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Article

FtsH, a membrane-bound ATPase, forms a complex in the cytoplasmic membrane of Escherichia coli.

The Journal of biological chemistry - 6 Oct 1995

Akiyama Y, Yoshihisa T, Ito K

Abstract excerpt

The FtsH (HflB) protein of Escherichia coli is integrated into the membrane with two N-terminally located transmembrane segments, while its large cytoplasmic domain is homologous to the AAA family of ATPases. The previous studies on dominant negative ftsH mutants raised a possibility that FtsH functions in multimeric states. We found that FtsH was eluted at fractions corresponding to a larger molecular weight...

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PMID: 7559511
DOI: 10.1074/jbc.270.40.23485

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

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FtsH, a membrane-bound ATPase, forms a complex in the cytoplasmic membrane of Escherichia coli.PMID 7559511Read ↗

Roles of the periplasmic domain of Escherichia coli FtsH (HflB) in protein interactions and activity modulation.Semantic proximity Read ↗

FtsH (HflB) is an ATP-dependent protease selectively acting on SecY and some other membrane proteins.Semantic proximity Read ↗

Involvement of FtsH in protein assembly into and through the membrane. II. Dominant mutations affecting FtsH functions.Semantic proximity Read ↗

A protease complex in the Escherichia coli plasma membrane: HflKC (HflA) forms a complex with FtsH (HflB), regulating its proteolytic activity against SecY.Semantic proximity Read ↗

A Lactococcus lactis gene encodes a membrane protein with putative ATPase activity that is homologous to the essential Escherichia coli ftsH gene product.Semantic proximity Read ↗

Roles of multimerization and membrane association in the proteolytic functions of FtsH (HflB).Semantic proximity Read ↗

Balanced biosynthesis of major membrane components through regulated degradation of the committed enzyme of lipid A biosynthesis by the AAA protease FtsH (HflB) in Escherichia coli.Semantic proximity Read ↗

Dislocation of membrane proteins in FtsH-mediated proteolysis.Semantic proximity Read ↗

A new Escherichia coli gene, fdrA, identified by suppression analysis of dominant negative FtsH mutations.Semantic proximity Read ↗

A trapping approach reveals novel substrates and physiological functions of the essential protease FtsH in Escherichia coli.Semantic proximity Read ↗

Characterization of the ftsH gene of Bacillus subtilis.Semantic proximity Read ↗

Bacillus subtilis SepF binds to the C-terminus of FtsZ.Semantic proximity Read ↗

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