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Article

Chemotactic signaling by an Escherichia coli CheA mutant that lacks the binding domain for phosphoacceptor partners.

Journal of bacteriology - 1 May 2004

Jahreis Knut, Morrison Tom B, Garzón Andrés, Parkinson John S

Abstract excerpt

CheA is a multidomain histidine kinase for chemotaxis in Escherichia coli. CheA autophosphorylates through interaction of its N-terminal phosphorylation site domain (P1) with its central dimerization (P3) and ATP-binding (P4) domains. This activity is modulated through the C-terminal P5 domain, which couples CheA to chemoreceptor control. CheA phosphoryl groups are donated to two response regulators, CheB and...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 15090507
DOI: 10.1128/JB.186.9.2664-2672.2004
PMCID: PMC387806

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Chemotactic signaling by an Escherichia coli CheA mutant that lacks the binding domain for phosphoacceptor partners.PMID 15090507Read ↗

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