Evidence map›Paper›PMID 24799078›Full record

ReviewMicrobial drug resistance (Larchmont, N.Y.)2014

Deciphering the metabolism of undecaprenyl-phosphate: the bacterial cell-wall unit carrier at the membrane frontier.

Guillaume Manat, Sophie Roure, Rodolphe Auger, Ahmed Bouhss, Hélène Barreteau, Dominique Mengin-Lecreulx, Thierry Touzé

Open access · hybridAbstract readReview
In one paragraph

Review in Microbial drug resistance (Larchmont, N.Y.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
5.8field-weighted citation impact, top 4% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

85 citing papers in PubMed, 151 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. ThemBio · 2026
    Article
  5. Review
  6. Article
  7. Article
  8. ThemBio · 2026
    Article
  9. Article
  10. Analysis of essential genes inJournal of bacteriology · 2025
    Article
  11. Article
  12. Characterization ofJournal of the American Society for Mass Spectrometry · 2025
    Article
  13. Peptidoglycan polymerase function and regulation.Microbiology and molecular biology reviews : MMBR · 2025
    Review
  14. Article
  15. Analysis of Essential Genes inbioRxiv : the preprint server for biology · 2025
    Article
  16. Review
  17. Article
  18. Lipopeptide antibiotics disrupt interactions of undecaprenyl phosphate with UptA.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  19. Review
  20. Review

25 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

Guillaume ManatLaboratoire des Enveloppes Bactériennes et Antibiotiques, IBBMC, UMR 8619 CNRS, Université Paris Sud , Orsay Cedex, France .
Sophie Roure
Rodolphe Auger
Ahmed Bouhss
Hélène Barreteau
Dominique Mengin-Lecreulx
Thierry Touzé
Université Paris-Sud · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

During the biogenesis of bacterial cell-wall polysaccharides, such as peptidoglycan, cytoplasmic synthesized precursors should be trafficked across the plasma membrane. This essential process requires a dedicated lipid, undecaprenyl-phosphate that is used as a glycan lipid carrier. The sugar is linked to the lipid carrier at the inner face of the membrane and is translocated toward the periplasm, where the glycan moiety is transferred to the growing polymer. Undecaprenyl-phosphate originates from the dephosphorylation of its precursor undecaprenyl-diphosphate, with itself generated by de novo synthesis or by recycling after the final glycan transfer. Undecaprenyl-diphosphate is de novo synthesized by the cytosolic cis-prenyltransferase undecaprenyl-diphosphate synthase, which has been structurally and mechanistically characterized in great detail highlighting the condensation process. In contrast, the next step toward the formation of the lipid carrier, the dephosphorylation step, which has been overlooked for many years, has only started revealing surprising features. In contrast to the previous step, two unrelated families of integral membrane proteins exhibit undecaprenyl-diphosphate phosphatase activity: BacA and members of the phosphatidic acid phosphatase type 2 super-family, raising the question of the significance of this multiplicity. Moreover, these enzymes establish an unexpected link between the synthesis of bacterial cell-wall polymers and other biological processes. In the present review, the current knowledge in the field of the bacterial lipid carrier, its mechanism of action, biogenesis, recycling, regulation, and future perspective works are presented.

Indexed as

Alkyl and Aryl TransferasesBiological TransportCell MembraneCell WallEscherichia coliEscherichia coli ProteinsLipid MetabolismPeptidoglycanPhosphatidate PhosphatasePhosphoric Monoester HydrolasesPolyisoprenyl PhosphatesAlkyl and Aryl TransferasesBacA protein, E coliEscherichia coli ProteinsPeptidoglycanPhosphatidate Phosphatasephosphatidic acid phosphatase type 2Phosphoric Monoester HydrolasesPolyisoprenyl Phosphatesundecaprenyl phosphateundecaprenyl pyrophosphateundecaprenyl pyrophosphate synthetase

Identifiers

PMID24799078
PMCPMC4050452
OpenAlexW2017331448

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.