Information on EC 3.4.24.B20 - FtsH protease

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

EC NUMBER
COMMENTARY hide
3.4.24.B20
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
FtsH protease
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
degradative cleavage of proteins
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY hide
253850-13-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Uniprot
Manually annotated by BRENDA team
gene ftsH
-
-
Manually annotated by BRENDA team
apple proliferation phytoplasma
-
-
Manually annotated by BRENDA team
isoform FtsH1
UniProt
Manually annotated by BRENDA team
gene ftsH
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
strains SS120 and MIT9313, representing two ecotypes belonging to the low-light-adapted ecotype subclades II and IV, respectively
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-
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
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
23 kDa fragment of photosystem II D1 protein + H2O
?
show the reaction diagram
alpha-casein + H2O
?
show the reaction diagram
-
ATP is required for the reaction. The enzyme is unable to degrade the substrate in the presence of AMPPNP
-
-
?
Anabaena apoflavodoxin + H2O
?
show the reaction diagram
beta-casein + H2O
?
show the reaction diagram
-
-
-
?
casein + H2O
?
show the reaction diagram
D1 protein + H2O
?
show the reaction diagram
damaged PSII D1 protein + H2O
?
show the reaction diagram
delta32 protein + H2O
?
show the reaction diagram
-
-
-
-
?
Fur repressor protein + H2O
?
show the reaction diagram
degraded by the FtsH1/FtsH3 complex
-
-
?
GgpS protein + H2O
?
show the reaction diagram
-
soluble substrate
-
-
?
H+-ATPase F0alpha + H2O
?
show the reaction diagram
-
membrane substrate of FtsH
-
-
?
heat shock transcription factor sigma 32 + H2O
?
show the reaction diagram
-
-
-
-
?
lambdaCII + H2O
?
show the reaction diagram
light-harvesting complex II + H2O
?
show the reaction diagram
-
AtFtsH6 is involved in the degradation of the light-harvesting complex II during high-light acclimation and senescence
-
-
?
LpxC + H2O
?
show the reaction diagram
-
cytosolic substrate of FtsH
-
-
?
photodamaged D1 protein + H2O
?
show the reaction diagram
photodamaged D2 protein + H2O
?
show the reaction diagram
-
-
-
-
?
photosystem II reaction center subunit D1 + H2O
?
show the reaction diagram
photosystem II reaction center subunit D2 + H2O
?
show the reaction diagram
-
FtsH has a key role in the repair of UVB-damaged photosystem II
-
-
?
Protein + H2O
?
show the reaction diagram
protein + H2O
peptides
show the reaction diagram
protein D1 + H2O
?
show the reaction diagram
protein D2 + H2O
?
show the reaction diagram
-
-
-
-
?
protein lambdaCII + H2O
?
show the reaction diagram
-
-
-
-
?
protein sigma32 + H2O
?
show the reaction diagram
-
-
-
-
?
proteins + H2O
peptides
show the reaction diagram
-
-
?
PsbA protein + H2O
?
show the reaction diagram
-
-
-
-
?
reaction center D1 protein + H2O
23-kDa N-terminal fragments of reaction center D1 protein
show the reaction diagram
-
-
-
-
?
Rieske FeS protein + H2O
?
show the reaction diagram
-
degradation of membrane protein, essentially required as a membrane-integrated quality control
-
?
RNase colicin D + H2O
?
show the reaction diagram
RNase colicin E3 + H2O
?
show the reaction diagram
RpoH + H2O
?
show the reaction diagram
sigma32 + H2O
?
show the reaction diagram
-
substrate from Escherichia coli
-
-
?
Spo0E + H2O
?
show the reaction diagram
subunit SecY of the SecAEG translocase + H2O
?
show the reaction diagram
-
membrane substrate of FtsH
-
-
?
unassembled cytochrome b6f complex + H2O
?
show the reaction diagram
-
-
-
?
unassembled Rieske FeS protein + H2O
?
show the reaction diagram
-
recombinant wild-type protein and mutant C162S, recombinant protein substrate is imported in vitro into intact Pisum sativum chloroplasts
-
?
