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Information on EC 3.4.25.2 - HslU-HslV peptidase and Organism(s) Escherichia coli and UniProt Accession P0A7B8
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3.4.25.2 HslU-HslV peptidaseSpecify your search results
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The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
atp-dependent protease, hsluv, clpyq, hslu atpase, hslv peptidase, hslvu protease, hslv protease, clpyq protease, hsluv complex, clpqy, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
hslVU
a two-component protease complex, which consists of the HslV peptidase and the HslU ATPase
ATP-dependent protease hslV
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ClpQ
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heat shock protein hslV
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hslVU
T01.006
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hslVU
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ATP-dependent protease consisting of two heat shock proteins, the HslU ATPase and HslV peptidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP-dependent cleavage of peptide bonds with broad specificity.
model for a proteolytic cycle by HslVU protease, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY
178303-43-0
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SUBSTRATE
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
benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-GGL + 7-amino-4-methylcoumarin
-
-
-
?
carbobenzoxy-Gly-Gly-Leu-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Gly-Gly-Leu + 7-amino-4-methylcoumarin
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-
-
?
Arc repressor + H2O
?
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interaction of Arc substrates with HslU variants bearing mutations in the GYVG pore loop or the I domain, overview. N-terminal residues of Arc initially interact with the GYVG loop in the axial pore of HslU, while other portions of Arc contact disordered I-domain loops, residues 175-209, that project into the substrate-binding funnel above the pore
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-
?
Arc-st11-ssrADD + H2O
?
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Arc variants with a C-terminal ssrA tag (Arc-ssrA), the st11 tag and a mutant ssrA tag in which the terminal AA sequence is replaced by DD
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-
?
Arc1-53-st11-titin-ssrA + H2O
?
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recombinant truncated Arc fusion protein
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-
?
benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-GGL + 7-amino-4-methylcoumarin
carbobenzoxy-Gly-Gly-Leu-7-amido-4-methyl coumarin + H2O
carbobenzoxy-Gly-Gly-Leu + 7-amino-4-methyl coumarin
-
the HslV peptidase alone shows a very weak peptidase activity towards carbobenzoxy-Gly-Gly-Leu-7-amido-4-methyl coumarin, but its activity increases 1-2 orders of magnitude when it binds to HslU in the presence of ATP
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-
?
DnaA204-protein + H2O
?
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the degradation of the DnaA204 protein contributes to the temperature sensitivity of the dna204 strain
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-
?
lambda cI repressor mutant ext1-lambdacIN-ISVTL + H2O
?
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a variant in which the C-terminal sequence is changed from RSEYE to ISVTL, to give ext1-lambdacIN-ISVTL, that HslUV degrades faster than the parental protein, ext1-lambdacIN-RSEYE, by 2fold increase in Vmax
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-
?
N-carbobenzyloxy-Gly-Gly-Leu-7-amido-4-methylcoumarin + H2O
N-carbobenzyloxy-Gly-Gly-Leu + 7-amino-4-methylcoumarin
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-
-
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?
puromycylpolypeptide + H2O
?
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HslV and HslU interact and participate in the degradation of misfolded puromycylpolypeptides
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-
?
succinyl-LLVY-7-amido-4-methylcoumarin + H2O
succinyl-LLVY + 7-amino-4-methylcoumarin
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?
unfolded lactalbumin + H2O
?
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HslV alone can efficiently degrade certain unfolded proteins, such as unfolded lactalbumin and lysozyme prepared by complete reduction of disulfide bonds, but not their native forms. HslV alone cleaves a lactalbumin fragment sandwiched by two thioredoxin molecules, indicating that it can hydrolyze the internal peptide bonds of lactalbumin. Uncomplexed HslV is inactive under normal conditions, but can degrade unfolded proteins when the ATP level is low, as it is during carbon starvation
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?
unfolded lysozyme + H2O
?
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HslV alone can efficiently degrade certain unfolded proteins, such as unfolded lactalbumin and lysozyme prepared by complete reduction of disulfide bonds, but not their native forms. HslV alone cleaved a lactalbumin fragment sandwiched by two thioredoxin molecules, indicating that it can hydrolyze the internal peptide bonds of lactalbumin. Uncomplexed HslV is inactive under normal conditions, but can degrade unfolded proteins when the ATP level is low, as it is during carbon starvation
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-
?
alpha-casein + H2O
?
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the structural features of the GYVG motif increase degrading activity
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-
?
Arc + H2O
?
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repressor protein, specific degradation, especially at heat shock temperatures, recognition of sequences near the N-terminus of Arc and strong binding requiring Mg2+ and ATP for degradation
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?
Arc + H2O
?
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N-terminal residues of Arc are important for HslUV degradation
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?
Arc-st11-ssrA + H2O
?
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Arc variants with a C-terminal ssrA tag (Arc-ssrA), the st11 and ssrA tags (Arc-st11-ssrA)
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-
?
Arc-st11-ssrA + H2O
?
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wild-type HslU binds this fluorescent substrate with an average affinity, whereas the Y91A mutant variant shows no detectable binding. Tyr91 side chain plays an important role in allowing HslU to bind Arc-st11-ssrA
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?
benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-GGL + 7-amino-4-methylcoumarin
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?
benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-GGL + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-GGL + 7-amino-4-methylcoumarin
-
-
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-
?
benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-GGL + 7-amino-4-methylcoumarin
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HslV alone cleaves to a much lesser extent than in presence of HslU
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-
?
benzyloxycarbonyl-Gly-Gly-Leu-7-amido-4-methylcoumarin + H2O
?
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the N-terminal Thr active sites of HslV are involved in the communication between HslV and HslU in addition to its role in the catalysis of peptide bond cleavage
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?
