Literature DB >> 11751838

Streptococcus pneumoniae capsule biosynthesis protein CpsB is a novel manganese-dependent phosphotyrosine-protein phosphatase.

Judy K Morona1, Renato Morona, David C Miller, James C Paton.   

Abstract

The first four genes of the capsule locus (cps) of Streptococcus pneumoniae (cpsA to cpsD) are common to most serotypes. We have previously determined that CpsD is an autophosphorylating protein-tyrosine kinase, demonstrated that CpsC is required for CpsD tyrosine-phosphorylation, and shown that CpsB is required for dephosphorylation of CpsD. In the present study we show that CpsB is a novel manganese-dependent phosphotyrosine-protein phosphatase that belongs to the PHP (polymerase and histidinol phosphatase) family of phosphoesterases. We also show that an S. pneumoniae strain with point mutations in cpsB, affecting one of the conserved motifs of CpsB, is unencapsulated and appears to be morphologically identical to a strain in which the cpsB gene had been deleted.

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Year:  2002        PMID: 11751838      PMCID: PMC139577          DOI: 10.1128/JB.184.2.577-583.2002

Source DB:  PubMed          Journal:  J Bacteriol        ISSN: 0021-9193            Impact factor:   3.490


  20 in total

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  44 in total

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Journal:  J Bacteriol       Date:  2002-09       Impact factor: 3.490

2.  Mutational analysis of the carboxy-terminal (YGX)4 repeat domain of CpsD, an autophosphorylating tyrosine kinase required for capsule biosynthesis in Streptococcus pneumoniae.

Authors:  Judy K Morona; Renato Morona; David C Miller; James C Paton
Journal:  J Bacteriol       Date:  2003-05       Impact factor: 3.490

3.  Membrane topology and DNA-binding ability of the Streptococcal CpsA protein.

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Journal:  J Bacteriol       Date:  2010-11-19       Impact factor: 3.490

4.  Streptococcus pneumoniae phosphotyrosine phosphatase CpsB and alterations in capsule production resulting from changes in oxygen availability.

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5.  Functional analysis of the CpsA protein of Streptococcus agalactiae.

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9.  Lipoprotein PsaA in virulence of Streptococcus pneumoniae: surface accessibility and role in protection from superoxide.

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Journal:  Appl Environ Microbiol       Date:  2007-09-07       Impact factor: 4.792

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