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

Mutants of Streptococcus faecalis sensitive to alkaline pH lack Na(+)-ATPase.

Journal of bacteriology - 1 Apr 1990

Kakinuma Y, Igarashi K

Abstract excerpt

Alkali-sensitive mutants which grow at pH 7.5 but not at pH 9.5 in Na(+)-rich media were isolated from Streptococcus faecalis ATCC 9790. One of the mutants, designated Nak1, lacked activities of both Na(+)-stimulated ATPase and KtrII (active K+ uptake by sodium ATPase). These activities were restored in a spontaneous revertant designated Nak1R. Active sodium extrusion from Nak1 was observed at pH 7.0, which...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphatases
Share to Cation Transport Proteins
Share to Cell Membrane

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

Share to Enterococcus faecalis

Share to Hydrogen-Ion Concentration

Share to Kinetics

Share to Mutation

Share to Sodium

Source

Open in PubMed Open full text

Identifiers

PMID: 2138604
DOI: 10.1128/jb.172.4.1732-1735.1990
PMCID: PMC208663

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

Mutants of Streptococcus faecalis sensitive to alkaline pH lack Na(+)-ATPase.PMID 2138604Read ↗

The Na+/H+ antiporter of alkaliphilic Bacillus sp.Semantic proximity Read ↗

Three putative cation/proton antiporters from the soda lake alkaliphile Alkalimonas amylolytica N10 complement an alkali-sensitive Escherichia coli mutant.Semantic proximity Read ↗

Redundant potassium transporter systems guarantee the survival of Enterococcus faecalis under stress conditionsSemantic proximity Read ↗

Isolation and properties of Enterococcus hirae mutants defective in the potassium/proton antiport system.Semantic proximity Read ↗

Ionic selectivity and thermal adaptations within the voltage-gated sodium channel family of alkaliphilic Bacillus.Semantic proximity Read ↗

A Bacillus flagellar motor that can use both Na+ and K+ as a coupling ion is converted by a single mutation to use only Na+.Semantic proximity Read ↗

Isolation of Enterococcus hirae mutant deficient in low-affinity potassium uptake at alkaline pH.Semantic proximity Read ↗

Deletion analysis of the subunit genes of V-type Na+-ATPase from Enterococcus hirae.Semantic proximity Read ↗

Identification of membrane domains of the Na+/H+ antiporter (NhaA) protein from Helicobacter pylori required for ion transport and pH sensing.Semantic proximity Read ↗

Escherichia coli is able to grow with negligible sodium ion extrusion activity at alkaline pH.Semantic proximity Read ↗

Identification and characterization of functional residues in a Na+/H+ antiporter (NhaA) from Escherichia coli by random mutagenesis.Semantic proximity Read ↗

NhaA Na+/H+ antiporter mutants that hardly react to the membrane potential.Semantic proximity Read ↗

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