YccA + H2O
?
show the reaction diagram
-
membrane substrate of FtsH
-
-
?
additional information
?
-
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
23 kDa fragment of photosystem II D1 protein + H2O
?
show the reaction diagram
Anabaena apoflavodoxin + H2O
?
show the reaction diagram
-
FtsH degradation of 31 point mutants of Anabaena apoflavodoxin is inversely proportional to their conformational stabilities. FtsH degrades the apo form of Anabaena flavodoxin, but it is unable to hydrolyze the holo form, activities with fully and partly unfolded substrate protein, overview
-
-
?
D1 protein + H2O
?
show the reaction diagram
damaged PSII D1 protein + H2O
?
show the reaction diagram
delta32 protein + H2O
?
show the reaction diagram
-
-
-
-
?
Fur repressor protein + H2O
?
show the reaction diagram
P72991, P73179, P73437, Q55700
degraded by the FtsH1/FtsH3 complex
-
-
?
heat shock transcription factor sigma 32 + H2O
?
show the reaction diagram
-
-
-
-
?
lambdaCII + H2O
?
show the reaction diagram
-
the key protein that influences the lysis/lysogeny decision of lambda by activating several phage promoters
-
-
?
light-harvesting complex II + H2O
?
show the reaction diagram
-
AtFtsH6 is involved in the degradation of the light-harvesting complex II during high-light acclimation and senescence
-
-
?
photodamaged D1 protein + H2O
?
show the reaction diagram
photodamaged D2 protein + H2O
?
show the reaction diagram
-
-
-
-
?
Protein + H2O
?
show the reaction diagram
protein + H2O
peptides
show the reaction diagram
protein D1 + H2O
?
show the reaction diagram
protein D2 + H2O
?
show the reaction diagram
-
-
-
-
?
proteins + H2O
peptides
show the reaction diagram
O80860
-
-
?
PsbA protein + H2O
?
show the reaction diagram
-
-
-
-
?
Rieske FeS protein + H2O
?
show the reaction diagram
-
degradation of membrane protein, essentially required as a membrane-integrated quality control
-
?
RNase colicin D + H2O
?
show the reaction diagram
RNase colicin E3 + H2O
?
show the reaction diagram
RpoH + H2O
?
show the reaction diagram
-
RpoH is rapidly degraded by chaperone-mediated FtsH-dependent proteolysis
-
-
?
Spo0E + H2O
?
show the reaction diagram
-
the Spo0E phosphatase is distinguished from the YisI and YnzD phosphatases by a C-terminal extension of about 25 amino acids, the C-terminal region of Spo0E confers target specificity to FtsH
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-
?
unassembled cytochrome b6f complex + H2O
?
show the reaction diagram
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-
-
?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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required
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-(3,4-dichlorophenyl)-1,1-dimethyl urea
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bromoxynil
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HflC protein
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purified recombinant His6-tagged, 74 kDa dimers from Escherichia coli expressed in strain Bl21, inhibits the proteolysis of lambdaCII by FtsH, i.e. HflB, both in vitro and in vivo, mechanism, overview. Each HflC molecules interacts with another HflC molecule attached to the juxtaposed HflB
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HflK protein
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purified recombinant His6-tagged, 74 kDa dimers from Escherichia coli expressed in strain Bl21, inhibits the proteolysis of lambdaCII by FtsH, i.e. HflB, both in vitro and in vivo, mechanism, overview. Each HflK molecules interacts with another HflK molecule attached to the juxtaposed HflB
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Lincomycin
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o-phenanthroline
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Trypsin
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additional information
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no inhibition by serine and cysteine protease inhibitors
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
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-
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
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assay at
8
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
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assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.11
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slr1640, sequence calculation
5.23
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slr1390, sequence calculation
5.29
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slr0228, sequence calculation
5.31
