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TranscriptomicsTranscriptome analysis of the eukaryotic-type ser/thr kinase PknB in Staphylococcus aureus
The function of the Staphylococcus aureus eukaryotic-like serine/threonine protein kinase PknB was investigated by transcriptome analysis using DNA-microarray technology and biochemical assays. The transcriptional profile reveals a strong regulatory impact of PknB on the expression of genes encoding...
ORGANISM(S): Staphylococcus aureus subsp. aureus NCTC 8325 
2010-05-05 | E-GEOD-15346 | biostudies-arrayexpress
ProteomicsTwo faces of an essential PknB substrate in mycobacteria
Tuberculosis claims nearly 2 million lives annually and its causative agent Mycobacterium tuberculosis is a highly successful pathogen which explores multiple signalling mechanisms to grow and survive in humans for decades. Well-studied protein kinase B (PknB), one of the 11 serine/threonine kinases...
ORGANISM(S): Mycobacterium tuberculosis H37Rv Mycobacterium tuberculosis complex 
2018-09-24 | PXD009239 | Pride
Mycobacterium tuberculosis Pasta domain Cwlm Pknb Murj Peptidoglycan Phosphoproteomics Serine/threonine protein kinase 
TranscriptomicsGene expression of Streptococcus mutans pknB mutant versus wild type strain
Bacteria can detect, transmit and react to signals from the outside world by using two-component systems an serine-threonine kinases and phosphatases. Streptococcus mutans contains one serine-threonine kinase, encoded by pknB. A gene encoding a serine-threonine phosphatase, pppL, is located downstre...
ORGANISM(S): Streptococcus mutans UA159 
2010-05-06 | E-GEOD-18355 | biostudies-arrayexpress
ProteomicsOverexpression of the mycobacterial PknB Ser/Thr kinase uncovers its global regulatory role in mycolic acids biosynthesis and trafficking
Comparison of the global phospho-proteomes of Mycobacterium smegmatis wild type, and over-expressing the protein kinase PknB from Mycobacterium tuberculosis or its enzymatically inactive K40M isoform.
ORGANISM(S): Escherichia coli 
2021-08-30 | PXD012553 | Pride
Mycobacterium smegmatis phosphoproteomics nanohlpc-ms/ms 
TranscriptomicsProtein kinase B-mediated phosphorylation controls binding of global transcriptional regulator Lsr2 to DNA in Mycobacterium tuberculosis
Two billion people are estimated to have latent tuberculosis infection associated with dormant Mycobacterium tuberculosis. Mycobacteria possess a great portfolio of regulatory proteins which that control transitions betweento dormancy and resuscitation, including the essential protein kinase B (PknB...
ORGANISM(S): Mycobacterium tuberculosis H37Rv 
2019-10-02 | E-MTAB-7627 | biostudies-arrayexpress
ProteomicsPhosphoproteomics to uncover phosphorylation substrates changes when serine/threonine protein kinase PknA and PknB depletion
The Mycobacterium tuberculosis eukaryotic-like serine/threonine protein kinase (STPKs) PknA and PknB regulate several processes required for cell growth, both kinase have been found to be and can be investigated by using the conditional mutant. In the present study, we created the M. tuberculosis ki...
ORGANISM(S): Mycobacterium tuberculosis C StG4006 
2020-05-27 | PXD015197 | Pride
Mycobacterium tuberculosis  serine/threonine protein kinase (stpks) pkna and pknb  phosphoproteomics 
ProteomicsInteraction of LipidII with specific residues of its extracytoplasmic domain governs appropriate localization and optimal activation of Mycobacterium tuberculosis PknB
The Mycobacterium tuberculosis kinase PknB is essential for growth and survival of the pathogen in vitro and in vivo. Here we present the results of our efforts to elucidate the mechanism of regulation of PknB activity. The specific residues in the kinases’s extracytoplasmic domain that are essentia...
ORGANISM(S): Mycobacterium tuberculosis H37Rv 
2019-03-14 | PXD012180 | Pride
Tuberculosis Activation Pknb Protein kinase Substrate Mycobacteria Pasta 
TranscriptomicsGene expression of Streptococcus mutans pknB mutant versus wild type strain
Bacteria can detect, transmit and react to signals from the outside world by using two-component systems an serine-threonine kinases and phosphatases. Streptococcus mutans contains one serine-threonine kinase, encoded by pknB. A gene encoding a serine-threonine phosphatase, pppL, is located downstre...
ORGANISM(S): Streptococcus mutans UA159 
2010-03-05 | GSE18355 | GEO
ProteomicsThe Hanks-type kinase PknB, targeting the divisome, is not the single player in the Streptococcus thermophilus protein phosphorylation process
This work focus on  in the role of Ser/Thr/Tyr protein phosphorylation in Streptococcus thermophilus, the only streptococcal species used in food fermentation. During technological processes, S. thermophilus has to adapt to various nutrition and physical-chemical stresses that require rapid adjustme...
ORGANISM(S): Streptococcus thermophilus LMD-9 
2019-07-08 | PXD011391 | Pride
Streptococcus thermophilus Pknb Phosphoproteome Shotgun 
ProteomicsAuxB interacts directly with GpsB and PknB to coordinate cell envelope processes that contribute to intrinsic antibiotic resistance in Staphylococcus aureus
Staphylococcus aureus, a leading cause of serious infections, produces various factors important for intrinsic resistance to antibiotics. Understanding what intrinsic resistance factors do may enable strategies to potentiate existing antibiotics. The membrane protein AuxB is an intrinsic resistance ...
ORGANISM(S): Staphylococcus aureus 
2025-08-25 | PXD065790 | Pride
Prka Prkc Pasta domain Staphylococcus aureus Serine/threonine kinases Cell wall Pknb Cell envelope Stkp Antibiotic resistance 
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