Proceedings of the National Academy of Sciences · 1995 · 302 citations · 18 references
Life SciencesMicrobiologyMolecular BiologyEnzymologyMedical MicrobiologyMicrobial GeneticsEnzyme DiscoveryEnzyme-substrate RecognitionAmino AcidsBacterial ProteasesEnrichment BrothLytic EnzymesMicrobial Extracellular EnzymesOpen Reading Frame IdentificationOpen Reading Frame LengthProteolytic Processing Analysis
The Tn551 insertion site of the autolysis-deficient Staphylococcus aureus mutant RUSAL2 was cloned and used to identify the autolysis gene atl in the parent strain, RN450. The open reading frame for atl was 3768 bp in length, encoding a deduced protein of 1256 amino acids and molecular size of 137,381 Da. The atl gene product is a bifunctional protein that has an amidase domain and an endo-beta-N-acetylglucosaminidase domain which must undergo proteolytic processing to generate the two extracellular lytic enzymes found in the culture broth of S. aureus.
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