Disease relevance of ECs4606

• The UhpA protein is required for expression of the sugar phosphate transporter UhpT in Escherichia coli and is regulated by phosphate transfer from the transmembrane UhpBC sensor kinase complex [1].

High impact information on ECs4606

• Binding to the -64 element exhibited positive cooperativity and was stimulated severalfold by phosphorylation of UhpA, whereas extension to the downstream region was more strongly affected by phosphorylation [2].
• The consensus sequences for the high affinity UhpA-binding sites in the -64 element and for the downstream, low affinity sites are proposed [2].
• Purified UhpA was phosphorylated by acetyl phosphate in a reaction that was dependent on Mg2+ and on the presence of aspartate 54, the site of phosphorylation in homologous response regulators [2].
• Inorganic phosphate interfered with glucose 6-phosphate-dependent, UhpBC-mediated, as well as pyruvate-mediated activation of UhpA [3].
• Together with the cytoplasmic response regulator UhpA, they constitute a typical two-component regulatory system based on His-to-Asp phosphoryl transfer [3].

Chemical compound and disease context of ECs4606

• The histidine kinase domain of UhpB inhibits UhpA action at the Escherichia coli uhpT promoter [4].

Biological context of ECs4606

• These proteins are thought to regulate the phosphorylation of the transcription activator, UhpA [2].
• Amino acid sequence comparisons showed that UhpA was homologous to a family of bacterial regulatory proteins, some of which act as transcriptional activators (OmpR, PhoB, NtrC, and DctD) [5].
• The interference phenotype shown by UhpB in excess of UhpC appears to include the binding and sequestration of UhpA [4].
• In vivo titration of transcriptional activator UhpA by the intact or mutant promoters on multicopy plasmids identified the -64 element as the UhpA-binding site [6].
• Transcription activation by UhpA is stimulated by the catabolite gene activator protein (CAP)-cyclic AMP complex and depends on the C-terminal domains of the RNA polymerase RpoA and RpoD subunits [7].

Associations of ECs4606 with chemical compounds

• UhpA activation could be made independent of transmembrane signaling when (Delta)uhpBC cells were grown on pyruvate [3].
• Transmembrane induction of uhpT expression by external glucose 6-phosphate is positively regulated by the promoter-specific activator protein UhpA and the global regulator catabolite gene activator protein (CAP) [8].
• The iron chelate FeBABE [iron (S)-1-(p-bromoacetamidobenzyl) EDTA] was covalently attached to engineered cysteine residues near the DNA-binding region in UhpA [7].
• Like UhpA as a response regulator of a bacterial two-component regulatory system, ORF2 contained a helix-turn-helix DNA-binding domain at its COOH-terminal portion and an Asp residue (Asp-54) probably to be phosphorylated at its NH2-terminal portion [9].
• To examine the possible roles of the two sets of UhpA-binding sites, a series of insertion and deletion mutations were introduced at the boundary between them, as suggested from the positions that were protected by UhpA against hydroxyl radical cleavage [10].

Analytical, diagnostic and therapeutic context of ECs4606

• The two halves of the -64 inverted repeat did not contribute equally to promoter function and did not have to be intact for UhpA titration [6].

References