Insulin B-chain + H2O
?
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HslVU degrades insulin B-chain even more rapidly in the presence of ATPgammaS than with ATP
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?
RcsA + H2O
?
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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
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?
RcsA + H2O
?
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specific substrate degradation, the enzyme is involved in regulation of RcsA, a capsule synthesis activator
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-
?
SulA + H2O
?
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specific substrate degradation, the substrate is a cell division inhibitor
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?
SulA + H2O
?
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recombinant substrate, produced as maltose-binding fusion protein and cleaved by factorXa
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?
SulA + H2O
?
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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
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?
SulA + H2O
?
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a cell division inhibitor protein. Degradation of MBP-SulA by ClpY and ClpY mutants Y408A and T87I in the presence of ClpQ
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?
SulA-maltose binding protein-fusion protein + H2O
?
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recombinant substrate, formation of a ternary complex of HslV-HslU-substrate during reaction, molecular interaction study, interaction via HslU, not HslV
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?
SulA-maltose binding protein-fusion protein + H2O
?
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recombinant substrate, specific substrate degradation requires the flexibility provided by glycine residues and aromatic ring structures of the first 91 amino acids
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?
TraJ + H2O
?
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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
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?
additional information
?
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hslV and hslU are coregulated. It is possible that ATPase HslU and protease HslV are involved in an ATP/GTP-dependent protein metabolism
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?
additional information
?
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no hydrolysis of gamma-globulin, lysozyme and bovine serum albumin
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?
additional information
?
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HslV and HslU can function together as a novel ATP-dependent protease, the HslVU protease. Pure HslV is a weak peptidase degrading certain hydrophobic peptides. HslU dramatically stimulates peptide hydrolysis by HslV when ATP is present. With a 1:4 molar ratio of HslV to HslU, approximately a 200fold increase in peptide hydrolysis is observed. HslV stimulates the ATPase activity of HslU 2-4fold. CTP and dATP are slowly hydrolyzed by HslU and allow some peptide hydrolysis
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?
additional information
?
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ATP-binding, but not its hydrolysis, is essential for assembly and proteolytic activity of HslVU
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?
additional information
?
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less than 1% of the activity with benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin is observed with succinyl-AAF-7-amido-4-methylcoumarin and succinyl-LLVY-7-amido-4-methylcoumarin. No activity with benzoyl-RGFFL-4-methoxy-beta-naphthylamide, glutaryl-AAA-4-methoxy-beta-naphthylamide, benzyloxycarbonyl-LLE-4-methoxy-beta-naphthylamide, succinyl-FLF-beta-naphthylamide, succinyl-LY-7-amido-4-methylcoumarin, benzoyl-GP-7-amido-4-methylcoumarin, acetyl-YVAA-7-amido-4-methylcoumarin, tert-butyloxycarbonyl-LRR-7-amido-4-methylcoumarin, t-butyloxycarbonyl-FVR-7-amido-4-methylcoumarin, benzoyl-GGR-7-amido-4-methylcoumarin, benzoyl-Arg-7-amido-4-methylcoumarin
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-
?
additional information
?
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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
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?
additional information
?
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analysis of interaction of free and inhibited HslV with HslU showing moderate affinity, scheme of substrate-induced HslUV assemblage, overview
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?
additional information
?
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substrate binding, ATP-dependent protein degradation, and reaction mechanism, substrate engagement must occur after ATP-binding before HslUV unfolds the proteins, overview
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?
additional information
?
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degradation of proteins in an ATP-dependent and tag-specific manner. For degradation from the N-terminus, HslUV has the strongest unfolding ability of all the bacterial proteases (unfolding abilities of the 26S proteasome), whereas for degradation from the C-terminus, HslUV is one of the weaker unfoldases. HslUV unfolds proteins more effectively when degrading from the N- towards the C-terminus than in the opposite direction
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-
?
additional information
?
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HslVU is an ATP-dependent protease consisting of two heat shock proteins, the HslU ATPase and HslV peptidase. In the reconstituted enzyme, HslU stimulates the proteolytic activity of HslV by one to two orders of magnitude, while HslV increases the rate of ATP hydrolysis by HslU several-fold. HslV alone can efficiently degrade certain unfolded proteins, such as unfolded lactalbumin and lysozyme prepared by complete reduction of disulfide bonds, but not their native forms. HslV alone cleaves a lactalbumin fragment sandwiched by two thioredoxin molecules, indicating that it can hydrolyze the internal peptide bonds of lactalbumin. Uncomplexed HslV is inactive under normal conditions, but can degrade unfolded proteins when the ATP level is low, as it is during carbon starvation
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-
?
additional information
?
-
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ClpQ and ClpY are two heat shock proteins
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-
?
additional information
?
-
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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
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-
?
additional information
?
-
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ClpYQ is a two-component ATP-dependent protease in which ClpQ is the peptidase subunit and ClpY is the ATPase and the substrate-binding subunit. The ATP-dependent proteolysis is mediated by substrate recognition in the ClpYQ complex
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?
additional information
?
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HslVU is a bacterial ATP-dependent protease consisting of hexameric HslU ATPase and dodecameric HslV protease. HslV uses the N-terminal threonine as the active site residue. HslV has 12 active sites among the 14beta-subunits that can potentially contribute to proteolytic activity, but only 6 active sites are sufficient to support full catalytic activity. Substrate-mediated stabilization of the HslV-HslU interaction
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-
?
additional information
?
-
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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
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-
?
additional information
?
-
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modeling of overall reaction by substrate binding and dissociation steps, and by a rate-limiting enzymatic step, which corresponds to substrate engagement, unfolding, or translocation
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-
?
additional information
?
