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. 2020 Mar 21;8(3):447. doi: 10.3390/microorganisms8030447

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© 2020 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Amino acid sequence alignments of M4Lys with other endolysins. (A) Phylogenetic analysis of endolysins from Gram-negative bacteria phages. Each group corresponds to a different functional domain: group I, V superfamily; group II, D-alanyl-D-alanine-carboxypeptidase; group III, N-acetyl muramoyl L-alanine amidase; group IV, glycoside hydrolase family 19; group V, N-acetylmuramidase; and group VI, glycoside hydrolase family 24, respectively; (B) Amino acid sequence alignments of the M4Lys protein of phage BSPM4 with other putative lysis proteins of relevant phages including SPN19, iEPS5, FSLSP088, and Chi. Conserved and identical residues are shaded in gray and black, respectively.

Amino acid sequence alignments of M4Lys with other endolysins. (A) Phylogenetic analysis of endolysins from Gram-negative bacteria phages. Each group corresponds to a different functional domain: group I, V superfamily; group II, D-alanyl-D-alanine-carboxypeptidase; group III, N-acetyl muramoyl L-alanine amidase; group IV, glycoside hydrolase family 19; group V, N-acetylmuramidase; and group VI, glycoside hydrolase family 24, respectively; (B) Amino acid sequence alignments of the M4Lys protein of phage BSPM4 with other putative lysis proteins of relevant phages including SPN19, iEPS5, FSLSP088, and Chi. Conserved and identical residues are shaded in gray and black, respectively.