Literature summary for 2.7.13.3 extracted from

Bouillet, S.; Wu, T.; Chen, S.; Stock, A.M.; Gao, R.
Structural asymmetry does not indicate hemiphosphorylation in the bacterial histidine kinase CpxA (2020), J. Biol. Chem., 295, 8106-8117 .

Search for more literature for 2.7.13.3

Protein Variants

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

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Posttranslational Modification

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

Synonyms	Comment	Organism
CpxA	-	Escherichia coli

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)