Penicillin-binding proteins (PBPs) are most commonly associated with binding to and inactivating b-lactam antibiotics. PBPs also participate in the final steps of the biosynthesis of the peptidoglycan layer and thus contribute to bacterial cell stability. ...
An integral outer-membrane protein containing eight membrane-embedded β-strands and four "loop" regions that are exposed to extracellular milieu. Belongs to a family of gram-negative outer membrane proteins embodied by E. coli OmpX. Some members of this protein family, namely Yersinia enterolitica Ail and Salmonella typhimurium Rck. ...
Rck belongs to a family of five homologous OMP proteins characterized in Salmonella (Rck and PagC), Escherichia coli (Lom), Yersinia enterocolitica (Ail) and Enterobacter cloacae (OmpX). ...
Streptococcal surface protein, no long repeats, C-terminal a proline-rich region adopts the conformation of a left-handed polyproline II (PPII) helix, an extended and solvent-exposed structure. ...