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 language | English (US) |
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Pages (from-to) | 2574-2581 |
Number of pages | 8 |
Journal | Protein Science |
Volume | 14 |
Issue number | 10 |
DOIs | |
State | Published - Oct 2005 |
Keywords
- Bacteriophage φ8
- Lysozyme
- Lysozyme-associated transmembrane modules
- Macromolecular secretion
- Structure prediction
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology