ArticleProtein science : a publication of the Protein Society2005
The P5 protein from bacteriophage phi-6 is a distant homolog of lytic transglycosylases.
Article in Protein science : a publication of the Protein Society, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed.
- Survival of Thermostable Φ6 Genotypes in Acidic, Basic, and UV Environments.bioRxiv : the preprint server for biology · 2025Article
- Discovery of potent endolysins against Pseudomonas aeruginosa and other gram-negative ESKAPE pathogens by an agar-based screening method.Scientific reports · 2025Article
- Characterization and genomic analysis of a novel halovirus infectingFrontiers in microbiology · 2022Article
- Existing Host Range Mutations Constrain Further Emergence of RNA Viruses.Journal of virology · 2019Article
- Using HHsearch to tackle proteins of unknown function: A pilot study with PH domains.Traffic (Copenhagen, Denmark) · 2016Article
- Selective pressure causes an RNA virus to trade reproductive fitness for increased structural and thermal stability of a viral enzyme.PLoS genetics · 2012Article
- HHsenser: exhaustive transitive profile search using HMM-HMM comparison.Nucleic acids research · 2006Article
- COG3926 and COG5526: a tale of two new lysozyme-like protein families.Protein science : a publication of the Protein Society · 2005Article
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2 authors.
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Abstract
Peptidases are classical objects of enzymology and structural studies. However, a few protein families with experimentally characterized proteolytic activity, but unknown catalytic mechanism and three-dimensional structures, still exist. Using comparative sequence analysis, we deduce spatial structure for one of such families, namely, U40, which contains just one P5 protein from bacteriophage phi-6. We show that this singleton sequence possesses conserved sequence motifs characteristic of lysozymes and is a distant homolog of lytic transglycosylases that cleave bacterial peptidoglycan. The structure of the P5 protein is therefore predicted to adopt the lysozyme-like fold shared by T4, lambda, C-type, G-type lysozymes, and lytic transglycosylases. Since previous biochemical experiments with P5 of phi-6 have indicated that the purified enzyme possesses endopeptidase activity and not glycosidase activity, our results point to the possibility of a newly evolved molecular function and call for further experimental characterization of this unusual P5 protein.
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