Recombinant Enterobacteria phage PRD1 Transglycosylase (VII)
Description
Introduction to Recombinant Enterobacteria Phage PRD1 Transglycosylase (VII)
Recombinant Enterobacteria phage PRD1 Transglycosylase (VII), commonly associated with protein P7, is a crucial enzyme encoded by the Enterobacteria phage PRD1. This enzyme plays a significant role in the phage's life cycle, particularly in facilitating the entry of phage DNA into host cells by breaking down peptidoglycan layers. The transglycosylase activity of protein P7 is essential for creating localized openings in the bacterial cell wall, allowing the phage genome to penetrate the host cell.
Structure and Function of Protein P7
Protein P7 is a structural component of the PRD1 virion and contains a conserved transglycosylase domain in its amino-terminal half . This domain is responsible for the enzymatic activity that degrades peptidoglycan, a key component of bacterial cell walls. The presence of this domain allows protein P7 to facilitate the entry of the phage genome into the host cell by creating temporary breaches in the cell wall .
Role in Phage Infection
During the infection process, protein P7 works in conjunction with other phage proteins to ensure efficient entry of the phage genome. The absence of protein P7 has been shown to delay phage DNA replication and host cell lysis, highlighting its critical role in the early stages of infection . Protein P7 likely forms a heteromultimeric complex with protein P14, which is also encoded by gene VII of PRD1, and this complex is involved in the initial steps of the phage life cycle .
Table 1: Key Features of Protein P7
Table 2: Comparison with Other Lytic Enzymes
References The Lytic Enzyme of Bacteriophage PRD1 Is Associated with the Phage Membrane. Bacteriophage PRD1 DNA entry uses a viral membrane. Exploitation of a Bacterium-Encoded Lytic Transglycosylase by a Human Oral Lytic Phage To Facilitate Infection. Tectiviridae | ICTV. DP01012 - Protein P16 - DisProt. Characterization, complete genome sequencing, and CRISPR/Cas9 system-based decontamination of a novel Escherichia coli phage TR1 from fermentation substrates. The Unique Vertex of Bacterial Virus PRD1 Is Connected to the Viral Membrane. XVII - Protein P17 - Enterobacteria phage PRD1 ... - UniProt. Peer review in Discovery and characterization of a prevalent human gut bacterial enzyme sufficient for the inactivation of a family of plant toxins.
Product Specs
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Target Background
Recombinant Enterobacteria phage PRD1 Transglycosylase (VII) is a component of the phage ejection machinery functioning as an exolysin. This muralytic protein is involved in host peptidoglycan digestion, a crucial step for viral DNA entry. It lacks intrinsic enzymatic activity but is essential for DNA injection during membrane transformation. It participates in forming the membrane tail tube connecting the virus interior with the host cytosol, and is critical for viral infectivity.
KEGG: vg:1260931
