Information on EC 3.4.25.2 - HslU-HslV peptidase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
3.4.25.2
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RECOMMENDED NAME
GeneOntology No.
HslU-HslV peptidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP-dependent cleavage of peptide bonds with broad specificity.
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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-
-
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CAS REGISTRY NUMBER
COMMENTARY hide
178303-43-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain K12
SwissProt
Manually annotated by BRENDA team
strain O6:H1, ATCC 700928
SwissProt
Manually annotated by BRENDA team
proteolytic and regulatory subunits
Q4Q116 and Q4QI03
UniProt
Manually annotated by BRENDA team
proteolytic and regulatory subunits
Q4Q116 and Q4QI03
UniProt
Manually annotated by BRENDA team
strain 2457T, ATCC 700930
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-
Manually annotated by BRENDA team
strain 301 serotype 2a
SwissProt
Manually annotated by BRENDA team
wild-type strain 8325-4, and mutant clpP-defective strain SaDELTAclpP
-
-
Manually annotated by BRENDA team
proteolytic and regulatory subunits
Q383Q5 and Q57VB1 and Q382V8
UniProt
Manually annotated by BRENDA team
; strain Berenice 62; strain Berenice 78
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-
Manually annotated by BRENDA team
strain Berenice 62
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-
Manually annotated by BRENDA team
strain Berenice 78
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-casein + H2O
?
show the reaction diagram
Arc + H2O
?
show the reaction diagram
Arc mutant I137A + H2O
?
show the reaction diagram
-
monomeric mutant, degradation
-
-
?
Arc repressor + H2O
?
show the reaction diagram
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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
-
-
?
Arc-MYL-st11 + H2O
?
show the reaction diagram
-
recombinant Arc fusion protein
-
-
?
Arc-MYL-st11 plus + H2O
?
show the reaction diagram
-
recombinant Arc fusion protein
-
-
?
Arc-st11-ssrA + H2O
?
show the reaction diagram
Arc-st11-ssrADD + H2O
?
show the reaction diagram
-
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
-
-
?
Arc/I37A + H2O
?
show the reaction diagram
-
-
-
-
?
Arc1-53-st11-titin-ssrA + H2O
?
show the reaction diagram
-
recombinant truncated Arc fusion protein
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
barnase-DHFR fusion proteins + H2O
?
show the reaction diagram
benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-GGL + 7-amino-4-methylcoumarin
show the reaction diagram
benzyloxycarbonyl-Gly-Gly-Leu-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
carbobenzoxy-Gly-Gly-Leu-7-amido-4-methyl coumarin + H2O
carbobenzoxy-Gly-Gly-Leu + 7-amino-4-methyl coumarin
show the reaction diagram
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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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-
?
carbobenzoxy-Gly-Gly-Leu-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Gly-Gly-Leu + 7-amino-4-methylcoumarin
show the reaction diagram
carboxymethylated lactalbumin + H2O
?
show the reaction diagram
-
-
-
-
?
casein + H2O
?
show the reaction diagram
DnaA204-protein + H2O
?
show the reaction diagram
-
the degradation of the DnaA204 protein contributes to the temperature sensitivity of the dna204 strain
-
-
?
fusion protein of SulA and maltose-binding protein + H2O
?
show the reaction diagram
-
-
-
-
?
gt1 + H2O
?
show the reaction diagram
-
substrate of HslU
-
-
?
Insulin B-chain + H2O
?
show the reaction diagram
lambda CI repressor ext1-lambdacIN-RSEYE + H2O
?
show the reaction diagram
-
-
-
-
?
lambda cI repressor mutant ext1-lambdacIN-ISVTL + H2O
?
show the reaction diagram
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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
-
-
?
MBP-SulA + H2O
?
show the reaction diagram
-
-
-
-
?
N-carbobenzoxy-Gly-Gly-Leu-7-amido-4-methylcoumarin + H2O
N-carbobenzoxy-Gly-Gly-Leu + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
N-carbobenzyloxy-Gly-Gly-Leu-7-amido-4-methylcoumarin + H2O
N-carbobenzyloxy-Gly-Gly-Leu + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
puromycylpolypeptide + H2O
?
show the reaction diagram
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HslV and HslU interact and participate in the degradation of misfolded puromycylpolypeptides
-
-
?
