Literature summary for 3.4.24.B20 extracted from

Adam, Z.; Aviv-Sharon, E.; Keren-Paz, A.; Naveh, L.; Rozenberg, M.; Savidor, A.; Chen, J.
The chloroplast envelope protease FTSH11 - interaction with CPN60 and identification of potential substrates (2019), Front. Plant Sci., 10, 428 .

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Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
chloroplast	chloroplast envelope	Arabidopsis thaliana	9507	-

Organism

Organism	UniProt	Comment	Textmining
Arabidopsis thaliana	Q9FGM0	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
leaf	-	Arabidopsis thaliana	-

General Information

General Information	Comment	Organism
physiological function	the proteolytic activity, and not only the ATPase one, is essential for conferring thermotolerance to the plants. FTSH11 interacts with different components of the CPN60 chaperonin. CPN60s as well as a number of envelope, stroma and thylakoid proteins are found associated with proteolytically inactive FTSH11. In a knockout strain, protein TIC40 is highly stabilized. The nucleotide antiporter PAPST2, the fatty acid binding protein FAP1 and the chaperone HSP70 are trapped in an affinity enrichment assay	Arabidopsis thaliana

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Release 2023.1 (January 2023)