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Literature summary for 3.4.21.92 extracted from

  • Stanne, T.M.; Pojidaeva, E.; Andersson, F.I.; Clarke, A.K.
    Distinctive types of ATP-dependent Clp proteases in cyanobacteria (2007), J. Biol. Chem., 282, 14394-14402.
    View publication on PubMed
Search for more literature for 3.4.21.92

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Synechococcus elongatus 5829
-
membrane
-
 Synechococcus elongatus 16020
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
140000
-
 native Page, ClpP1 Synechococcus elongatus
140000
-
 native Page, ClpP2 Synechococcus elongatus
270000
-
 native Page, ClpP3 and ClpPR Synechococcus elongatus
300000
-
 gel filtration, ClpP1 and ClpP2 Synechococcus elongatus

Organism

Organism UniProt Comment Textmining
Synechococcus elongatus
-
 wild type and mutants with deleted ClpP1 and ClpP2 genes
-

Purification (Commentary)

Purification (Comment) Organism
by immunoprecipitation Synechococcus elongatus

Subunits

Subunits Comment Organism
heptamer single mixed heptameric ring of ClpP1 and ClpP2 Synechococcus elongatus
More Two soluble Clp proteolytic cores consisting of distinct pairs of ClpP/R paralogs, ClpP1/P2 and ClpP3/R exist in cyanobacteria. Each proteolytic core associates with a different HSP100 partner, ClpX with ClpP1/P2 and ClpC with ClpP3/R, ClpC with two ClpS adaptors. Synechococcus elongatus

Synonyms

Synonyms Comment Organism
Clp protease
-
 Synechococcus elongatus
ClpP cyanobacteria have many ClpP paralogs plus a ClpP variant, ClpP1, ClpP2, ClpP3, ClpR, ClpX, ClpS1 and ClpS2 Synechococcus elongatus