Protein Family Models

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:

2024-08-14

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.

Date:

2023-03-03

tail fiber domain-containing protein similar to Enterobacteria phage long tail fiber protein p37, a structural component of the distal-half tail fiber, and to the C-terminal chaperone domain of Escherichia coli phage K1F endosialidase, a S74 family serine endopeptidase

Date:

2019-03-21