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. 2016 Jan 21;8(1):26. doi: 10.3390/v8010026

Figure 2.

Figure 2

(A) BlastP alignment of the C-terminal fragments of LtfA proteins from phages DT57-1/2 and DT57C. The fragment that was transmitted by recombination with plasmids (see explanations in the text) to switch host specificity is highlighted in green. The predicted autocleavage site is marked by “^” and highlighted in yellow; (B) ClustalV alignment of the regions neighboring the putative cleavage site of the LtfA and LtfB proteins of our phages and in proteins with known structures of the autocleavable C-terminal chaperone domain: Ltf of bacteriophage T5 (X69460), gp12 of Bacillus subtilis bacteriophage Ga-1 (NC_002649) and endo-sialidase of E. coli bacteriophage K1F (AJ505988). “^” indicates the predicted or experimentally determined autocleavage sites. Red highlight indicates the residues conserved in six or more out of seven aligned sequences.