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Literature summary for 2.7.13.3 extracted from

  • Eguchi, Y.; Utsumi, R.
    Alkali metals in addition to acidic pH activate the EvgS histidine kinase sensor in Escherichia coli (2014), J. Bacteriol., 196, 3140-3149.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.13.3

Activating Compound

Activating Compound Comment Organism Structure
additional information a high concentration of alkali metals (Na+, K+) in addition to low pH is essential for the activation of histidine kinase EvgS. EvgS/EvgA is activated under mildly acidic conditions at pH 5.0-5.5. EvgS has a large periplasmic sensor region consisting of two tandem bacterial periplasmic solute-binding protein (PBPb) domains at its N-terminus. The periplasmic sensor region of EvgS is necessary for EvgS activation, and Leu152, located within the first PBPb domain, is involved in the activation. Alkali metals are perceived at the periplasmic sensor region, whereas the cytoplasmic linker domain, connecting the transmembrane region and the histidine kinase domain, is required for low-pH perception Escherichia coli

Protein Variants

Protein Variants Comment Organism
K152A site-directed mutagenesis, the mutant is expressed in the membrane at levels comparable to the wild-type EvgS strain. The mutant shows moderate activation by KCl-supplemented M9 medium, pH 5.5 Escherichia coli
K152E site-directed mutagenesis, the mutant is expressed in the membrane at levels comparable to the wild-type EvgS strain. The mutant shows strong activation by KCl-supplemented M9 medium, pH 5.5 Escherichia coli
K152F naturally occuring mutation and site-directed mutagenesis, in the mutant, EvgS activation is observed only by complementation with pBADevgS, mutation L152F leads to the desensitization of EvgS in strain KMY1. The mutant shows no activation by KCl-supplemented M9 medium, pH 5.5. The L152F mutation is found in only two Escherichia coli strains, MC4100 and DH1 Escherichia coli
K152I site-directed mutagenesis, the mutant is expressed in the membrane at levels comparable to the wild-type EvgS strain. The mutant shows strong activation by KCl-supplemented M9 medium, pH 5.5 Escherichia coli
K152R site-directed mutagenesis, the mutant is expressed in the membrane at levels comparable to the wild-type EvgS strain. The mutant shows moderate activation by KCl-supplemented M9 medium, pH 5.5 Escherichia coli
K152Y site-directed mutagenesis, the mutant is expressed in the membrane at levels comparable to the wild-type EvgS strain. The mutant shows no activation by KCl-supplemented M9 medium, pH 5.5 Escherichia coli
additional information construction of EvgS-PhoQ chimeras and activation of these chimera sensors, overview. The EvgS sensor domain is fused to the cytoplasmic region of PhoQ to examine whether it still responded to the signals. In chimera PvgS-A, the region from the N terminus to the transmembrane region of EvgS (residues 1 to 558 of EvgS) is fused to the cytoplasmic region of PhoQ (residues 215 to 486 of PhoQ) comprising the HAMP, HisKA, and HATPase_c domains, and in chimera PvgS-B, the region from the N terminus to the linker domain of EvgS (residues 1 to 710 of EvgS) is fused to the HisKA and HATPase_c domains of PhoQ (residues 267 to 486 of PhoQ) Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
cell membrane
-
 Escherichia coli
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
K+ activates Escherichia coli
Mg2+ required Escherichia coli
additional information addition of KCl, NaCl, and LiCl to M9 medium (pH 5.5) at final concentrations of 50 and 100 mM induces the transcriptional activity of ydeP but not addition of MgCl2 Escherichia coli
Na+ activates Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P30855 strains KMY1 and MG1655
-

Subunits

Subunits Comment Organism
More EvgS is a hybrid histidine kinase composed of a histidine kinase domain, receiver domain, and Hpt transmitter domain. EvgS has a large periplasmic sensor region consisting of two tandem bacterial periplasmic solute-binding protein (PBPb) domains at its N-terminus. The periplasmic sensor region of EvgS is necessary for EvgS activation, and Leu152, located within the first PBPb domain, is involved in the activation. Alkali metals are perceived at the periplasmic sensor region, whereas the cytoplasmic linker domain, connecting the transmembrane region and the histidine kinase domain, is required for low-pH perception Escherichia coli

Synonyms

Synonyms Comment Organism
EvgS
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Escherichia coli

General Information

General Information Comment Organism
additional information EvgS is a hybrid histidine kinase composed of a histidine kinase domain, receiver domain, and Hpt transmitter domain. The phosphate at the initial histidine residue in the histidine kinase domain is subsequently transferred to an aspartate residue in the receiver domain and is relayed to the second histidine residue in the Hpt domain before being transferred to the aspartate residue in EvgA Escherichia coli
physiological function two-component signal transduction systems (TCSs) in bacteria perceive environmental stress and transmit the information via phosphorelay to adjust multiple cellular functions for adaptation. The EvgS/EvgA system is a TCS that confers acid resistance to Escherichia coli cells. Activation of the EvgS sensor initiates a cascade of transcription factors, EvgA, YdeO, and GadE, which induce the expression of a large group of acid resistance genes Escherichia coli