3.4.25.2: HslU-HslV peptidase
This is an abbreviated version!
For detailed information about HslU-HslV peptidase, go to the full flat file.
Word Map on EC 3.4.25.2
Reaction
ATP-dependent cleavage of peptide bonds with broad specificity. =
Synonyms
AAA+ HslUV protease, AAA+ protease HslUV, ATP-dependent protease, ATP-dependent protease hslV, ClpQ, ClpQY, ClpYQ, ClpYQ complex, ClpYQ protease, CodW, CodW-CodX, heat shock protein hslV, HslU ATPase, HslU chaperone, HslU/HslV, HslUV, HslUV complex, HslUV protease, HslUV protease-chaperone complex, HslV, HslV peptidase, HslV protease, HslV-HslU, hslVU, HslVU ATP-dependent protease, HslVU protease, LINF_150005800, PfHslUV, T01.006
ECTree
3.4.25.2 HslU-HslV peptidaseAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 3.4.25.2 - HslU-HslV peptidase
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Arc + H2O
?
-
N-terminal residues of Arc are important for HslUV degradation
-
-
?
DnaA204-protein + H2O
?
-
the degradation of the DnaA204 protein contributes to the temperature sensitivity of the dna204 strain
-
-
?
puromycylpolypeptide + H2O
?
-
HslV and HslU interact and participate in the degradation of misfolded puromycylpolypeptides
-
-
?
RcsA + H2O
?
-
specific substrate degradation, the enzyme is involved in regulation of RcsA, a capsule synthesis activator, the ClpYQ protease acts as a secondary protease in degrading the Lon protease substrate RscA
-
-
?
TraJ + H2O
?
-
TraJ appears to be a substrate for HslVU throughout the growth cycle, but is protected or modified by a factor encoded by the F transfer region in the absence of stress. Activation of the Cpx regulon destabilizes the F plasmid transfer activator, TraJ, via the HslVU protease
-
-
?
SulA + H2O
?
-
the double loops, i.e amino acids 137 to 150 and 175 to 209, in domain I of ClpY are necessary for initial recognition/tethering of natural substrates such as SulA, a cell division inhibitor protein
-
-
?
additional information
?
-
hslV and hslU are coregulated. It is possible that ATPase HslU and protease HslV are involved in an ATP/GTP-dependent protein metabolism
-
-
?
additional information
?
-
-
the GYVG motif of HslU is important in unfolding of natively folded proteins as well as in translocation of unfolded proteins for degradation by HslV in its inner chamber
-
-
?
additional information
?
-
-
ClpQ and ClpY are two heat shock proteins
-
-
?
additional information
?
-
-
in vivo, ClpYQ targets SulA, RcsA, RpoH, and TraJ molecules, identification of the molecular determinants required for the binding of its natural protein substrates by yeast two-hybrid analysis. Domain I of ClpY contains the residues, amino acids 137-150 of loop 1 and 175-209 of loop 2, double loops in domain I of ClpY, that are responsible for recognition of its natural substrates, while domain C is necessary to engage ClpQ, overview
-
-
?
additional information
?
-
-
HslU hexamers recognize and unfold native protein substrates and then translocate the polypeptide into the degradation chamber of the HslV peptidase. The degradation appears to consist of discrete steps, which involve the interaction of different terminal sequence signals in the substrate with different receptor sites in the HslUV protease. Mutations in the unstructured N-terminal and C-terminal sequences of two model substrates alter HslUV recognition and degradation kinetics, including changes in Vmax. Blocking either terminus of the substrate interferes with HslUV degradation, with synergistic effects when both termini are obstructed
-
-
?
additional information
?
-
-
the HslUV complex is an assembly of heat shock locus gene products U and V. The formation of the complete complex is essential for the proteasome to carry out its biochemical and physiological role in the parasite, namely to degrade specific target proteins in an ATP-dependent chaperone assisted manner
-
-
?
additional information
?
-
-
ClpYQ plays a minor role in stress survival and is required for growth at high temperature of 45°C
-
-
?
SulA + H2O
additional information
-
-
-
the enzyme produces 58 peptides with various sizes, 3-31 residues
?
SulA + H2O
additional information
-
-
hslVU in addition to Lon plays an important role in regulation of cell division through degradation of SulA
-
-
?
