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Article

The ClpXP ATP-dependent protease regulates flagellum synthesis in Salmonella enterica serovar typhimurium.

Journal of bacteriology - 1 Feb 2002

Tomoyasu Toshifumi, Ohkishi Tomiko, Ukyo Yoshifumi, Tokumitsu Akane, Takaya Akiko, Suzuki Masato, Sekiya Kachiko, Matsui Hidenori, Kutsukake Kazuhiro, Yamamoto Tomoko

Abstract excerpt

The ClpXP protease is a member of the ATP-dependent protease family and plays a dynamic role in the control of availability of regulatory proteins and the breakdown of abnormal and misfolded proteins. The proteolytic activity is rendered by the ClpP component, while the substrate specificity is d...

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Identifiers

PMID: 11790733
DOI: 10.1128/JB.184.3.645-653.2002
PMCID: PMC139528

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-11790733-2026-09-04.1. Manifest publication-graph-cohort-2026-09-04.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

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Research trail→

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The ClpXP ATP-dependent protease regulates flagellum synthesis in Salmonella enterica serovar typhimurium.PMID 11790733Read ↗

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FliT selectively enhances proteolysis of FlhC subunit in FlhD4C2 complex by an ATP-dependent protease, ClpXP.Semantic proximity Read ↗

Coordinated regulation of expression of Salmonella pathogenicity island 1 and flagellar type III secretion systems by ATP-dependent ClpXP protease.Semantic proximity Read ↗

Cellular levels and activity of the flagellar sigma factor FliA of Escherichia coli are controlled by FlgM-modulated proteolysis.Semantic proximity Read ↗

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Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli.Semantic proximity Read ↗

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ClpP-deletion impairs the virulence of Legionella pneumophila and the optimal translocation of effector proteins.Semantic proximity Read ↗

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