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Article

Characterization of pneumococcal Ser/Thr protein phosphatase phpP mutant and identification of a novel PhpP substrate, putative RNA binding protein Jag.

BMC microbiology - 24 Oct 2016

Ulrych Aleš, Holečková Nela, Goldová Jana, Doubravová Linda, Benada Oldřich, Kofroňová Olga, Halada Petr, Branny Pavel

Abstract excerpt

BACKGROUND: Reversible protein phosphorylation catalyzed by protein kinases and phosphatases is the primary mechanism for signal transduction in all living organisms. Streptococcus pneumoniae encodes a single Ser/Thr protein kinase, StkP, which plays a role in virulence, stress resistance and the regulation of cell wall synthesis and cell division. However, the role of its cognate phosphatase, PhpP, is not well...

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Identifiers

PMID: 27776484
DOI: 10.1186/s12866-016-0865-6
PMCID: PMC5078927

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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