-
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substrates are typically targeted to specific AAA+ proteases by peptide sequences. In the AAA+ HslUV protease, substrates are bound and unfolded by a ring hexamer of HslU, before translocation through an axial pore and into the HslV degradation chamber. The I domain plays an active role in coordinating substrate binding, ATP hydrolysis, and protein degradation by the HslUV proteolytic machine
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?
SulA + H2O
additional information
-
-
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the enzyme produces 58 peptides with various sizes, 3-31 residues
?
SulA + H2O
additional information
-
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the central and the C-terminal regions are preferentially cleaved. Major cleavage sites: Ala80-Ser81, Ala150-Ser151, Leu54-Gln55, Ile163-His164, Leu67-Thr68, Leu49-Leu50, Leu65-Trp66. No cleavage in absence of ATP
the enzyme produces 58 peptides with various sizes, 3-31 residues
?
SulA + H2O
additional information
-
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cell division inhibitor SulA, the internal region of SulA is necessary for interactions with ClpY, the N-terminal amino acid residues of SulA are not necessary
-
-
?
SulA + H2O
additional information
-
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hslVU in addition to Lon plays an important role in regulation of cell division through degradation of SulA
-
-
?
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
-
-
?
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
adenosine 5'-(alpha,beta-methylene)triphosphate
-
HslVU degrades insulin B-chain more rapidly in the presence of ATPgammaS than with ATP
ATPgammaS
-
HslVU degrades insulin B-chain more rapidly in the presence of ATPgammaS than with ATP
beta,gamma-Imido-ATP
-
supports proteolytic activity to an extent less than 10% of that seen with ATP
5'-adenylyl beta,gamma-imidotriphosphate
-
the enzyme degrades SulA and the fusion protein of SulA and maltose-binding protein in presence of ATP but not with ATPgammaS
5'-adenylyl beta,gamma-imidotriphosphate
-
can support peptide hydrolysis, but only after an initial time lag not seen with ATP. This delay decreases at higher temperatures and with higher HslV or HslU concentrations and is eliminated by preincubation of HslV and HslU together
5'-adenylyl beta,gamma-imidotriphosphate
-
can support peptide hydrolysis, but only after an initial time lag not seen with ATP. This delay decreases at higher temperatures and with higher HslV or HslU concentrations and is eliminated by preincubation of HslV and HslU together. Supports hydrolysis of casein and other polypeptides only 20% as well as ATP. But in presence of K+, Cs+ or NH4+, activation of casein degradation is even better than that by ATP, although it is not hydrolyzed
ATP
-
ATP-binding, but not its hydrolysis, is essential for assembly and proteolytic activity of HslVU. The ability of ATP and its analogs in supporting the proteolytic activity is closely correlated with their ability in supporting the oligomerization of HslU and the formation of the HslVU complex
ATP
-
ATP activates hydrolysis of benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin 150fold
ATP
-
HslV and HslU can function together as a novel ATP-dependent protease, the HslVU protease. Pure HslV is a weak peptidase degrading certain hydrophobic peptides. HslU dramatically stimulates peptide hydrolysis by HslV when ATP is present. With a 1:4 molar ratio of HslV to HslU, approximately a 200fold increase in peptide hydrolysis is observed. HslV stimulates the ATPase activity of HslU 2-4fold. CTP and dATP are slowly hydrolyzed by HslU and allow some peptide hydrolysis
ATP
-
the enzyme degrades SulA and the fusion protein of SulA and maltose-binding protein in presence of ATP but not with ATPgammaS
ATP
-
HslV can slowly hydrolyze insulin B-chain, casein or carboxymethylated lactalbumin, but its activity is stimulated 20fold by HslU in presence of ATP
ATP
-
ATP concentrations that activate hydrolysis of benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin are 50-100fold lower than those necessary for degradation of proteins, e.g. casein. ATP binding to a high affinity site triggers the formation of an active state capable of peptide cleavage, although ATP hydrolysis facilitates this process
ATP
-
ATP binding and hydrolysis are critical for protein degradation by HslUV, an AAA+ machine containing one or two HslU ATPases and the HslV peptidase. Asymmetric mechanism of ATP binding and hydrolysis. Molecular contacts between HslU and HslV vary dynamically throughout the ATPase cycle. Nucleotide binding controls HslUV assembly and activity. Binding of a single ATP allows HslU to bind HslV, whereas additional ATPs must bind HslU to support substrate recognition and to activate ATP hydrolysis, which powers substrate unfolding and translocation
ATP
-
dependent on, an ATP-binding site in domain N, separate from its role in polypeptide, ClpY, oligomerization, is required for complex formation with ClpQ
ATP
-
dependent on. The intermediate domain of HslU is required for robust ATP hydrolysis, ATP hydrolysis activities of wild-type and mutant enzymes, overview
additional information
-
HslU requires Mg2+ together with ATP for activity
-
additional information
-
HslU does not hydrolyze ATPgammaS, an ATP analogue
-
additional information
-
no activity with ATP-gammaS analogue, thermodynamic analysis of ATP-gammaS-binding and ATPase activity of wild-type ClpY and its T87I mutant, overview. In the presence of MBP-SulA and ClpQ, the mutant has about one-fourth of the ATPase activity of wild-type ClpY, ClpY mutant T87I in its hexameric form is defective in ATPase activity
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CaCl2
-
