ArticleJournal of bacteriology2003
The VirB4 family of proposed traffic nucleoside triphosphatases: common motifs in plasmid RP4 TrbE are essential for conjugation and phage adsorption.
Article in Journal of bacteriology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
43 citing papers in PubMed, 72 citations in OpenAlex.
- The cryo-EM structure of bacteriophage PRR1 and its role in conjugation inhibition.Journal of virology · 2026Article
- Suppressing Transfer of Antibiotic Resistance by a Small RNA Virus.bioRxiv : the preprint server for biology · 2026Article
- Roles of the components of theFuture microbiology · 2024Review
- Characterization of ConE, the VirB4 Homolog of the Integrative and Conjugative Element ICEJournal of bacteriology · 2023Article
- Genomic insight into the integrative conjugative elements from ICEFrontiers in veterinary science · 2022Article
- VirB4- and VirD4-Like ATPases, Components of a Putative Type 4C Secretion System in Clostridioides difficile.Journal of bacteriology · 2021Article
- Structural bases for F plasmid conjugation and F pilus biogenesis inProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Bacteria-Killing Type IV Secretion Systems.Frontiers in microbiology · 2019Review
- Structure of a VirD4 coupling protein bound to a VirB type IV secretion machinery.The EMBO journal · 2017Article
- Prevalence of Flp Pili-Encoding Plasmids inFrontiers in microbiology · 2017Article
- Article
- Article
- Mechanism and structure of the bacterial type IV secretion systems.Biochimica et biophysica acta · 2014Review
- Common requirement for the relaxosome of plasmid R1 in multiple activities of the conjugative type IV secretion system.Journal of bacteriology · 2014Article
- A genetic approach to the development of new therapeutic phages to fight pseudomonas aeruginosa in wound infections.Viruses · 2012Review
- Genome characterization and population genetic structure of the zoonotic pathogen, Streptococcus canis.BMC microbiology · 2012Article
- The hexameric structure of a conjugative VirB4 protein ATPase provides new insights for a functional and phylogenetic relationship with DNA translocases.The Journal of biological chemistry · 2012Article
- Enterococcus faecalis PrgJ, a VirB4-like ATPase, mediates pCF10 conjugative transfer through substrate binding.Journal of bacteriology · 2012Article
- Structure of the VirB4 ATPase, alone and bound to the core complex of a type IV secretion system.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteins of the VirB4 family are encoded by conjugative plasmids and by type IV secretion systems, which specify macromolecule export machineries related to conjugation systems. The central feature of VirB4 proteins is a nucleotide binding site. In this study, we asked whether members of the VirB4 protein family have similarities in their primary structures and whether these proteins hydrolyze nucleotides. A multiple-sequence alignment of 19 members of the VirB4 protein family revealed striking overall similarities. We defined four common motifs and one conserved domain. One member of this protein family, TrbE of plasmid RP4, was genetically characterized by site-directed mutagenesis. Most mutations in trbE resulted in complete loss of its activities, which eliminated pilus production, propagation of plasmid-specific phages, and DNA transfer ability in Escherichia coli. Biochemical studies of a soluble derivative of RP4 TrbE and of the full-length homologous protein R388 TrwK revealed that the purified forms of these members of the VirB4 protein family do not hydrolyze ATP or GTP and behave as monomers in solution.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.