Protein Variants | Comment | Organism |
---|---|---|
H248A | mutation abrogates autophosphorylation by disrupting the phosphorylation site in the DHp domain | Escherichia coli |
H248A/N356K | mutation abrogates autophosphorylation | Escherichia coli |
additional information | engineering of covalent dimers of the cytoplasmic domains of CpxA which provide a robust experimental system for investigating cooperativity in histidine kinase autophosphorylation | Escherichia coli |
N356K | mutation abrogates autophosphorylation by disrupting the ATP-binding site in the CA domain | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
phosphoprotein | autophosphorylation of the homodimer occurs in trans. No cooperativity in autophosphorylation of CpxA is observed despite its asymmetric structures. Minor amounts of ADP generated during autophosphorylation reactions or present in ATP preparations, can produce about 50% total phosphorylation | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
CpxA | - |
Escherichia coli |