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PXD024033 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleTargets of kinase/phosphatase signalling pair StkP/PhpP in S. pneumoniae and their involvement in response to cell wall stress
DescriptionStreptococcus pneumoniae is an opportunistic human pathogen which encodes a single eukaryotic-type Ser/Thr protein kinase StkP and its functional counterpart protein phosphatase PhpP. These signalling enzymes play a crucial role in the coordination of cell division and growth in pneumococcus. In this study, we determined the proteomic and phosphoproteomic profiles of relevant mutants. A comparison with the wild type provided a representative data set of new phosphoacceptor sites and StkP-dependent substrates. StkP phosphorylates key proteins involved in cell division and cell wall biosynthesis in unencapsulated laboratory Rx1 strain as well as encapsulated virulent strain D39. Moreover, we show that StkP plays important role in eliciting an adaptive response induced by cell wall directed antibiotic. Phosphorylation of WalK sensor kinase and decline of the abundance of WalK and proteins of core WalR/K regulon implies cross-talk between StkP and WalR/K two-component system. Inspection of proteome profiles revealed gene clusters regulated by catabolite control mechanism suggesting a tight coupling of carbon flow and cell wall homeostasis. The disbalance of steady-state protein phosphorylation in the mutants as well as after antibiotic treatment is accompanied by accumulation of global Spx regulator indicating Spx-mediated envelope stress response. In summary, StkP translates the sensed signal about the cell-wall status to key cell division and regulatory proteins and in this way controls cell cycle and cell wall homeostasis.
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterIvo Fabrik
SpeciesList scientific name: Streptococcus pneumoniae R6; NCBI TaxID: 171101; scientific name: Streptococcus pneumoniae D39; NCBI TaxID: 373153;
ModificationListphosphorylated residue; monohydroxylated residue; iodoacetamide derivatized residue
InstrumentQ Exactive Plus
Dataset History
RevisionDatetimeStatusChangeLog Entry
02021-02-07 23:56:32ID requested
12022-05-12 06:17:17announced
Publication List
Ulrych A, Fabrik I, Kupčík R, Vajrychová M, Doubravová L, Branny P, Cell Wall Stress Stimulates the Activity of the Protein Kinase StkP of Streptococcus pneumoniae, Leading to Multiple Phosphorylation. J Mol Biol, 433(24):167319(2021) [pubmed]
Keyword List
submitter keyword: Streptococcus pneumoniae, Ser/Thr protein kinase StkP, phosphatase PhpP, phosphoproteome, cell wall stress, ampicillin treatment, signalling
Contact List
Pavel Branny
contact affiliationInstitute of Microbiology of the CAS, v. v. i., Videnska 1083, 142 20 Prague, Czech Republic
contact emailbranny@biomed.cas.cz
lab head
Ivo Fabrik
contact affiliationBiomedical Research Center, University Hospital Hradec Kralove
contact emailivo.fabrik@gmail.com
dataset submitter
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