Streptococcus mutans murein hydrolase

Diana M. Catt, Richard Gregory

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

Allelic replacement of the C terminus of a Streptococcus mutans surface protein affects murein nydrolase 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 -).

Original languageEnglish
Pages (from-to)7863-7865
Number of pages3
JournalJournal of Bacteriology
Volume187
Issue number22
DOIs
StatePublished - Nov 2005

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N-Acetylmuramoyl-L-alanine Amidase
Streptococcus mutans
Nucleic Acid Repetitive Sequences
Amino Acids
Peptidoglycan
Protein Sorting Signals
Open Reading Frames
Membrane Proteins
Proteins

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Immunology

Cite this

Streptococcus mutans murein hydrolase. / Catt, Diana M.; Gregory, Richard.

In: Journal of Bacteriology, Vol. 187, No. 22, 11.2005, p. 7863-7865.

Research output: Contribution to journalArticle

Catt, Diana M. ; Gregory, Richard. / Streptococcus mutans murein hydrolase. In: Journal of Bacteriology. 2005 ; Vol. 187, No. 22. pp. 7863-7865.
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