min. A construct containing the LOV core and the nonconserved N-terminal flanking sequence, LovK(1-138), has a half-life of only 2 min, but this N-terminal region has not a general rate enhancement effect. LovK(1-163), a construct with fully intact N- and C-termini (but missing the kinase domain), is slower to recover than either LovK(25-138), LovK(1-138), or LovK(25-163) | Caulobacter vibrioides |