RcsA + H2O
?
show the reaction diagram
RpoH + H2O
?
show the reaction diagram
-
RpoH is a heat shock sigma transcription factor
-
-
?
succinyl-LLVY-7-amido-4-methylcoumarin + H2O
succinyl-LLVY + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
SulA + H2O
?
show the reaction diagram
SulA-maltose binding protein-fusion protein + H2O
?
show the reaction diagram
TraJ + H2O
?
show the reaction diagram
unfolded lactalbumin + H2O
?
show the reaction diagram
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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
?
show the reaction diagram
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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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-
?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Arc + H2O
?
show the reaction diagram
-
N-terminal residues of Arc are important for HslUV degradation
-
-
?
DnaA204-protein + H2O
?
show the reaction diagram
-
the degradation of the DnaA204 protein contributes to the temperature sensitivity of the dna204 strain
-
-
?
lambda CI repressor ext1-lambdacIN-RSEYE + H2O
?
show the reaction diagram
-
-
-
-
?
puromycylpolypeptide + H2O
?
show the reaction diagram
-
HslV and HslU interact and participate in the degradation of misfolded puromycylpolypeptides
-
-
?
RcsA + H2O
?
show the reaction diagram
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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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-
?
SulA + H2O
?
show the reaction diagram
TraJ + H2O
?
show the reaction diagram
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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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5'-adenylyl beta,gamma-imidotriphosphate
adenosine 5'-(alpha,beta-methylene)triphosphate
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HslVU degrades insulin B-chain more rapidly in the presence of ATPgammaS than with ATP
ATPgammaS
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HslVU degrades insulin B-chain more rapidly in the presence of ATPgammaS than with ATP
beta,gamma-Imido-ATP
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supports proteolytic activity to an extent less than 10% of that seen with ATP
additional information
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CaCl2
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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+
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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
MgCl2
-
allows some peptidase and caseinase activity in the absence of any nucleotide
MnCl2
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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+
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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
additional information
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HslU requires Mg2+ together with ATP for activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3,4-dichloroisocoumarin
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0.2 mM, 50% inhibition
acety-Leu-Leu-norleucinal
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0.01 mM, 90% inhibition
ADP
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when added together with ATP
benzyloxycarbonyl-Ile-Glu(tert-butyl)-Ala-Leu-al
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0.001 mM, almost complete inhibition of peptidase activity, no inhibition of hydrolysis of insulin B-chain or other polypeptide substrates
benzyloxycarbonyl-Leu-Leu-norleucinal
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0.01 mM, 97% inhibition
benzyloxycarbonyl-Leu-Leu-norvalinal
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0.004 mM, inhibits hydrolysis of both benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin and insulin B-chain to a similar extent
diisopropyl fluorophosphate
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10 mM, about 70% inhibition
dithiothreitol
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lactacystin
N-acetyl-Leu-Leu-norleucinal
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i.e. calpain inhibitor-I, inhibits HslV
NLVS
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in the presence of ATP, the proteasome inhibitor markedly increases the interaction between HslV and HslU and causes the activation of the HslU ATPase
phenylmethylsulfonyl fluoride
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-(3,4-dihydroxyphenyl)-2-[2-(pyridin-2-yl)-1H-benzimidazol-1-yl]ethanone
1-(4-nitrophenyl)-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
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HslU ATPase
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N'-[(E)-(4-oxo-4H-chromen-2-yl)methylidene]benzohydrazide
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0052
Arc-MYL-st11
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pH 7.6, 37C, HslUV
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0.04
Arc-MYL-st11 plus
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pH 7.6, 37C, HslUV
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0.02 - 0.125
Arc-st11-ssrA
-
0.004
Arc1-53-st11-titin-ssrA
-
pH 7.6, 37C, HslUV
-
0.014
Insulin B-chain
-
pH 8, 37C
0.0023
SulA
-
pH 5.5, 37C, wild-type SulA, recombinant enzyme
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0.0034
SulA mutant F10A
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pH 5.5, 37C, recombinant enzyme
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0.0032
SulA mutant I37V
-
pH 5.5, 37C, recombinant enzyme
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0.001
SulA mutant P8L
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pH 5.5, 37C, recombinant enzyme
-
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.11
Arc-MYL-st11
Escherichia coli
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pH 7.6, 37C, HslUV
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0.077
Arc-MYL-st11 plus
Escherichia coli
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pH 7.6, 37C, HslUV
-
0.11
Arc1-53-st11-titin-ssrA
Escherichia coli
-
pH 7.6, 37C, HslUV
-
0.05
SulA
Haemophilus influenzae
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pH 5.5, 37C, wild-type SulA, recombinant enzyme
-
0.063
SulA mutant F10A
Haemophilus influenzae
-
pH 5.5, 37C, recombinant enzyme
-
0.068
SulA mutant I37V
Haemophilus influenzae
-
pH 5.5, 37C, recombinant enzyme
-
0.033
SulA mutant P8L
Haemophilus influenzae
