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Appl Environ Microbiol, July 1998, p. 2439-2442, Vol. 64, No. 7
0099-2240/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Cytoplasmic Membrane Lipoprotein LppC of Streptococcus equisimilis Functions as an Acid Phosphatase

Horst Malke*

Institute for Molecular Biology, Jena University, D-07745 Jena, Germany

Received 6 February 1998/Accepted 1 May 1998

The function of the streptococcal cytoplasmic membrane lipoprotein, LppC, was identified with isogenic Streptococcus equisimilis H46A and Escherichia coli JM109 strain pairs differing in whether they contained [H46A and JM109(pLPP2)] or lacked (H46A lppC::pLPP10 and JM109) the functional lppC gene for comparative phosphatase determinations under acidic conditions. lppC-directed acid phosphatase activity was demonstrated zymographically and by specific enzymatic activity assays, with whole cells or cell membrane preparations as enzyme sources. LppC acid phosphatase showed optimum activity at pH 5, and the enzyme activity was unaffected by Triton X-100, L-(+)-tartaric acid, or EDTA. Database searches revealed significant structural homology of LppC to the Streptococcus pyogenes LppA, Flavobacterium meningosepticum OplA, Helicobacter pylori HP1285, and Haemophilus influenzae Hel [e (P4)] proteins. These results suggest a possible function for these proteins and establish a novel function of streptococcal cell membrane lipoproteins.

* Mailing address: Institute for Molecular Biology, Jena University, Winzerlaer Strasse 10, D-07745 Jena, Germany. Phone: 49-(0)3641-657530. Fax: 49-(0)3641-657520. E-mail: hmalke{at}imb-jena.de.

Appl Environ Microbiol, July 1998, p. 2439-2442, Vol. 64, No. 7
0099-2240/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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