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Literature summary for 2.7.13.1 extracted from

  • Lee, P.; Stock, A.
    Characterization of the genes and proteins of a two-component system from the hyperthermophilic bacterium Thermotoga maritima (1996), J. Bacteriol., 178, 5579-5585 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.13.1

Cloned(Commentary)

Cloned (Comment) Organism
truncated HpkA lacking the putative membrane-spanning N-terminal amino acids is expressed in Escherichia coli Thermotoga maritima

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane HpkA possesses one membrane-spanning segment located at the extreme N-terminus Thermotoga maritima 16020
-

Organism

Organism UniProt Comment Textmining
Thermotoga maritima G4FG43
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-
Thermotoga maritima DSM 3109 G4FG43
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-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein in an in vitro assay, truncated HpkA protein is autophosphorylated in the presence of ATP. Thus, the N-terminal hydrophobic region is not required for kinase activity. Phosphotransfer between truncated enzyme (HpkA) and the DNA-binding response regulator (DrrA) is demonstrated in vitro with the partially purified proteins. The phosphorylation reactions are strongly temperature dependent Thermotoga maritima

Purification (Commentary)

Purification (Comment) Organism
partial Thermotoga maritima

Synonyms

Synonyms Comment Organism
histidine protein kinase
-
 Thermotoga maritima
HpkA
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 Thermotoga maritima

General Information

General Information Comment Organism
metabolism the enzyme is part of the phosphotransfer signal transduction system Thermotoga maritima