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Literature summary 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

Cloned(Commentary)

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

Localization

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

Organism

EC Number Organism UniProt Comment Textmining
2.7.13.1 Thermotoga maritima G4FG43
-
-
2.7.13.1 Thermotoga maritima DSM 3109 G4FG43
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.7.13.1 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)

EC Number Purification (Comment) Organism
2.7.13.1 partial Thermotoga maritima

Synonyms

EC Number Synonyms Comment Organism
2.7.13.1 histidine protein kinase
-
 Thermotoga maritima
2.7.13.1 HpkA
-
 Thermotoga maritima

General Information

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