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multimer
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n * 230000, n * 180000, ClpP1, ClpP3, clpP4, ClpP5, clpP6, clpR1, clpR2, ClpR3, cClR4, ClpS1
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1 * 230000, subunit ClpP (12 * 21000, amino acid sequence, subunit of ClpP)
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x * 120000-140000, subunit ClpA, gel filtration, x * 83000, subunit ClpA, amino acid sequence
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ClpP is composed of two superimposed rings of six subunits each, ClpA and ClpP form a tight complex in the presence of MgCl2 and ATP, the ClpAP complex is composed of a dodecamer of ClpP and a hexamer of ClpA
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x * 46300, ClpX, calculation from amino acid sequence
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x * 46000, ClpX, SDS-PAGE
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x * 80000 (ClpA, SDS-PAGE, behaves as a dimer of MW 140000 Da on gel filtration) + x * 23000 (ClpP, SDS-PAGE, behaves as a complex of 10-12 subunits, MW 260000 Da)
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240000 (ClpP with the subunit structure 12 * 23000, SDS-PAGE), gel filtration in presence of more than or at 0.1 M KCl, in absence of KCl, native ClpP appears to dimerize giving a structure with a MW of 500000
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x * 81000, ClpA, SDS-PAGE
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1 * 230000, subunit ClpP (12 * 21000, amino acid sequence, subunit of ClpP)
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x * 120000-140000, subunit ClpA, gel filtration, x * 83000, subunit ClpA, amino acid sequence
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ClpP is composed of two superimposed rings of six subunits each, ClpA and ClpP form a tight complex in the presence of MgCl2 and ATP, the ClpAP complex is composed of a dodecamer of ClpP and a hexamer of ClpA
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x * 80000 (ClpA, SDS-PAGE, behaves as a dimer of MW 140000 Da on gel filtration) + x * 23000 (ClpP, SDS-PAGE, behaves as a complex of 10-12 subunits, MW 260000 Da)
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x * 46000, ClpX, SDS-PAGE
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heptamer
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heptamer
homoheptamer, gel filtration
heptamer
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single mixed heptameric ring of ClpP1 and ClpP2
oligomer
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oligomer
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ClpP3/R complex, SDS-PAGE
tetradecamer
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tetradecamer
crystal structure
additional information
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1400 ClpX hexamers, 250 ClpC heaxmers and 100 ClpE hexamers and 1200 ClpP tetramers are found in one cell during exponential growth at 37°C
additional information
ATPases ClpX and ClpA form active protease complexes with ClpP1. ATPase ClpA is autodegraded in the absence of other substrates
additional information
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ATPases ClpX and ClpA form active protease complexes with ClpP1. ATPase ClpA is autodegraded in the absence of other substrates
additional information
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a subcomplex of ClpP can be produced by dissociation, comprising ClpP1 and ClpR1, 2, 3 and 4, similar to the ClpR-ring described in land plants. Purified ClpP preparation also contains two ClpT subunits, ClpT3 and ClpT4, which like the land plant ClpT1 and ClpT2 show 2 Clp-N domains. The Chlamydomonas complex retains the barrel-like shape of homooligomeric ClpPs, with 4 additional peripheral masses
additional information
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the enzyme is a complex consisting of two components I and II, that can be separated from each other
additional information
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bacteria, tomatoes and Trypanosomes all contain genes for a large protein with extensive homology to the regulartory subunit, ClpA
additional information
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ClpP subunits (MW 21500 Da) are arranged in two hexagonal rings directly superimposed on each other, ClpA (subunit 83000) and ClpP do not associate in absence of ATP
additional information
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ClpA subunit has ATPase activity, ClpP subunit has the proteolytic active site and is activated by ClpA in the presence of ATP
additional information
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enzyme consists of two components: ClpP and ClpA or ClpX
additional information
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enzyme consists of two components: ClpP and ClpA or ClpX
additional information
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enzyme consists of two components: ClpP and ClpA or ClpX
additional information
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enzyme consists of two components: ClpP and ClpA or ClpX
additional information
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enzyme consists of two components: ClpP and ClpA or ClpX
additional information
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enzyme consists of two components: ClpP and ClpA or ClpX
additional information
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enzyme consists of two components: ClpP and ClpA or ClpX
additional information
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ClpX participates with ClpP in the rapid and specific degradation of the lambda O protein
additional information
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ClpX participates with ClpP in the rapid and specific degradation of the lambda O protein
additional information
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ClpX participates with ClpP in the rapid and specific degradation of the lambda O protein
additional information
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ClpA bound with ATP associates with ClpP to form an active proteolytic complex with MW 700000
additional information
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ClpP and ClpA interact to form the active protease, this complex degrades a number of proteins, such as alpha-casein into small peptides and can hydrolyze ATP
additional information
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but the combination of ClpX and ClpP has very little activity against alpha-casein
additional information
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ClpP is synthesized with a 14-amino acid leader which is rapidly cleaved in vivo yielding the in vitro active protein of 193 amino acids
additional information
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effective degradation by enzyme requires an intact complex with N-terminal domains of ClpA chaperone protein to ensure the unfolding of substrates and targeting of unfolded substrates to the protease
additional information
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tetradecamer, sedimentation velocity analytical ultracentrifugation
additional information
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bacteria, tomatoes and Trypanosomes all contain genes for a large protein with extensive homology to the regulartory subunit, ClpA
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additional information
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enzyme consists of two components: ClpP and ClpA or ClpX
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additional information
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enzyme consists of two components: ClpP and ClpA or ClpX
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additional information
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enzyme consists of two components: ClpP and ClpA or ClpX
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additional information
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ClpX participates with ClpP in the rapid and specific degradation of the lambda O protein
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additional information
the ClpP1P2 double-ring complex can be assembled without activator peptide and ipropeptides are processed in a chaperone-dependent manner
additional information
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the ClpP1P2 double-ring complex can be assembled without activator peptide and ipropeptides are processed in a chaperone-dependent manner
additional information
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there exists a flexible N-terminal loop in each enzyme subunit that is important for complex formation with ClpXP and ClpAP
additional information
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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.