C-terminal WxL domain mediates cell wall binding in Enterococcus faecalis and other gram-positive bacteria.

ABSTRACT: Analysis of the genome sequence of Enterococcus faecalis clinical isolate V583 revealed novel genes encoding surface proteins. Twenty-seven of these proteins, annotated as having unknown functions, possess a putative N-terminal signal peptide and a conserved C-terminal region characterized by a novel conserved domain designated WxL. Proteins having similar characteristics were also detected in other low-G+C-content gram-positive bacteria. We hypothesized that the WxL region might be a determinant of bacterial cell location. This hypothesis was tested by generating protein fusions between the C-terminal regions of two WxL proteins in E. faecalis and a nuclease reporter protein. We demonstrated that the C-terminal regions of both proteins conferred a cell surface localization to the reporter

SUBMITTER: Brinster S 

PROVIDER: S-EPMC1797349 | biostudies-literature | 2007 Feb

REPOSITORIES: biostudies-literature