The Streptococcus pneumoniae beta-galactosidase is a surface protein

The beta-galactosidase gene of Streptococcus pneumoniae, bgaA, encodes a putative 2,235-amino-acid protein with the two amino acid motifs characteristic of the glycosyl hydrolase family of proteins. In addition, an N-terminal signal sequence and a C-terminal LPXTG motif typical of surface-associated...

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Published inJournal of bacteriology Vol. 182; no. 20; pp. 5919 - 5921
Main Authors Zähner, D, Hakenbeck, R
Format Journal Article
LanguageEnglish
Published United States American Society for Microbiology 01.10.2000
SeriesNote
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Summary:The beta-galactosidase gene of Streptococcus pneumoniae, bgaA, encodes a putative 2,235-amino-acid protein with the two amino acid motifs characteristic of the glycosyl hydrolase family of proteins. In addition, an N-terminal signal sequence and a C-terminal LPXTG motif typical of surface-associated proteins of gram-positive bacteria are present. Trypsin treatment of cells resulted in solubilization of the enzyme, documenting that it is associated with the cell envelope. In order to obtain defined mutants suitable for lacZ reporter experiments, the bgaA gene was disrupted, resulting in a complete absence of endogenous beta-galactosidase activity. The results are consistent with beta-galactosidase being a surface protein that seems not to be involved in lactose metabolism but that may play a role during pathogenesis.
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Corresponding author. Mailing address: Department of Microbiology, University of Kaiserslautern, Paul Ehrlich Strasse, D-67663 Kaiserslautern, Germany. Phone: 49-631-205-2353. Fax: 49-631-205-3799. E-mail: hakenb@rhrk.uni-kl.de.
ISSN:0021-9193
1098-5530
DOI:10.1128/JB.182.20.5919-5921.2000