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sll1463, sequence calculation
5.91
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
isoforms FtsH 7 and 9 are localized in the chloroplast envelope membrane
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Manually annotated by BRENDA team
additional information
-
FtsH co-purifies with PSII complexes in Synechocystis
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65000
-
mature FtsH2
67000
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mature FtsH5
67250
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x * 68199, sll1463, sequence calculation, x * 68496, slr0228, sequence calculation, x * 67250, slr1640, sequence calculation, x * 69304, slr1390, sequence calculation
68199
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x * 68199, sll1463, sequence calculation, x * 68496, slr0228, sequence calculation, x * 67250, slr1640, sequence calculation, x * 69304, slr1390, sequence calculation
68496
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x * 68199, sll1463, sequence calculation, x * 68496, slr0228, sequence calculation, x * 67250, slr1640, sequence calculation, x * 69304, slr1390, sequence calculation
69304
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x * 68199, sll1463, sequence calculation, x * 68496, slr0228, sequence calculation, x * 67250, slr1640, sequence calculation, x * 69304, slr1390, sequence calculation
70709
x * 70709, sequence calculation
71000
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6 * 71000, FtsH forms a barrel-shaped oligomer
72000
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mature enzyme, SDS-PAGE
73198
x * 73198, FtsH8, sequence calculation
74000
-
precursor to FtsH2
74515
x * 74515, FtsH6, sequence calculation
75000
-
precursor to FtsH5
75232
x * 75232, FtsH5, sequence calculation
76000
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full length enzyme, SDS-PAGE
76759
x * 76759, FtsH1, sequence calculation
77000
-
SDS-PAGE
77275
x * 77275, FtsH4, sequence calculation
80000
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x * 78000, mature form, SDS-PAGE, x * 80000, pro-form, SDS-PAGE
87802
x * 87802, FtsH7, sequence calculation
87838
x * 87838, FtsH9, sequence calculation
88717
x * 88717, FtsH11, sequence calculation
89353
x * 89353, FtsH3, sequence calculation; x * 89353, FtsH3, sequence calculation
89555
x * 89555, FtsH10, sequence calculation
100000
6 * 100000, isoform FtsH2-GST fusion protein, SDS-PAGE
104000
-
6 * 104000, GST-tagged FtsH1, SDS-PAGE
115105
x * 115105, FtsH12, sequence calculation
400000 - 480000
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-
410000
gel filtration
450000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterohexamer
hexamer
homohexamer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
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FtsH is subject to selfprocessing and removes its C-terminal 7 amino acid residues
ubiquitylation
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ubiquitylation of FtsH1 by AtCHIP might lead to the degradation of FtsH1 in vivo
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
vapor diffusion method, using either 2 M ammonium sulfate, 0.1 M Tris-HCl pH 8.5, 10 mM EDTA or, as another condition, 60% tacsimate pH 7.0, 10 mM adenylyl imidodiphosphate lithium salt hydrate
cytosolic region of apo-FtsH, microbatch method by mixing equal volumes of 20 mg/ml protein with crystallization buffer containing 30% w/v PEG 400, 200 mM CaCl2, 100 mM HEPES, pH 7.5, 200 mM glycine, and 0.1-0.2% w/v low-melt agarose, 20°C, X-ray diffraction structure determination and analysis at 2.6 A resolution
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
hexameric FtsH is relatively resistant to light stress and heat stress
-
under light stress conditions (intensity, 1 mM of photons m-2 s-1), FtsH hexamers in thylakoids are stable even in longer stress periods
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
glutathione agarose column chromatography and Ni-NTA column chromatography
-
glutathione-agarose resin column chromatography
His-Bind column chromatography
Ni-NTA column chromatography, Resource Q anion-exchange chromatography, and Superdex 16/6000 gel filtration
partially
recombinant amino acids 147-610 of FtsH with K410L-K415A surface mutations, and recombinant G404L and K207A mutants
recombinant as GST-fusion protein from Escherichia coli
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recombinant wild-type enzyme from Escherichia coli strain AR5771
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4 alleles of gene var2, positional cloning, initiation of chromosome walking of the var2 gene on chromosome 2, amino acid sequence determination, mechanism of genetic variation
