Evidence map›Paper›PMID 23913323›Full record

ArticleJournal of bacteriology2013

TraG encoded by the pIP501 type IV secretion system is a two-domain peptidoglycan-degrading enzyme essential for conjugative transfer.

Karsten Arends, Ertugrul-Kaan Celik, Ines Probst, Nikolaus Goessweiner-Mohr, Christian Fercher, Lukas Grumet, Cem Soellue, Mohammad Yaser Abajy, Tuerkan Sakinc, Melanie Broszat and 4 more

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

32 citing papers in PubMed, 56 citations in OpenAlex.

  1. Review
  2. Article
  3. The type IV secretion system ofMicrobial genomics · 2025
    Article
  4. Article
  5. Article
  6. Measure of Peptidoglycan Degradation Activity.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  7. Review
  8. Article
  9. Article
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  11. Article
  12. Article
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  14. Review
  15. Article
  16. Review
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  18. Review
  19. Structural basis of a histidine-DNA nicking/joining mechanism for gene transfer and promiscuous spread of antibiotic resistance.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  20. Article
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

14 authors at 4 institutions in 2 countries.

Karsten ArendsDepartment of Environmental Microbiology/Genetics, University of Technology Berlin, Berlin, Germany.
Ertugrul-Kaan Celik
Ines Probst
Nikolaus Goessweiner-Mohr
Christian Fercher
Lukas Grumet
Cem Soellue
Mohammad Yaser Abajy
Tuerkan Sakinc
Melanie Broszat
Katarzyna Schiwon
Guenther Koraimann
Walter Keller
Elisabeth Grohmann
University of Graz · ATTechnische Universität Berlin · DEUniversity Medical Center Freiburg · DEUniversity of Freiburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

pIP501 is a conjugative broad-host-range plasmid frequently present in nosocomial Enterococcus faecalis and Enterococcus faecium isolates. We focus here on the functional analysis of the type IV secretion gene traG, which was found to be essential for pIP501 conjugative transfer between Gram-positive bacteria. The TraG protein, which localizes to the cell envelope of E. faecalis harboring pIP501, was expressed and purified without its N-terminal transmembrane helix (TraGΔTMH) and shown to possess peptidoglycan-degrading activity. TraGΔTMH was inhibited by specific lytic transglycosylase inhibitors hexa-N-acetylchitohexaose and bulgecin A. Analysis of the TraG sequence suggested the presence of two domains which both could contribute to the observed cell wall-degrading activity: an N-terminal soluble lytic transglycosylase domain (SLT) and a C-terminal cysteine-, histidine-dependent amidohydrolases/peptidases (CHAP) domain. The protein domains were expressed separately, and both degraded peptidoglycan. A change of the conserved glutamate residue in the putative catalytic center of the SLT domain (E87) to glycine resulted in almost complete inactivity, which is consistent with this part of TraG being a predicted lytic transglycosylase. Based on our findings, we propose that TraG locally opens the peptidoglycan to facilitate insertion of the Gram-positive bacterial type IV secretion machinery into the cell envelope.

Indexed as

AcetylglucosamineBacterial ProteinsConjugation, GeneticEnterococcus faecalisEnterococcus faeciumGene DeletionGene Expression Regulation, BacterialGene Expression Regulation, EnzymologicOligosaccharidesPeptidoglycanPlasmidsProlineAcetylglucosamineBacterial Proteinsbulgecin AN-acetylchitohexaoseOligosaccharidesPeptidoglycanProline

Identifiers

PMID23913323
PMCPMC3807477
OpenAlexW2067778654

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.