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

Protein Sci. 2005 Oct;14(10):2574-81. doi: 10.1110/ps.051656805. Epub 2005 Sep 9.

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 bacteriophage phi8, 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.

Publication types

  • Comparative Study
  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / genetics
  • Cell Membrane / chemistry
  • Cell Membrane / genetics
  • Computational Biology / methods
  • Cystoviridae / enzymology*
  • Cystoviridae / genetics
  • Molecular Sequence Data
  • Multigene Family / genetics
  • Muramidase / chemistry*
  • Muramidase / genetics
  • Protein Structure, Tertiary
  • Sequence Analysis, Protein* / methods
  • Viral Proteins / chemistry*
  • Zymomonas / enzymology*
  • Zymomonas / genetics

Substances

  • Bacterial Proteins
  • Viral Proteins
  • Muramidase