allows some peptidase and caseinase activity in the absence of any nucleotide, however Ca2+ abolishes ATP hydrolysis and prevents further activation by ATP and 5'-adenylyl beta,gamma-imidodiphosphate
Cs+
-
stimulates 4-6fold the peptidase activity with 5'-adenylyl beta,gamma-imidodiphosphate present and eliminates the time lag for activation, no stimulatory effect with ATP
KCl
-
stimulates 4-6fold the peptidase activity with 5'-adenylyl beta,gamma-imidodiphosphate present and eliminates the time lag for activation, no stimulatory effect with ATP
Mg2+
MgCl2
-
allows some peptidase and caseinase activity in the absence of any nucleotide
MnCl2
-
allows some peptidase and caseinase activity in the absence of any nucleotide, however Mn2+ abolishes ATP hydrolysis and prevents further activation by ATP and 5'-adenylyl beta,gamma-imidodiphosphate
NH4+
-
stimulates 4-6fold the peptidase activity with 5'-adenylyl beta,gamma-imidodiphosphate present and eliminates the time lag for activation, no stimulatory effect with ATP
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
benzyloxycarbonyl-Ile-Glu(tert-butyl)-Ala-Leu-al
-
0.001 mM, almost complete inhibition of peptidase activity, no inhibition of hydrolysis of insulin B-chain or other polypeptide substrates
benzyloxycarbonyl-Leu-Leu-norvalinal
-
0.004 mM, inhibits hydrolysis of both benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin and insulin B-chain to a similar extent
NLVS
-
in the presence of ATP, the proteasome inhibitor markedly increases the interaction between HslV and HslU and causes the activation of the HslU ATPase
ATP
-
inhibits the degradation of unfolded proteins by HslV. This inhibitory effect of ATP is markedly diminished by substitution of the Arg86 residue located in the apical pore of HslV with Gly, suggesting that interaction of ATP with the Arg residue blocks access of unfolded proteins to the proteolytic chamber of HslV
lactacystin
-
irreversible, much greater inhibition of the degradation of insulin B-chain than on peptide hydrolysis
lactacystin
-
in the presence of ATP, the proteasome inhibitor markedly increases the interaction between HslV and HslU and causes the activation of the HslU ATPase
NEM
-
preincubation with followed by inactivation of dithiothreitol causes inhibition of peptide hydrolysis
additional information
-
the I125-labeled nitrophenyl derivative 125iodo-NIP-Leu-Leu-Leu vinyl sulfone covalently modifies and inhibits HslV, but only in presence of HslU and ATP
-
additional information
-
enzyme inactivation by 7.5% SDS and 10% v/v 2-mercaptoethanol
-
additional information
-
protein binding, e.g. of Escherichia coli ClpS, SspB, or DegS PDZ domain polypeptides, to the C-terminus of substrates selectively slows HslUV degradation, the inhibition affects an early step in degradation. Synergistic effects of N- and C-terminal blocking
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-(3,4-dihydroxyphenyl)-2-[2-(pyridin-2-yl)-1H-benzimidazol-1-yl]ethanone
-
-
3-{(E)-[(2-hydroxynaphthalen-1-yl)methylidene]amino}-2-(4-nitrophenyl)quinazolin-4(3H)-one
-
-
HslU
-
HslV can slowly hydrolyze insulin B-chain, casein or carboxymethylated lactalbumin, but its activity is stimulated 20fold by HslU in presence of ATP
-
HslU
-
the HslU C-terminal tails act as a molecular switch for the assembly of HslVU complex and the activation of HslV peptidase
-
HslU
-
HslV protomer interfaces perform distinct functions: whereas intra-ring interface participates in HslV:HslU interaction resulting in allosteric activation of HslV protease by HslU, the interring interfaces uphold the oligomeric form of HslV
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetics, analysis of interaction of free and inhibited HslV with HslU
-
additional information
additional information
-
Michaelis-Menten steady-state kinetics of wild-type and point mutant as well as deletion mutant enzymes with Arc substrates and ATP, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
HslUV is involved in DNA replication and transcription
evolution
-
Escherichia coli HslUV protease is a member of a major family of ATP-dependent AAA+ degradation machines
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
additional information
-
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
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
220000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dodecamer
hexamer
oligomer
-
HslVU is a bacterial ATP-dependent protease consisting of hexameric HslU ATPase and dodecameric HslV protease. HslV has 12 active sites among the 14beta-subunits that can potentially contribute to proteolytic activity
additional information
dodecamer
-
HslV, the proteolytic active sites are sequestered in the inner chamber of HslV
dodecamer
-
HslVU, a two-component proteasome-related prokaryotic system is composed of HslV protease and HslU ATPase. HslV protomers assemble in a dodecamer of two-stacked hexameric rings that form a complex with HslU hexamers. Structural analyses of protomer interfaces in HslV dodecamer suggests that HslV interfaces involve extensive area in which major determinants for function and stability constitute hot spots
hexamer
-
self-oligomerization of each ClpQ and ClpY, four hexamers constitute a dumb-bell-shaped complex ina Y6Q6Q6Y6 configuration
additional information
-
HslVU protease is a two-component protease in which HslV harbors the peptidase activity, while HslU provides an essential ATPase activity
additional information
-
the crystal strcuture shows that HslU forms a hexamer with a pore at one end and HslV forms a dodecamer with translocation pores at both ends of two back-to-back stacked hexameric rings
additional information
-
HslVU is a ATP-dependent protease composed of two multimeric complexes: the hslU ATPase and the HslV peptitase
additional information
-
