title: Streptococcus mutans murein hydrolase.
abstract: Allelic replacement of the C terminus of a Streptococcus mutans surface protein affects murein hydrolase activity. The targeted open reading frame encodes a 67-kDa protein (SmaA) with an N-terminal signal sequence and cleavage site, three 46-amino-acid (aa) direct repeats, and two 88-aa direct repeats. The identical autolytic profile was obtained using a sortase mutant (SrtA(-)).
authors.affiliation: Department of Oral Biology, Indiana University School of Dentistry, Indianapolis, 46202, USA. dcatt@iupui.edu
authors.forename: Diana M
authors.initials: DM
authors.lastname: Catt
authors.forename: Richard L
authors.initials: RL
authors.lastname: Gregory
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D008969:Molecular Sequence Data; D008970:Molecular Weight; D016254:Mutagenesis, Insertional; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000235:genetics* / Q000378:metabolism*; D016366:Open Reading Frames / Q000235:genetics; D010457:Peptidoglycan / Q000378:metabolism; D021382:Protein Sorting Signals / Q000235:genetics; D012091:Repetitive Sequences, Nucleic Acid / Q000235:genetics; D017384:Sequence Deletion; D017386:Sequence Homology, Amino Acid; D013295:Streptococcus mutans / Q000201:enzymology*
chemical_list: D001426:Bacterial Proteins; D010457:Peptidoglycan; D021382:Protein Sorting Signals; D009238:N-Acetylmuramoyl-L-alanine Amidase