Literature summary for 3.4.21.92 extracted from

Tryggvesson, A.; Stahlberg, F.M.; Mogk, A.; Zeth, K.; Clarke, A.K.
Interaction specificity between the chaperone and proteolytic components of the cyanobacterial Clp protease (2012), Biochem. J., 446, 311-320.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
modeling of chaperone ClpC and ClpP3/R subunit structures. The R-ring of ClpP3 is most likely to associate with ClpC	Synechococcus elongatus

Organism

Organism	UniProt	Comment	Textmining
Synechococcus elongatus	Q9L4P3	-	-
Synechococcus elongatus PCC 7942	Q9L4P3	-	-

Synonyms

Synonyms	Comment	Organism
ClpP3	-	Synechococcus elongatus

General Information

General Information	Comment	Organism
physiological function	highly specific association between HSP100 chaperone ClpC and the ClpP3/R core. Two conserved sequences in the N-terminus of ClpR and one in the N-terminus of ClpP3 are crucial for the ClpC-ClpP3/R sdubunit association. These N-terminal domains also influence the stability of the ClpP3/R core complex itself. A unique C-terminal sequence just downstream of the P-loop region previously in ClpC confers specificity for the ClpP3/R core and prevents association with Escherichia coli ClpP	Synechococcus elongatus

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Release 2023.1 (January 2023)