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Links from Protein

Items: 7

1.

tail fiber domain-containing protein

This is the very C-terminal, chaperone, domain of the bacteriophage protein endosialidase. It releases itself, via the serine-lysine dyad at the N-terminus, from the remainder of the end-tail-spike. Cleavage occurs after the threonine which is the final residue of the End-tail-spike family, Pfam:PF12219. The endosialidase protein forms homotrimeric molecules in bacteriophages [1]. The catalytic dyad allows this portion of the molecule to be cleaved from the more N-terminal region such that the latter can fold and bind to polysialic acid in the bacterial outer envelope [1]. [1]. 17158460. Characterization of a novel intramolecular chaperone domain conserved in endosialidases and other bacteriophage tail spike and fiber proteins. Schwarzer D, Stummeyer K, Gerardy-Schahn R, Muhlenhoff M;. J Biol Chem. 2007;282:2821-2831. (from Pfam)

Date:
2024-10-16
Family Accession:
NF025253.5
Method:
HMM
2.

phage tail protein

This family is of prophage tail proteins that are probably acting as endopeptidases. (from Pfam)

Date:
2024-08-14
Family Accession:
NF018329.5
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 tail spike protein

This HMM represents the conserved N-terminal region, typically from about residue 25 to about residue 350, of a family of uncharacterized phage proteins 500 to 1700 residues in length. Member protein Gp21 of Bacillus phage SPP1 is a tail spike protein involved in binding to the receptor on the host and in DNA ejection.

GO Terms:
Molecular Function:
structural molecule activity (GO:0005198)
Biological Process:
viral process (GO:0016032)
Date:
2023-03-03
Family Accession:
TIGR01665.1
Method:
HMM
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