Modular design of the Enterococcus hirae muramidase-2 and Streptococcus faecalis autolysin

FEMS Microbiol Lett. 1992 Mar 15;70(3):257-64. doi: 10.1016/0378-1097(92)90707-u.


The mature forms of the extracellular muramidase-2 of Enterococcus hirae and Streptococcus faecalis autolysin have very similar primary structures. Each consists of an active-site-containing N-terminal domain fused to a multiple-repeat C-terminal domain. Polypeptide segments occurring at equivalent places in these two bacterial wall lytic enzymes have homologues in two phage lysozymes and in three functionally unrelated proteins, illustrating the principle that protein molecules frequently are constructed from modules that are linked in a single polypeptide chain.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Enterococcus / enzymology
  • Enterococcus / genetics*
  • Enterococcus faecalis / enzymology
  • Enterococcus faecalis / genetics*
  • Molecular Sequence Data
  • Muramidase / genetics*
  • N-Acetylmuramoyl-L-alanine Amidase / genetics*
  • Protein Conformation
  • Sequence Homology, Nucleic Acid


  • Muramidase
  • N-Acetylmuramoyl-L-alanine Amidase