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GpV Apex motif
This entry represents a short motif found at the C-terminus of Phage gpV proteins. These proteins act as a spike for piercing the host membrane. The apex motif contains a conserved HXH motif that coordinates an iron ion [1]. [1]. 22325780. Phage pierces the host cell membrane with the iron-loaded spike. Browning C, Shneider MM, Bowman VD, Schwarzer D, Leiman PG;. Structure. 2012;20:326-339. (from Pfam)
phage baseplate assembly protein V
Family of bacterial and phage baseplate assembly proteins responsible for forming the small spike at the end of the tail or bacterial pathogenic needle-shaft [1]. This entry represents the OB fold part of the structure. This structure contains an unusual extra beta hairpin that forms the foundation of the spike protein's beta helix [3]. [1]. 7483254. Bacteriophage P2: genes involved in baseplate assembly. Haggard-Ljungquist E, Jacobsen E, Rishovd S, Six EW, Nilssen O, Sunshine MG, Lindqvist BH, Kim KJ, Barreiro V, Koonin EV, et al.;. Virology 1995;213:109-121. [2]. 24381728. The rise of the Type VI secretion system. Filloux A;. F1000Prime Rep. 2013;5:52. [3]. 22325780. Phage pierces the host cell membrane with the iron-loaded spike. Browning C, Shneider MM, Bowman VD, Schwarzer D, Leiman PG;. Structure. 2012;20:326-339. (from Pfam)
phage baseplate assembly protein V forms the small spikes on the baseplate that plug the end of the tube before DNA ejection and form a channel perforating the host membrane during ejection
This HMM describes a family of phage (and bacteriocin) proteins related to the phage P2 V gene product, which forms the small spike at the tip of the tail. Homologs in general are annotated as baseplate assembly protein V. At least one member is encoded within a region of Pectobacterium carotovorum (Erwinia carotovora) described as a bacteriocin, a phage tail-derived module able to kill bacteria closely related to the host strain.
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