ClpYQ is an ATP-dependent protease that consists of an ATPase large subunit, ClpY, and a peptidase small subunit, ClpQ. Six identical subunits of both ClpY and ClpQ self-assemble into an oligomeric ring, and two rings of each subunit, two ClpQ rings surrounded by single ClpY rings, form a dumbbell shape complex
additional information
-
HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase
additional information
-
the subunits of ClpY and ClpQ are arranged in hexagonal rings. The structure of ClpQ is a double hexameric ring
additional information
-
HslV and HslU form cylindrical four-ring structures in which the HslV dodecamer is flanked at each end by a HslU ring
additional information
-
structure analysis using crystal structure PDB code 1G4A, the GYVG motif is essential for enzyme complex activity, overview
additional information
-
ClpYQ is a two-component ATP-dependent protease in which ClpQ is the peptidase subunit and ClpY is the ATPase and the substrate-binding subunit. ClpY has three domains, N, I, and C, and these domains are discrete and exhibit different binding preferences
additional information
-
mathematical models for stochastically assembled HslV dodecamers, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of an 820000 Da relative molecular mass complex of the ATPase HslU and the protease component HslV, sitting drop vapour diffusion against a reservoir containing 100 mM sodium cacodylate pH 6.5, 15% glycerol, 10.5% polyethylene glycol PEG 8K and 500 mM (NH4)2SO4
mutant enzyme L88A, hanging drop vapor diffusion method, using 0.1 M Tris-HCl (pH 8.0), 28% (v/v) PEG monomethyl ether 550, and 0.2 M ammonium formate
sitting drop vapor difussion against a reservoir containing 100 mM Hepes/NaOH at pH 7.5, 200 mM sodium acetate, 0.02% NaN3 and between 9% and 14% ethanol
hanging-drop vapor diffusion method. 3.0 A resolution crystal structure of hslV with an HslU hexamer bound at one end of an HslV dodecamer. The structure shows that the central pores of the ATPase and peptidase are next to each other and alligned
-
purified recombinant HslU and HslV and hybrid complexes with Bacillus subtilis enzymes CodW-HslU and HslV-CodX, X-ray diffraction strucure determination and analysis at 3.5-4.6 A resolution, the co-crystals contain lattice-translocation defects, correction, application of the lattice-translocation defect theory to atomic models, overview
-
the crystal strcuture shows that HslU forms a hexamer with a pore at one end and HslV forms a dodecamer with translocation pores at both ends of two back-to-back stacked hexameric rings
-
wild-type or HslV-HsvU complexed with resorufin casein, hanging-drop vapor diffusion method
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
L88A
the mutation leads to a tighter binding between HslV and HslU and a dramatic stimulation of both the proteolytic and ATPase activities. Furthermore, the HslV mutant shows a more than 7fold increase of basal hydrolytic activities toward small peptides and unstructured proteins
L88F
the muattion increases the peptidolytic activity of HslV in both the absence and presence of HslU and stimulates the ATPase activity of HslU more than wild type HslV
L88G
the HslV mutant shows a marked increase of basal hydrolytic activities toward small peptides and unstructured proteins
L88S
the HslV mutant shows a marked increase of basal hydrolytic activities toward small peptides and unstructured proteins
L88W
the muattion increases the peptidolytic activity of HslV in both the absence and presence of HslU and stimulates the ATPase activity of HslU more than wild type HslV
R86A
the mutant shows little peptidolytic activity compared to the wild type
R89A
the mutant shows little peptidolytic activity compared to the wild type
S103A
50% of the activity of the wild-type enzyme with benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin in presence of the ATPase component HslU
S124A
3% of the activity of the wild-type enzyme with benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin in presence of the ATPase component HslU
S143A
95% of the activity of the wild-type enzyme with benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin in presence of the ATPase component HslU
S172A
1% of the activity of the wild-type enzyme with benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin in presence of the ATPase component HslU
S5A
124% of the activity of the wild-type enzyme with benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin in presence of the ATPase component HslU
A188S
-
clpY mutant, the mutant shows altered interaction with SulA substrates, wild-type and mutant, and altered induction by arabinose or glutamate compared to the wild-type, overview
DELTA111-239
2 Gly linker, amidolytic ativity is 60-80% of the activity of the wild-type enzyme, caseinolytic activity is 60-80% of the activity of the wild-type enzyme, activity with SulA-MBP fusion protein is less than 20% of the activity of the wild-type enzyme, ATPase activity is 60-80% of the activity of the wild-type enzyme
DELTA137-150
2 Gly linker, amidolytic ativity, caseinolytic activity, activity with SulA-MBP fusion protein and ATPase activity are unchanged
DELTA175-209
2 Gly linker, amidolytic ativity, caseinolytic activity, and ATPase activity are unchanged, activity with the SalU-MBP fusion protein is less than 20% of the activity of the wild-type enzyme
DELTA423-443
5 Gly insertion, no amidolytic activity, no activity with casein and SulA-MBP fusion protein, no ATPase activity
DELTA88-92
3 Gly linker, amidolytic ativity, caseinolytic activity, activity with SulA-MBP fusion protein and ATPase activity are less than 20% of the activity of the wild-type enzyme
DELTA89-92
1 Gly linker, amidolytic ativity is 40-60% of the activity of the wild-type enzyme, caseinolytic activity is 40-60% of the activity of the wild-type enzyme, activity with SulA-MBP fusion protein is less than 20% of the activity of the wild-type enzyme, ATPase activity is 40-60% of the activity of the wild-type enzyme
