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COG3926 and COG5526: A tale of two new lysozyme‐like protein families
Author(s) -
Pei Jimin,
Grishin Nick V.
Publication year - 2005
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.051656805
Subject(s) - lysozyme , lytic cycle , lysin , bacteriophage , peptidoglycan , biology , computational biology , protein domain , transmembrane domain , sequence analysis , protein family , function (biology) , binding domain , protein structure , peptide sequence , biochemistry , gene , genetics , binding site , escherichia coli , virus
We have identified two new lysozyme‐like protein families by using a combination of sequence similarity searches, domain architecture analysis, and structural predictions. First, the P5 protein from bacteriophage ϕ8, which belongs to COG3926 and Pfam family DUF847, is predicted to have a new lysozyme‐like domain. This assignment is consistent with the lytic function of P5 proteins observed in several related double‐stranded RNA bacteriophages. Domain architecture analysis reveals two lysozyme‐associated transmembrane modules (LATM1 and LATM2) in a few COG3926/DUF847 members. LATM2 is also present in two proteins containing a peptidoglycan binding domain (PGB) and an N‐terminal region that corresponds to COG5526 with uncharacterized function. Second, structure prediction and sequence analysis suggest that COG5526 represents another new lysozyme‐like family. Our analysis offers fold and active‐site assignments for COG3926/DUF847 and COG5526. The predicted enzymatic activity is consistent with an experimental study on the zliS gene product from Zymomonas mobilis , suggesting that bacterial COG3926/DUF847 members might be activators of macromolecular secretion.