PXD052685-1

PXD052685 is an original dataset announced via ProteomeXchange.

Title	Phosphorylation of the juxta-membrane domain of the membrane serine/threonine-kinase StkP and characterization of the impact on the cell cycle of Streptococcus pneumoniae
Description	StkP is the single membrane serine/threonine kinase encoded by the human bacterial pathogen Streptococcus pneumoniae. This protein-kinase is considered to be a key regulator of pneumococcal cell division and morphogenesis. In particular, it phosphorylates and/or interacts with several key cell division proteins to control cell elongation, cell constriction and the final separation of daughter cells. A long-standing question concerns the mode of activation of StkP. Even if, it is proposed that StkP activity could be triggered by an extracellular stimulus from the bacterial cell wall, how StkP carries out the phosphorylation of its substrates in response to this stimulus remains enigmatic. It is proposed that the flexible and intrinsically disordered juxta-membrane domain (JMD) of StkP, which connects the cytoplasmic catalytic domain to the transmembrane span, plays a critical role in StkP activation. Our preliminary experiments showed that when the JMD is deleted, StkP is inactive and unable to phosphorylate its cellular targets in vivo. Importantly, several phosphoproteomic studies performed in other bacterial models have shown that some amino acids of the JMD are phosphorylated, suggesting that StkP JMD phosphorylation could also be key for StkP activation. To test this, we wanted to perform a comprehensive identification of the potential phosphorylation sites within the JMD. For that, we purified StkP from Streptococcus pneumoniae and characterized all the amino acids phosphorylated inside de JMD by mass spectrometry. We will then evaluate the impact of the phosphorylation sites on the activation of StkP and its ability to regulate cell division.
HostingRepository	PRIDE
AnnounceDate	2025-03-20
AnnouncementXML	Submission_2025-03-20_11:13:51.453.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Vaishnavi Ravikumar
SpeciesList	scientific name: Streptococcus pneumoniae (strain ATCC BAA-255 / R6); NCBI TaxID: 171101;
ModificationList	phosphorylated residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2024-05-29 14:47:04	ID requested
⏵ 1	2025-03-20 11:13:52	announced

Dataset with its publication pending

submitter keyword: protein-kinase, cell division, phosphorylation,Streptococcus pneumoniae

Ivan Mijakovic
contact affiliation	Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark
contact email	ivmi@biosustain.dtu.dk
lab head
Vaishnavi Ravikumar
contact affiliation	Copenhagen University Hospital
contact email	vaishnavi.ravikumar@gmail.com
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2025/03/PXD052685

PRIDE project URI

• PRIDE
  1. PXD052685
     1. Label: PRIDE project
     2. Name: Phosphorylation of the juxta-membrane domain of the membrane serine/threonine-kinase StkP and characterization of the impact on the cell cycle of Streptococcus pneumoniae