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pH 5.5, 37C, recombinant enzyme
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
7.6
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain 55989 / EAEC)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
19000
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x * 19000, HslV protein, SDS-PAGE
19095
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x * 19095, calculation from nucleotide sequence
20000
-
12 * 20000, SDS-PAGE
23500
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12 * 23500, calculated from amino acid sequence
190000
-
gel filtration
220000
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ClpQ in presence of ATP; gel filtration
230000
-
HslV protease component
250000
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purified HslV in presence or absence of ATP, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
wild-type enzyme
dodecamer
hexamer
homododecamer
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12 * 20000, SDS-PAGE
monomer
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recombinant mutant I37A, predominantly
oligomer
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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
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant CodX and CodW and hybrid complexes with Escherichia coli 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
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sitting drop vapor diffusion method
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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
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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
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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
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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
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quarternary arrangement of hslU and hslV in a cocrystal
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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
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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
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wild-type or HslV-HsvU complexed with resorufin casein, hanging-drop vapor diffusion method
asymmetric HslU(DELTAI)6HslV12 complex.HslV can be activated by binding of a hexameric HslU(DELTAI)6 ring lacking the I domain
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
rapid freezing and thawing inactivates
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70C, stable for at least 1 month in presence of 20% glycerol and 1 mM dithiothreitol
-
4C rapid inactivation in absence of dithiothreitol
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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recombinant His-tagged HslU and HslUV from strain BB101 by nickel affinity and ion exchange chromatography, and gel filtration
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recombinant His-tagged HslU and HslV from Escherichia coli by nickel affinity chromatography and gel filtration
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recombinant His-tagged wild-type and mutant enzymes from BW25113 DELTAhslVU::kan cells by nickel affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BW21135 cells
-
expressed in Escherichia coli KY2266 cells
-
expression of His-tagged HslU and HslV in Escherichia coli
-
expression of His-tagged wild-type and mutant enzymes in BW25113 DELTAhslVU::kan cells
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expression of wild-type and mutant enzyme sin Saccharomyces cerevisiae strain EGY48 containing plasmid BD-sulA or BD-sulA mutant M89I
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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
-
gene clpY and gene clpQ, DNA and amino acid sequence determination and analysis, subcloning and expression in Escherichia coli strain DH5alpha
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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
-
HslU and HslV were coexpressed in BL21 (DE3) pLysS cells
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
overexpression of His-tagged HslU and HslUV in strain BB101
-
the amplified fragment coding for HslV-EFHHHHHH is cloned into pET12b usind restriction sites Nde and SalI, expression in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
E61C
-
clpQ mutant
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
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
-
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
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
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
R86A
-
the mutant shows little peptidolytic activity compared to the wild type
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
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
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
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
DELTA83-92
-
hydrolysis of casein, SulA-MBP or benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin is less than 20% of the activity of the wild-type enzyme
DELTA86-91
-
hydrolysis of casein, SulA-MBP or benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin is unchanged
K28A
-
hydrolysis of casein, SulA-MBP or benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin is less than 20% of the activity of the wild-type enzyme
R35A
-
hydrolysis of casein, SulA-MBP or benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin is less than 20% of the activity of the wild-type enzyme
R86D
-
hydrolysis of casein, SulA-MBP or benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin is less than 20% of the activity of the wild-type enzyme
R89A/K90A
-
hydrolysis of casein, SulA-MBP or benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin is less than 20% of the activity of the wild-type enzyme
R89D
-
hydrolysis of casein, SulA-MBP or benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin is 40-60% of the activity of the wild-type enzyme
R89D/K90E
-
hydrolysis of casein and SulA-MBP is less than 20% of the activity of the wild-type enzyme, hydrolysis of benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin is higher than that of the wild-type enzyme
V112A
-
hydrolysis of casein, SulA-MBP or benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin is less than 20% of the activity of the wild-type enzyme
additional information
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