E193L/E194L
-
clpY mutant, the mutant shows altered interaction with SulA substrates, wild-type and mutant, and altered induction by arabinose or glutamate compared to the wild-type, overview
E266Q
amidolytic ativity, caseinolytic activity, activity with SulA-MBP fusion protein and ATPase activity are unchanged
E266Q/E385
amidolytic ativity, caseinolytic activity, activity with SulA-MBP fusion protein and ATPase activity are unchanged
E286Q
amidolytic ativity is 40-60% of the activity of the wild-type enzyme, caseinolytic activity is 40-60% of the activity of the wild-type enzyme, activity with SulA-MBP fusion protein is 40-60% of the activity of the wild-type enzyme, ATPase activity is unchanged
E321Q
amidolytic ativity, caseinolytic activity, activity with SulA-MBP fusion protein and ATPase activity is less than 20% of the activity of the wild-type enzyme
E325E
amidolytic ativity, caseinolytic activity, activity with SulA-MBP fusion protein and ATPase activity are less than 20% of the activity of the wild-type enzyme. Crystal structure of the mutant complex is nearly identical to then active complex
E436K/D437K
amidolytic ativity is 60-80% of the activity of the wild-type enzyme, caseinolytic activity is unchanged, activity with SulA-MBP fusion protein is less than 20% of the activity of the wild-type enzyme, ATPase activity is unchanged
E88Q
amidolytic ativity is 20-40% of the activity of the wild-type enzyme, caseinolytic activity is less than 20% of the activity of the wild-type enzyme, activity with SulA-MBP fusion protein is less than 20% of the activity of the wild-type enzyme, ATPase activity is unchanged
E88Q/E266Q
amidolytic ativity is 20-40% of the activity of the wild-type enzyme, caseinolytic activity is less than 20% of the activity of the wild-type enzyme, activity with SulA-MBP fusion protein is less than 20% of the activity of the wild-type enzyme, ATPase activity is unchanged
E95W
amidolytic activity, activity with casein and ATPase activity are unchanged, activity with SulA-MBP fusion protein is 20-40% of the activity of the wild-type enzyme
G90P
-
mutation of the GYVG motif residues affects protein unfolding, ATP hydrolysis, affinity for ADP, and interaction of HslU and HslV, overview, the mutant shows 41% reduced ATP hydrolysis activity compared to wild-type HslU
G93A
G93P
-
mutation of the GYVG motif residues affects protein unfolding, ATP hydrolysis, affinity for ADP, and interaction of HslU and HslV, overview
I186N
-
clpY mutant, the mutant does not interact with SulA compared to the wild-type ClpY
I312W
amidolytic ativity, caseinolytic activity, activity with SulA-MBP fusion protein and ATPase activity are higher than the wild-type activities
Ins(435,436)
5 Gly insertion, no amidolytic activity, no activity with casein and SulA-MBP fusion protein, no ATPase activity
K80T
amidolytic ativity is 20-40% of the activity of the wild-type enzyme, caseinolytic activity is 40-60% of the activity of the wild-type enzyme, activity with SulA-MBP fusion protein is unchanged, ATPase activity is unchanged
L199Q
M187I
-
clpY mutant, the mutant shows altered interaction with SulA substrates, wild-type and mutant, and altered induction by arabinose or glutamate compared to the wild-type, overview
N141L/N142L
-
the ClpY loop 1 mutant is defective in complete degradation of SulA
N205K
-
clpY mutant, the mutant shows altered interaction with SulA substrates, wild-type and mutant, and altered induction by arabinose or glutamate compared to the wild-type, overview
Q148L/Q149L/Q150L
-
the ClpY loop 1 mutant shows altered substrate recognition and binding, but shows normal activity similar to that of the wild-type ClpY
Q198L/Q200L
-
clpY mutant, the mutant shows altered interaction with SulA substrates, wild-type and mutant, and altered induction by arabinose or glutamate compared to the wild-type, overview
Q311_I312insGGGGG
5 Gly insertion, amidolytic ativity, caseinolytic activity and activity with SulA-MBP fusion protein are less than 20% of the activity of the wild-type enzyme, ATPase activity is 20-40% of the activity of the wild-type enzyme
R393A
amidolytic ativity, caseinolytic activity, activity with SulA-MBP fusion protein and ATPase activity is less than 20% of the activity of the wild-type enzyme
R86G
-
ATP inhibits the degradation of unfolded proteins by HslV. This inhibitory effect of ATP is markedly diminished by substitution of the Arg86 residue located in the apical pore of HslV with Gly
T387_E388insGGGGG
5 Gly insertion, amidolytic ativity is unchanged, caseinolytic activity is 60-80% of the activity of the wild-type enzyme, ATPase activity is unchanged
V92A
-
mutation of the GYVG motif residues affects protein unfolding, ATP hydrolysis, affinity for ADP, and interaction of HslU and HslV, overview
V92G
amidolytic activity, activity with casein and ATPase activity are unchanged, activity with SulA-MBP fusion protein is less than 20% of the activity of the wild-type enzyme
V92I
-
mutation of the GYVG motif residues affects protein unfolding, ATP hydrolysis, affinity for ADP, and interaction of HslU and HslV, overview
V92S
-
mutation of the GYVG motif residues affects protein unfolding, ATP hydrolysis, affinity for ADP, and interaction of HslU and HslV, overview
Y91A
Y91F
Y91G
amidolytic ativity is 40-60% of the activity of the wild-type enzyme, caseinolytic activity is 40-60% of the activity of the wild-type enzyme, activity with SulA-MBP fusion protein is less than 20% of the activity of the wild-type enzyme, ATPase activity is unchanged
Y91S
-
mutation of the GYVG motif residues affects protein unfolding, ATP hydrolysis, affinity for ADP, and interaction of HslU and HslV, overview
additional information
G93A
