The Erwinia Phage Phi-Ea1h Holin (EPPE-Hol) Family (TC# 1.E.58) consists of a single protein, holin of Erwinia Phage Phi-Ea1h (TC# 1.E.58.1.1), which is 119 amino acyl residues in length and exhibits a single transmembrane segment (TMS). Out of three open reading frames sequenced from bacteriophage Phi-Ea1h, the second ORF encodes this holin.[1] Kim and Geider found that no signal sequence was observed at the N-terminus of the enzyme and suggested that the holin possibly facilities the export of an which may export a lysozyme and EPS depolymerase that carries out extracellular polysaccharide (EPS)-degrading activity.[1][2]
See also
Further reading
- Reddy, Bhaskara L.; Saier Jr, Milton H. (2013). "Topological and phylogenetic analyses of bacterial holin families and superfamilies". Biochimica et Biophysica Acta (BBA) - Biomembranes. 1828 (11): 2654–2671. doi:10.1016/j.bbamem.2013.07.004. PMC 3788059. PMID 23856191.
- Saier, Milton H.; Reddy, Bhaskara L. (2015). "Holins in Bacteria, Eukaryotes, and Archaea: Multifunctional Xenologues with Potential Biotechnological and Biomedical Applications". Journal of Bacteriology. 197 (1): 7–17. doi:10.1128/JB.02046-14. PMC 4288690. PMID 25157079.
- Wang, I. N.; Smith, D. L.; Young, R. (2000). "Holins: the protein clocks of bacteriophage infections". Annual Review of Microbiology. 54: 799–825. doi:10.1146/annurev.micro.54.1.799. PMID 11018145.
References
- 1 2 Kim, W. S.; Geider, K. (2000-11-01). "Characterization of a Viral EPS-Depolymerase, a Potential Tool for Control of Fire Blight". Phytopathology. 90 (11): 1263–1268. doi:10.1094/PHYTO.2000.90.11.1263. ISSN 0031-949X. PMID 18944430.
- ↑ "1.E.58. The Erwinia Phage Phi-Ea1h Holin (EPPE-Hol) Family". TCDB. Retrieved 2016-03-29.
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