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Article

Mutations that alter the kinase and phosphatase activities of the two-component sensor EnvZ.

Journal of bacteriology - 1 Sept 1998

Hsing W, Russo F D, Bernd K K, Silhavy T J

Abstract excerpt

EnvZ, a membrane receptor kinase-phosphatase, modulates porin expression in Escherichia coli in response to medium osmolarity. It shares its basic scheme of signal transduction with many other sensor-kinases, passing information from the amino-terminal, periplasmic, sensory domain via the transme...

Topics

Adenosine Triphosphate
Amino Acid Sequence
Bacterial Outer Membrane Proteins
Cell Membrane
Escherichia coli
Escherichia coli Proteins
Molecular Sequence Data
Multienzyme Complexes
Mutation
Phosphoprotein Phosphatases
Protein Binding

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Sequence Homology, Amino Acid

Source

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Identifiers

PMID: 9721293
DOI: 10.1128/JB.180.17.4538-4546.1998
PMCID: PMC107465

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9721293-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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Mutations that alter the kinase and phosphatase activities of the two-component sensor EnvZ.PMID 9721293Read ↗

Transmembrane signal transduction and osmoregulation in Escherichia coli: functional importance of the transmembrane regions of membrane-located protein kinase, EnvZ.Semantic proximity Read ↗

Cysteine-scanning analysis of the dimerization domain of EnvZ, an osmosensing histidine kinase.Semantic proximity Read ↗

Kinase activity of EnvZ, an osmoregulatory signal transducing protein of Escherichia coli.Semantic proximity Read ↗

The role of the G2 box, a conserved motif in the histidine kinase superfamily, in modulating the function of EnvZ.Semantic proximity Read ↗

A single amino acid substitution in the C terminus of OmpR alters DNA recognition and phosphorylation.Semantic proximity Read ↗

A phosphorylation site mutant of OmpR reveals different binding conformations at ompF and ompC.Semantic proximity Read ↗

Intramolecular second-site revertants to the phosphorylation site mutation in OmpR, a kinase-dependent transcriptional activator in Escherichia coli.Semantic proximity Read ↗

The inner membrane histidine kinase EnvZ senses osmolality via helix-coil transitions in the cytoplasm.Semantic proximity Read ↗

Molecular analysis of the signaling pathway between EnvZ and OmpR in Escherichia coli.Semantic proximity Read ↗

Role of His243 in the phosphatase activity of EnvZ in Escherichia coli.Semantic proximity Read ↗

Gene activation by the Escherichia coli positive regulator, OmpR. Phosphorylation-independent mechanism of activation by an OmpR mutant.Semantic proximity Read ↗

Re-examination of the role of the periplasmic domain of EnvZ in sensing of osmolarity signals in Escherichia coli.Semantic proximity Read ↗

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