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

Structural and functional studies on an FtsH inhibitor from Bacillus subtilis.

Biochimica et biophysica acta - 26 Jul 2000

Prajapati R S, Ogura T, Cutting S M

Abstract excerpt

The small 3 kDa SpoVM protein is essential for development of the spore in Bacillus subtilis. Genetic and biochemical experiments have shown that the function of SpoVM is to inhibit the proteolytic activity of FtsH during sporulation. We have used a combination of genetic and biophysical techniques to characterise the role of this small polypeptide. SpoVM was found to be widespread in Bacillus as well as in two...

Read the complete abstract on PubMed

Topics

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

Share to Bacillus subtilis
Share to Circular Dichroism
Share to Clostridium

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

Share to Mutagenesis, Site-Directed

Share to Protein Conformation

Share to Protein Structure, Secondary

Share to Sequence Homology, Amino Acid

Share to Spores

Source

Identifiers

PMID: 10913836
DOI: 10.1016/s0304-4165(00)00089-1

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

Structural and functional studies on an FtsH inhibitor from Bacillus subtilis.PMID 10913836Read ↗

The PDZ domain of the SpoIVB serine peptidase facilitates multiple functions.Semantic proximity Read ↗

The small acid-soluble proteins of Clostridioides difficile regulate sporulation in a SpoIVB2-dependent manner.Semantic proximity Read ↗

The Bacillus subtilis signaling protein SpoIVB defines a new family of serine peptidases.Semantic proximity Read ↗

The spoIIN279(ts) mutation affects the FtsA protein of Bacillus subtilis.Semantic proximity Read ↗

Identification and characterization of sporulation gene spoVS from Bacillus subtilis.Semantic proximity Read ↗

Sporulation gene spoIIB from Bacillus subtilis.Semantic proximity Read ↗

Structure and function of the Bacillus SpoIIE protein and its localization to sites of sporulation septum assembly.Semantic proximity Read ↗

The structure of bypass of forespore C, an intercompartmental signaling factor during sporulation in Bacillus.Semantic proximity Read ↗

Near-atomic resolution cryoelectron microscopy structure of the 30-fold homooligomeric SpoIIIAG channel essential to spore formation in Bacillus subtilis.Semantic proximity Read ↗

Differential requirements for conserved peptidoglycan remodeling enzymes during Clostridioides difficile spore formationSemantic proximity Read ↗

Lessons and questions from the structure of the Spo0A activation domain.Semantic proximity Read ↗

A sporulation signature protease is required for assembly of the spore surface layers, germination and host colonization in Clostridioides difficileSemantic proximity Read ↗

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