COG3926 and COG5526: A tale of two new lysozyme-like protein families

Jimin Pei, Nick V. Grishin

Research output: Contribution to journalArticle

18 Scopus citations

Abstract

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 bacterio-phage 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. Published by Cold Spring Harbor Laboratory Press.

Original languageEnglish (US)
Pages (from-to)2574-2581
Number of pages8
JournalProtein Science
Volume14
Issue number10
DOIs
StatePublished - Oct 1 2005

Keywords

  • Bacteriophage φ8
  • Lysozyme
  • Lysozyme-associated transmembrane modules
  • Macromolecular secretion
  • Structure prediction

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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