3.4.25.2: HslU-HslV peptidase
This is an abbreviated version!
For detailed information about HslU-HslV peptidase, go to the full flat file.
Word Map on EC 3.4.25.2
Reaction
ATP-dependent cleavage of peptide bonds with broad specificity. =
Synonyms
AAA+ HslUV protease, AAA+ protease HslUV, ATP-dependent protease, ATP-dependent protease hslV, ClpQ, ClpQY, ClpYQ, ClpYQ complex, ClpYQ protease, CodW, CodW-CodX, heat shock protein hslV, HslU ATPase, HslU chaperone, HslU/HslV, HslUV, HslUV complex, HslUV protease, HslUV protease-chaperone complex, HslV, HslV peptidase, HslV protease, HslV-HslU, hslVU, HslVU ATP-dependent protease, HslVU protease, LINF_150005800, PfHslUV, T01.006
ECTree
3.4.25.2 HslU-HslV peptidaseAdvanced search results
results (
results (Engineering
Engineering on EC 3.4.25.2 - HslU-HslV peptidase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
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
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
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
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
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
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
