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ClpXP, ClpCP and ClpEP proteases effects on the Streptococcus pneumoniae proteome

ABSTRACT: In the important human pathogen, Streptococcus pneumoniae, the ClpP protease is essential for modulating virulence and the cellular stress response. Here, the Clp ATPase chaperones associate with the ClpP protease to mediate general and targeted proteolysis. To identify the ClpP-dependent function of the Clp ATPases, we modified the IGF-tripeptide ClpP recognition motif for each of the Clp ATPases. We assess the ClpP-dependent phenotypes associated with inactivation of each of the ClpEP (XCP), ClpCP (XEP) and ClpXP (CEP) proteases compared to the wild type (XCEP).

INSTRUMENT(S): Orbitrap Exploris 480

ORGANISM(S): Staphylococcus Aureus

SUBMITTER: Larissa Busch

LAB HEAD: Uwe Völker

PROVIDER: PXD061622 | Pride | 2025-05-01

REPOSITORIES: Pride

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			Action	DRS
	20231012_Exp_LB_Co_Dfre_01_CEPtrap_exp_BR1.raw	Raw
	20231012_Exp_LB_Co_Dfre_02_CEPtrap_exp_BR2.raw	Raw
	20231012_Exp_LB_Co_Dfre_03_CEPtrap_exp_BR3.raw	Raw
	20231012_Exp_LB_Co_Dfre_04_CEPtrap_exp_BR4.raw	Raw
	20231012_Exp_LB_Co_Dfre_05_CEPtrap_stat_BR1.raw	Raw

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