Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Deletion analysis of MotA and MotB, components of the force-generating unit in the flagellar motor of Salmonella.

Molecular microbiology - 1 Sept 1998

Muramoto K, Macnab R M

Abstract excerpt

MotA and MotB are cytoplasmic membrane proteins that form the force-generating unit of the flagellar motor in Salmonella typhimurium and many other bacteria. Many missense mutations in both proteins are known to cause slow motor rotation (slow-motile phenotype) or no rotation at all (non-motile or paralysed phenotype). However, large stretches of sequence in the cytoplasmic regions of MotA and in the periplasmic...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Bacterial Proteins
Share to Genetic Complementation Test

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

Share to Membrane Proteins

Share to Molecular Sequence Data

Share to Mutagenesis, Site-Directed

Share to Phenotype

Share to Sequence Deletion

Source

Identifiers

PMID: 9767587
DOI: 10.1046/j.1365-2958.1998.00998.x

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

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Deletion analysis of MotA and MotB, components of the force-generating unit in the flagellar motor of Salmonella.PMID 9767587Read ↗

Mutant MotB proteins in Escherichia coli.Semantic proximity Read ↗

Mot protein assembly into the bacterial flagellum: a model based on mutational analysis of the motB gene.Semantic proximity Read ↗

Mutations in the MotA protein of Escherichia coli reveal domains critical for proton conduction.Semantic proximity Read ↗

Tryptophan-scanning mutagenesis of MotB, an integral membrane protein essential for flagellar rotation in Escherichia coli.Semantic proximity Read ↗

The role of a cytoplasmic loop of MotA in load-dependent assembly and disassembly dynamics of the MotA/B stator complex in the bacterial flagellar motor.Semantic proximity Read ↗

The swimming defect caused by the absence of the transcriptional regulator LdtR in Sinorhizobium meliloti is restored by mutations in the motility genes motA and motS.Semantic proximity Read ↗

Conformational change in the stator of the bacterial flagellar motor.Semantic proximity Read ↗

Analysis of the motA flagellar motor gene from Rhodobacter sphaeroides, a bacterium with a unidirectional, stop-start flagellum.Semantic proximity Read ↗

Extragenic suppression of motA missense mutations of Escherichia coli.Semantic proximity Read ↗

GFP Fusion to the N-Terminus of MotB Affects the Proton Channel Activity of the Bacterial Flagellar Motor in Salmonella.Semantic proximity Read ↗

Function of proline residues of MotA in torque generation by the flagellar motor of Escherichia coli.Semantic proximity Read ↗

Motility protein interactions in the bacterial flagellar motor.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.