Literature summary extracted from
Greenswag, A.R.; Muok, A.; Li, X.; Crane, B.R.
Conformational transitions that enable histidine kinase autophosphorylation and receptor array integration (2015), J. Mol. Biol., 427, 3890-3907.
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
2.7.13.3 |
P3P4 domain structure of Thermotoga maritima CheA, vapor diffusion method, mixing of 0.001 ml of 0.7 mM protein in 50 mM HEPES, pH 7.5, 150 mM NaCl, and 2 mM DTT, with 0.001 ml of reservoir solution containing 0.5 M ammonium sulfate, 0.1 M sodium citrate tribasic dihydrate, pH 5.6, and 1.0 M lithium sulfate monohydrate, 4°C, X-ray small angle diffraction structure determination and analysis at 3.0 A resolution, molecular replacement and modelling |
Thermotoga maritima |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
2.7.13.3 |
D449A |
site-directed mutagenesis, the mutation in the ATP-binding pocket prevents nucleotide binding |
Thermotoga maritima |
2.7.13.3 |
H405Y |
site-directed mutagenesis, the mutation abrogates the kinase activity |
Thermotoga maritima |
2.7.13.3 |
H45K |
site-directed mutagenesis, a CheAFL variant that lacks the substrate His |
Thermotoga maritima |
2.7.13.3 |
H45K/H405Y |
site-directed mutagenesis, the mutant shows reduced kinase activity compared to the wild-type |
Thermotoga maritima |
2.7.13.3 |
H45K/S492C |
site-directed mutagenesis |
Thermotoga maritima |
2.7.13.3 |
additional information |
disulfide cross-linking of mutant enzymes, overview |
Thermotoga maritima |
2.7.13.3 |
S492C |
site-directed mutagenesis |
Thermotoga maritima |
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
2.7.13.3 |
Mg2+ |
required |
Thermotoga maritima |
|
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
2.7.13.3 |
ATP + protein L-histidine |
Thermotoga maritima |
- |
ADP + protein N-phospho-L-histidine |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.7.13.3 |
Thermotoga maritima |
- |
- |
- |
Posttranslational Modification
EC Number |
Posttranslational Modification |
Comment |
Organism |
---|
2.7.13.3 |
phosphoprotein |
histidine kinase performs autophosphorylation |
Thermotoga maritima |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
2.7.13.3 |
ATP + protein L-histidine |
- |
Thermotoga maritima |
ADP + protein N-phospho-L-histidine |
- |
? |
|
2.7.13.3 |
additional information |
histidine kinase performs autophosphorylation. The His-containing substrate domain (P1) is sequestered by interactions that depend upon P1 of the adjacent subunit. Non-hydrolyzable ATP analogues (but not ATP or ADP) release P1 from the protein core (domains P3P4P5) and increase its mobility. Autophosphorylation is possible only when the subunit with a functional P4 domain trans phosphorylates a functional P1 domain of the opposing subunit |
Thermotoga maritima |
? |
- |
? |
|
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
2.7.13.3 |
CheA |
- |
Thermotoga maritima |
Temperature Optimum [°C]
EC Number |
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
---|
2.7.13.3 |
25 |
- |
assay at |
Thermotoga maritima |
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
2.7.13.3 |
7.5 |
- |
assay at |
Thermotoga maritima |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
2.7.13.3 |
ATP |
residue Ser492 resides on the ATP lid, near to the Mg2+ ion that coordinates the gamma-phosphate of ATP in the P4 active site |
Thermotoga maritima |
|
2.7.13.3 |
additional information |
non-hydrolyzable ATP analogues (but not ATP or ADP) release P1 from the protein core (domains P3P4P5) and increase its mobility |
Thermotoga maritima |
|
General Information
EC Number |
General Information |
Comment |
Organism |
---|
2.7.13.3 |
evolution |
CheA differs from sensor histidine kinases in several ways: CheA does not contain a transmembrane domain, relying instead on P5 and CheW for interaction with transmembrane components. It has the phosphorylatable His residue on a separate domain (P1) instead of the dimerization domain (P3), and it utilizes a separate docking domain (P2) for CheY. P2 is not necessary for phosphotransfer to the response regulator CheY per se but variants lacking the P2 domain (DELTAP2) exhibit a reduced phosphotransfer rate relative to full-length CheA (CheAFL) and support a lower extent of chemotaxis. The linkers between the CheA domains play important roles in CheA activity |
Thermotoga maritima |
2.7.13.3 |
physiological function |
CheA differs from sensor histidine kinases in several ways: CheA does not contain a transmembrane domain, relying instead on P5 and CheW for interaction with transmembrane components. It has the phosphorylatable His residue on a separate domain (P1) instead of the dimerization domain (P3), and it utilizes a separate docking domain (P2) for CheY. P2 is not necessary for phosphotransfer to the response regulator CheY per se but variants lacking the P2 domain (DELTAP2) exhibit a reduced phosphotransfer rate relative to full-length CheA (CheAFL) and support a lower extent of chemotaxis. The linkers between the CheA domains play important roles in CheA activity |
Thermotoga maritima |