Sequence analysis of a Staphylococcus aureus gene encoding a peptidoglycan hydrolase activity.
The nucleotide (nt) sequence of a 2.0-kb NheI-XbaI DNA fragment containing a peptidoglycan hydrolase-encoding gene, lytA, tentatively identified as encoding an N-acetylmuramyl-L-alanine amidase, from Staphylococcus aureus, was determined. The nt sequencing revealed an open reading frame (ORF) of 1443 bp with a consensus ribosome-binding site located 7 nt upstream from the ATG start codon. The primary amino acid (aa) sequence deduced from the nt sequence revealed a putative protein of 481 aa residues with an Mr of 53815. Comparison of the aa sequence of the ORF with aa sequences in the GenBank data base (version 63, March 1990) revealed that the C-terminal sequence showed significant homology to the C-terminal sequence of lysostaphin from Staphylococcus simulans biovar staphylolyticus.
Department of Biological Sciences, Illinois State University, Norman 61761.
X
X
Wang
B J
BJ
Wilkinson
R K
RK
Jayaswal
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D008248:Lysostaphin / Q000235:genetics; D008969:Molecular Sequence Data; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000235:genetics* / Q000378:metabolism; D016366:Open Reading Frames; D012689:Sequence Homology, Nucleic Acid; D013211:Staphylococcus aureus / Q000201:enzymology / Q000235:genetics*
D008248:Lysostaphin; D009238:N-Acetylmuramoyl-L-alanine Amidase