Molecular characterization and functional analysis of the major autolysin of Staphylococcus aureus 8325/4.
The gene encoding the major autolysin of Staphylococcus aureus 8325/4 has been cloned, sequenced, and insertionally inactivated. The three-domain, 137,384-Da protein has a C-terminal glucosaminidase active site and is involved in cell separation, generalized cell lysis, and release of wall material at the cell surface. Expression occurs throughout growth and is stimulated by low temperatures and in the presence of 1 M NaCl.
Foster
S J
SJ
Department of Molecular Biology and Biotechnology, University of Sheffield, United Kingdom.
D001665:Binding Sites; D002473:Cell Wall / Q000201:enzymology; D003001:Cloning, Molecular; D015964:Gene Expression Regulation, Bacterial / Q000187:drug effects; D005798:Genes, Bacterial / Q000235:genetics*; D006596:Hexosaminidases / Q000378:metabolism; D008969:Molecular Sequence Data; D009154:Mutation; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000235:genetics / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis; D015183:Restriction Mapping; D017422:Sequence Analysis, DNA; D012965:Sodium Chloride / Q000494:pharmacology; D013211:Staphylococcus aureus / Q000201:enzymology* / Q000235:genetics; D013696:Temperature
D011993:Recombinant Fusion Proteins; D012965:Sodium Chloride; D006596:Hexosaminidases; D009238:N-Acetylmuramoyl-L-alanine Amidase