Modular design of the Enterococcus hirae muramidase-2 and Streptococcus faecalis autolysin.
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.
Centre d'Ingénierie des Protéines, Université de Liège, Belgium.
B
B
Joris
S
S
Englebert
C P
CP
Chu
R
R
Kariyama
L
L
Daneo-Moore
G D
GD
Shockman
J M
JM
Ghuysen
D000595:Amino Acid Sequence; D016983:Enterococcus / Q000201:enzymology / Q000235:genetics*; D013293:Enterococcus faecalis / Q000201:enzymology / Q000235:genetics*; D008969:Molecular Sequence Data; D009113:Muramidase / Q000235:genetics*; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000235:genetics*; D011487:Protein Conformation; D012689:Sequence Homology, Nucleic Acid
D009113:Muramidase; D009238:N-Acetylmuramoyl-L-alanine Amidase