amidolytic ativity is 20-40% of the activity of the wild-type enzyme, caseinolytic activity is 20-40% of the activity of the wild-type enzyme, activity with SulA-MBP fusion protein is less than 20% of the activity of the wild-type enzyme, ATPase activity is 40-60% of the activity of the wild-type enzyme
G93A
-
mutation of the GYVG motif residues affects protein unfolding, ATP hydrolysis, affinity for ADP, and interaction of HslU and HslV, overview
L199Q
-
clpY mutant, the mutant shows altered interaction with SulA substrates, wild-type and mutant, and altered induction by arabinose or glutamate compared to the wild-type, overview. SulA accumulates in the bacterial cells that express ClpY
L199Q
P0A6H5; P0A7B8
substitution in I-domain of subunit HslU. Mutation does not alter the structure of the AAA+ ring or its interactions with HslV but increases I-domain susceptibility to limited endoproteolysis. The mutation increases the rate of ATP-hydrolysis substantially, results in slower degradation of some proteins but faster degradation of other substrates, and markedly changes the preference of HslUV for initiating degradation at the N-terminus or C-terminus of model substrates
Y91A
-
mutation of the GYVG motif residues affects protein unfolding, ATP hydrolysis, affinity for ADP, and interaction of HslU and HslV, overview
Y91A
-
site-directed mutagenesis of the HslU GYVG pore loop, the mutant shows no remaining activity, the mutant hydrolyzes ATP and stimulates HslV peptidase activity
Y91F
-
mutation of the GYVG motif residues affects protein unfolding, ATP hydrolysis, affinity for ADP, and interaction of HslU and HslV, overview
Y91F
-
site-directed mutagenesis of the HslU GYVG pore loop, the mutant shows reduced activity, the mutant hydrolyzes ATP and stimulates HslV peptidase activity
additional information
-
clpQ+Y+ promoter is fused to a lacZ reporter gene. The transcriptional or translational clpQ+::lacZ fusion gene is each crossed into lambda phage. The lambdaclpQ+::lacZ+, a transcriptional fusion gene, is used to form lysogens in the wild-type, rpoH or/and rpoS mutants. Upon shifting the temperature up from 30°C to 42°C, the wild-type transcriptional lambdaclpQ+::lacZ+ demonstrates an increased beta-galactosidase activity, overview. RpoH itself regulates clpQ+Y+ gene expression. The clpQ+Y+ message carries a conserved 71 bp at the 5'-untranslated region that is predicted to form the stem-loop structure by analysis of its RNA secondary structure
additional information
-
construction of mixed dodecamers having varied numbers of HslV and T1A subunits, and of a series of HslV dodecamers containing different numbers of active sites showing that HslV with only 6 active sites is sufficient to support full catalytic activity, a further reduction of the number of active sites leads to a proportional decrease in activity. Substrate-mediated stabilization of the HslV-HslU interaction remains unchanged until the number of the active sites is decreased to 6 but is gradually compromised upon further reduction. Deletion of Thr1 causes a dramatic increase in affinity between HslV and HslU
additional information
-
construction of truncation mutants lacking the substrate binding residues 137-209 of ClpY
additional information
-
construction of deletion mutants DELTA175-209linker, DELTA175-209GG, and DELTA108-243GG
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, stable for at least 1 month in presence of 20% glycerol and 1 mM dithiothreitol
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged HslU and HslUV from strain BB101 by nickel affinity and ion exchange chromatography, and gel filtration
-
recombinant His-tagged HslU and HslV from Escherichia coli by nickel affinity chromatography and gel filtration
-
recombinant His-tagged wild-type and mutant enzymes from BW25113 DELTAhslVU::kan cells by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
the amplified fragment coding for HslV-EFHHHHHH is cloned into pET12b usind restriction sites Nde and SalI, expression in Escherichia coli
expression of His-tagged wild-type and mutant enzymes in BW25113 DELTAhslVU::kan cells
-
expression of wild-type and mutant enzyme sin Saccharomyces cerevisiae strain EGY48 containing plasmid BD-sulA or BD-sulA mutant M89I
-
gene clpQY or hslVU, expression of diverse gene constructs, e.g. as lacZ fusion constructs, and of truncated variants, in AC3112 cells, analysis of regulation of gene expression, overview. The stem-loop secondary structure of 5'-UTR of clpQ+Y+ is responsible for its mRNA stability
-
genes clpQ and clpY, DNA sequence determination, overexpression in a Lon protease-deficient mutant strain suppresses expression of the cps gene and of mucoid phenotype
-
genes clpY, co-expression of ClpQ and ClpY mutants in AC3112 cells. Co-expression of ClpY with HA-tagged SulA and mutant SulA M89I, RcsA, RpoH, and TraJ molecules in the yeast two-hybrid system, expression of recombinant ClpYQ mutants
-
mutant enzymes K80T, E286Q, E312Q, R325E, R393A, DELTA137-150, DELTA175-209, DELTA111-239, E266Q, Es66Q/E385K, I312W, ins(264,265), Ins(311, 312), Ins(387,388), Ins(435,436), DELTA432-443, E436A/D437A, E436K/D437K, E88Q, E88Q/E266Q, Y91G, V92G, G93A, E95W, DELTA88-92, DELTA89-92
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Welch, R.A.; Burland, V.; Plunkett, G.III; Redford, P.; Roesch, P.; Rasko, D.; Buckles, E.L.; Liou, S.R.; Boutin, A.; Hackett, J.; Stroud, D.; Mayhew, G.F.; Rose, D.J.; Zhou, S.; Schwartz, D.C.; Perna, N.T.; Mobley, H.L.T.; Donnenberg, M.S.; Blattner, F.R.
Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli
Proc. Natl. Acad. Sci. USA
99
17020-17024
2002
Escherichia coli (P0A7B9)
Plunkett, G.3rd; Burland, V.; Daniels, D.L.; Blattner, F.R.
Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes
Nucleic Acids Res.
21
3391-3398
1993
Escherichia coli (P0A7B8)
Perna, N.T.; Plunkett, G.; Burland, V.; Mau, B.; Glasner, J.D.; et al.
