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Links from Protein

Items: 8

1.

Phage spike trimer

Bacteriophages penetrate the host cell membrane using their tail to inject genetic material into the host [1]. In this penetration process, they use central spike domain located beneath their baseplate [2]. The spike domain folds as a trimeric iron-binding structure [1]. This entry contains three copies of the repeat unit. [1]. 21821878. The host-binding domain of the P2 phage tail spike reveals a trimeric iron-binding structure. Yamashita E, Nakagawa A, Takahashi J, Tsunoda K, Yamada S, Takeda S;. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011;67:837-841. [2]. 22922659. Crystal structure of the C-terminal domain of Mu phage central spike and functions of bound calcium ion. Harada K, Yamashita E, Nakagawa A, Miyafusa T, Tsumoto K, Ueno T, Toyama Y, Takeda S;. Biochim Biophys Acta. 2013;1834:284-291. (from Pfam)

Date:
2024-10-16
Family Accession:
NF037093.5
Method:
HMM
2.

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)

Date:
2024-10-16
Family Accession:
NF016595.5
Method:
HMM
3.
new record, indexing in progress
Family Accession:
4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.

phage baseplate assembly protein V

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

Date:
2019-09-11
Family Accession:
10008608
Method:
Sparcle
8.

phage baseplate assembly protein V

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.

GO Terms:
Molecular Function:
structural molecule activity (GO:0005198)
Biological Process:
virion assembly (GO:0019068)
Cellular Component:
virion component (GO:0044423)
Date:
2021-05-12
Family Accession:
TIGR01644.1
Method:
HMM
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