Mur1, a Streptococcus thermophilus peptidoglycan hydrolase devoid of a specific cell wall binding domain.
The gene encoding Mur1, a Streptococcus thermophilus peptidoglycan hydrolase, was cloned by homology with acmA, the Lactococcus lactis major autolysin gene. Mur1 is a 24.7-kDa protein endowed with a putative signal peptide. Sequence analysis evidenced that Mur1 encompasses exactly the AcmA region containing the catalytic domain, but lacks the one containing amino acid repeats involved in cell wall binding. Mur1 appears to be expressed and cell-associated in S. thermophilus, as revealed by immunoblot analysis. These results suggest that the cell wall attachment mode of Mur1 differs from that of most peptidoglycan hydrolases described so far.
Husson-Kao
C
C
Unité de Biochemie et Structure des Protéines, INRA, Jouy-en-Josas, France.
Mengaud
J
J
Benbadis
L
L
Chapot-Chartier
M P
MP
D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D001483:Base Sequence; D015153:Blotting, Western; D003001:Cloning, Molecular; D016384:Consensus Sequence; D004591:Electrophoresis, Polyacrylamide Gel; D005798:Genes, Bacterial; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009113:Muramidase / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification*; D016415:Sequence Alignment; D013291:Streptococcus / Q000201:enzymology* / Q000235:genetics
D001426:Bacterial Proteins; C410402:Mur1 protein, Streptococcus thermophilus; D009113:Muramidase