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
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General Information on EC 3.4.25.2 - HslU-HslV peptidase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
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Escherichia coli HslUV protease is a member of a major family of ATP-dependent AAA+ degradation machines
malfunction
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depletion of HslUV leads to an increase in the number of kinetoplasts which undergo abnormal segregation, causing the appearance of giant kinetoplasts as a result of the overreplication of minicircle DNA
physiological function
additional information
physiological function
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the enzyme is involved in a non-lysosomal degradation pathway important for Trypanosoma cruzi biology
physiological function
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HslUV is involved in DNA replication and transcription
physiological function
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HslUV is involved in DNA replication and transcription
physiological function
HslUV is involved in DNA replication and transcription
physiological function
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HslV is essential for Leishmania donovani viability
physiological function
Q383Q5; Q57VB1; Q382V8
the protease complex subunits are involved in the control of cell cycle events
physiological function
Q4Q116; Q4QI03
the protease complex subunits are involved in the control of cell cycle events
physiological function
P0A6H5; P0A7B8
constrction of subunit HslU pseudohexamers containing mixtures of ATPase active and inactive subunits at defined positions in the hexameric ring. Genetic tethering impairs subunit HslV binding and degradation, even for pseudohexamers with six active subunits, but disulfide-linked pseudohexamers do not have these defects. Pseudohexamers containing different patterns of hydrolytically active and inactive subunits retain the ability to unfold protein substrates and/or collaborate with HslV in their degradation
physiological function
A0A0N7ELI3; A0A0N9ELN0
leptospiral HslUV is an ATP-dependent chaperone-peptidase complex containing ATPase associated with various cellular activity (AAA+) and N-terminal nucleophile (Ntn) hydrolase superfamily domains, respectively, which hydrolyzes casein and chymotrypsin-like substrates. Hydrolysis is blocked by threonine protease inhibitors. The infection of J774A.1 acrophages causes the increase of leptospiral denatured protein aggresomes, but more aggresomes accumulate in hslUV gene-deleted mutant. Compared to the wild-type strain, infection of cells in vitro with the mutant result in a higher number of dead leptospires, less leptospiral colonyforming units and lower growth ability, but also display a lower half lethal dose, attenuated histopathological injury and decreased leptospiral loading in lungs, liver, kidneys, peripheral blood and urine in hamsters
physiological function
protease HslV can be activated by peptides derived from the C-termini of both ATPase isoforms HslU1 and HslU2. Five out of the six C-terminal residues of HslU2 are essential for binding to and activating HslV. Dodecapeptides derived from HslU of other parasites and bacteria are able to activate HslV with similar or even higher efficiency
physiological function
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the Hsp90 chaperone and the HslVU protease together regulate the level of TilS, involved in tRNA modification. Deletion of the genes coding for the HslVU protease suppresses the growth defect of an strain with hsp90 deleted, by increasing the cellular level of the essential TilS protein
physiological function
Q92TA7; Q92TA9
the shoot dry weight of Medicago sativa plants inoculated with Rhizobium meliloti HslU, HslV, HslUV or protease ClpXP1 deletion mutants is significantly reduced, and plants display slower free-living growth. All deletion mutants produce less exopolysaccharide and succinoglycan. Protease complexes HslUV and ClpXP are closely associated with ribosomal and proteome quality control proteins
physiological function
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the enzyme is involved in a non-lysosomal degradation pathway important for Trypanosoma cruzi biology
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physiological function
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the protease complex subunits are involved in the control of cell cycle events
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physiological function
-
the enzyme is involved in a non-lysosomal degradation pathway important for Trypanosoma cruzi biology
-
physiological function
-
the enzyme is involved in a non-lysosomal degradation pathway important for Trypanosoma cruzi biology
-
physiological function
-
the enzyme is involved in a non-lysosomal degradation pathway important for Trypanosoma cruzi biology
-
physiological function
-
the protease complex subunits are involved in the control of cell cycle events
-
physiological function
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HslV is essential for Leishmania donovani viability
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additional information
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ClpYQ or HslUV is a two-component ATP-dependent protease composed of ClpY or HslU, an ATPase with unfolding activity, and ClpQ or HslV, a peptidase. In the ClpYQ proteolytic complex, the hexameric rings of ClpY (HslU) are responsible for protein recognition, unfolding, and translocation into the proteolytic inner chamber of the dodecameric ClpQ (HslV). The highly conserved sequence GYVG, residues 90 to 93, pore I site, along with the GESSG pore II site, residues 265 to 269, contribute to the central pore of ClpY in domain N. These two central loops of ClpY are in the center of its hexameric ring in which the energy of ATP hydrolysis allows substrate translocation and then degradation by ClpQ. The pore I site of ClpY has an effect on the adjoining structural region in protein substrates, and the pore I site is essential for the translocation of substrates. The pore II site also interfaces with nearby regions in the substrates but is not necessary for their translocation. An ATP-binding site in domain N, separate from its role in polypeptide, ClpY, oligomerization, is required for complex formation with ClpQ. Tyr408 in ClpY, like residue 385 in ClpX, is necessary for self-oligomerization, and this activity is likely important for in vivo protein-subunit stability
additional information
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the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV
additional information
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the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV. PSI, a classical proteasome inhibitor, does not influence the co-expression level of HslV and proteasome 20 in strain Be-78
additional information
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the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV. PSI, a classical proteasome inhibitor, influences the co-expression level of HslV and proteasome 20 in strain Be-62
additional information
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the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV. PSI, a classical proteasome inhibitor, influences the co-expression level of HslV and proteasome 20 in strain Y
additional information
-
the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV
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additional information
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the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV. PSI, a classical proteasome inhibitor, does not influence the co-expression level of HslV and proteasome 20 in strain Be-78
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additional information
-
the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV. PSI, a classical proteasome inhibitor, influences the co-expression level of HslV and proteasome 20 in strain Be-62
-
additional information
-
the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV. PSI, a classical proteasome inhibitor, influences the co-expression level of HslV and proteasome 20 in strain Y
-
additional information
-
the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV
-
additional information
-
the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV. PSI, a classical proteasome inhibitor, does not influence the co-expression level of HslV and proteasome 20 in strain Be-78
-
additional information
-
the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV. PSI, a classical proteasome inhibitor, influences the co-expression level of HslV and proteasome 20 in strain Be-62
-
additional information
-
the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV. PSI, a classical proteasome inhibitor, influences the co-expression level of HslV and proteasome 20 in strain Y
-
additional information
-
the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV
-
additional information
-
the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV. PSI, a classical proteasome inhibitor, does not influence the co-expression level of HslV and proteasome 20 in strain Be-78
-
additional information
-
the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV. PSI, a classical proteasome inhibitor, influences the co-expression level of HslV and proteasome 20 in strain Be-62
-
additional information
-
the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV. PSI, a classical proteasome inhibitor, influences the co-expression level of HslV and proteasome 20 in strain Y
-
additional information
-
the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV
-
additional information
-
the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV. PSI, a classical proteasome inhibitor, does not influence the co-expression level of HslV and proteasome 20 in strain Be-78
-
additional information
-
the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV. PSI, a classical proteasome inhibitor, influences the co-expression level of HslV and proteasome 20 in strain Be-62
-
additional information
-
the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV. PSI, a classical proteasome inhibitor, influences the co-expression level of HslV and proteasome 20 in strain Y
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