DNA and amino acid sequence determination and analysis, in vitro translation and import into isolated Pisum sativum chloroplasts, where the enzyme is processed to its mature form and targeted into the thylakoid membrane
expressed in Escherichia coli BL21 cells
expressed in Escherichia coli BL21(DE3) CodonPlus cells
expressed in Escherichia coli C41(DE3) cells
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expressed in Escherichia coli strain BL21(DE3)
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expressed in Escherichia coli strain BW25113; expressed in Escherichia coli strain BW25113; expressed in Escherichia coli strain BW25113; expressed in Escherichia coli strain BW25113
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expressed in Escherichia coli XL1 Blue cells
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expressed in Synechocystis sp. strain PCC6803
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expression of amino acids 147-610 of FtsH with K410L-K415A surface mutations, and expression of G404L and K207A mutants
expression of GST-tagged wild-type and mutant enzymes in Escherichia coli ftsh-deficient strain A8296
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expression of wild-type enzyme in Escherichia coli strain AR5771
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functional expression in Escherichia coli as GST-fusion protein
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gene ftsh, expression in Escherichia coli
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genes ftsH-1, ftsH-2, ftsH-3, and ftsH-4, DNA and amino acid sequence determination and analysis, quantitative real time RT-PCR expression anaylsis
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genetic allelic variants of gene var2, i.e. AtFtsH2, DNA and amino acid sequence determination and analysis
mutant enzymes are expressed in Escherichia coli AR5088 cells
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ZmFtsH2A, DNA and amino acid sequence determination and analysis, expression of ZmFtsH2A in Nicotiana tabacum transgenic plants using the Agrobacterium tumefaciens strain LBA4404 freeze-thaw transfection method. The full length gene is cloned into a binary vector pCAMBIA1300-35SMCSnos-als containing a constitutive CaMV35S promoter, a nos terminiter, and a mutational chlorsulfuron-resistance acetolactate synthase gene from Arabidopsis thaliana; ZmFtsH2B, DNA and amino acid sequence determination and analysis, expression of ZmFtsH2B in Nicotiana tabacum transgenic plants using the Agrobacterium tumefaciens strain LBA4404 freeze-thaw transfection method. The full length gene is cloned into a binary vector pCAMBIA1300-35SMCSnos-als containing a constitutive CaMV35S promoter, a nos terminiter, and a mutational chlorsulfuron-resistance acetolactate synthase gene from Arabidopsis thaliana
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
construction of a DELTAPsbO/DELTASlr0228 double mutant strain that shows the presence of newly synthesized, unassembled D1 protein, especially its non-mature forms pD1 and iD1, not observed in the not in the DELTAPsbO single mutant. Inactivation of the slr0228 gene in the DELTAPsbV strain markedly increases the accumulation the monomeric PSII core complex RCC(1) and RC47 complex, the core complex lacking the inner antenna CP43, but still there is no accumulation of the dimeric PSII core complex RCC(2)
ethyl methanesulfonate can cause loss-of-function mutations in gene var2, D1 degradation is impaired in var2 mutant; the knockout mutant of gene AtFtsH11 shows a phenotype susceptible to high temperature stress
ftsH expression levels are upregulated upon exposure to agents that produce reactive oxygen and nitrogen intermediates and growth in macrophages
phosphatases RapA, RapB, RapE and Spo0E are negative regulators of FtsH
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D326N
-
the mutant does not cleave delta32 protein
G195D
-
the mutant does not cleave delta32 protein
G267D
-
the mutant does not cleave delta32 protein
G302S
-
the mutant does not cleave delta32 protein
G433R
-
the mutant does not cleave delta32 protein
H417L
-
the mutant accumulates about 20% relative to the wild type enzyme and does not cleave delta32 protein
H488L
-
the FtsH2 mutation inhibits zinc binding and inactivates proteolysis
P320L
-
the mutant does not cleave delta32 protein
G404L
site-directed mutagenesis, the mutant is monomeric and inactive in the ATPase assay and possesses only very low proteolytic activity
K207A
site-directed mutagenesis, crystal structure determination
additional information