Genome sequence of enterohaemorrhagic Escherichia coli O157:H7
Nature
409
529-533
2001
Escherichia coli (P0A7C0)
Hayashi, T.; Makino, K.; Ohnishi, M.; Kurokawa, K.; Ishii, K.; et al.
Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12
DNA Res.
8
11-22
2001
Escherichia coli (P0A7C0)
Bochtler, M.; Ditzel, L.; Groll, M.; Huber, R.
Crystal structure of heat shock locus V (HslV) from Escherichia coli
Proc. Natl. Acad. Sci. USA
94
6070-6074
1997
Escherichia coli (P0A7B8), Escherichia coli
Bochtler, M.; Hartmann, C.; Song, H.K.; Bourenkov, G.P.; Bartunik, H.D.; Huber R.
The structures of HslU and the ATP-dependent protease HslU-HslV
Nature
403
800-805
2000
Escherichia coli (P0A7B8), Escherichia coli
Chuang, S.E.; Burland, V.; Plunkett, G.III; Daniels, D.L.; Blattner, F.R.
Sequence analysis of four new heat-shock genes constituting the hslTS/ibpAB and hslVU operons in Escherichia coli
Gene
134
1-6
1993
Escherichia coli (P0A7B8)
Yoo, S.J.; Shim, Y.K.; Seong, I.S.; Seol, J.H.; Kang, M.S.; Chung, C.H.
Mutagenesis of two N-terminal Thr and five Ser residues in HslV, the proteolytic component of the ATP-dependent HslVU protease
FEBS Lett.
412
57-60
1997
Escherichia coli (P0A7B8), Escherichia coli
Yoo, S.J.; Seol, J.H.; Shin, D.H.; Rohrwild, M.; Kang, M.S.; Tanaka, K.; Goldberg, A.L.; Chung, C.H.
Purification and characterization of the heat shock proteins HslV and HslU that form a new ATP-dependent protease in Escherichia coli
J. Biol. Chem.
271
14035-14040
1996
Escherichia coli
Yoo, S.J.; Seol, J.H.; Seong, I.S.; Kang, M.S.; Chung, C.H.
ATP binding, but not its hydrolysis, is required for assembly and proteolytic activity of the HslVU protease in Escherichia coli
Biochem. Biophys. Res. Commun.
238
581-585
1997
Escherichia coli
Bochtler, M.; Song, H.K.; Hartmann, C.; Ramachandran, R.; Huber, R.
The quaternary arrangement of HslU and HslV in a cocrystal: a response to Wang, Yale
J. Struct. Biol.
135
281-293
2001
Escherichia coli
Bogyo, M.; McMaster, J.S.; Gaczynska, M.; Tortorella, D.; Goldberg, A.L.; Ploegh, H.
Covalent modification of the active site threonine of proteasomal beta subunits and the Escherichia coli homolog HslV by a new class of inhibitors
Proc. Natl. Acad. Sci. USA
94
6629-6634
1997
Escherichia coli
Huang, H.; Goldberg, A.L.
Proteolytic activity of the ATP-dependent protease HslVU can be uncoupled from ATP hydrolysis
J. Biol. Chem.
272
21364-21372
1997
Escherichia coli
Lee, Y.Y.; Chang, C.F.; Kuo, C.L.; Chen, M.C.; Yu, C.H.; Lin, P.I.; Wu, W.F.
Subunit oligomerization and substrate recognition of the Escherichia coli ClpYQ (HslUV) protease implicated by in vivo protein-protein interactions in the yeast two-hybrid system
J. Bacteriol.
185
2393-2401
2003
Escherichia coli
Seong, I.S.; Kang, M.S.; Choi, M.K.; Lee, J.W.; Koh, O.J.; Wang, J.; Eom, S.H.; Chung, C.H.
The C-terminal tails of HslU ATPase act as a molecular switch for activation of HslV peptidase
J. Biol. Chem.
277
25976-25982
2002
Escherichia coli
Nishii, W.; Takahashi, K.
Determination of the cleavage sites in SulA, a cell division inhibitor, by the ATP-dependent HslVU protease from Escherichia coli
FEBS Lett.
553
351-354
2003
Escherichia coli
Rohrwild, M.; Coux, O.; Huang, H.C.; Moerschell, R.P.; Yoo, S.J.; Seol, J.H.; Chung, C.H.; Goldberg, A.L.
HslV-HslU: A novel ATP-dependent protease complex in Escherichia coli related to the eukaryotic proteasome
Proc. Natl. Acad. Sci. USA
93
5808-5813
1996
Escherichia coli
Slominska, M.; Wahl, A.; Wegrzyn, G.; Skarstad, K.
Degradation of mutant initiator protein DnaA204 by proteases ClpP, ClpQ and Lon is prevented when DNA is SeqA-free
Biochem. J.
370
867-871
2003
Escherichia coli
Seong, I.S.; Oh, J.Y.; Yoo, S.J.; Seol, J.H.; Chung, C.H.
ATP-dependent degradation of SulA, a cell division inhibitor, by the HslVU protease in Escherichia coli
FEBS Lett.
456
211-214
1999
Escherichia coli
Song, H.K.; Hartmann, C.; Ramachandran, R.; Bochtler, M.; Behrendt, R.; Moroder, L.; Huber, R.
Mutational studies on HslU and its docking mode with HslV
Proc. Natl. Acad. Sci. USA
97
14103-14108
2000
Escherichia coli, Escherichia coli (Q8FBC0)
Wang, J.
A corrected quaternary arrangement of the peptidase HslV and atpase HslU in a cocrystal structure
J. Struct. Biol.
134
15-24
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