Information on EC 2.7.13.3 - histidine kinase and Organism(s) Escherichia coli and UniProt Accession P30844

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Escherichia coli
UNIPROT: P30844


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


The taxonomic range for the selected organisms is: Escherichia coli

EC NUMBER
COMMENTARY hide
2.7.13.3
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RECOMMENDED NAME
GeneOntology No.
histidine kinase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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SYSTEMATIC NAME
IUBMB Comments
ATP:protein-L-histidine N-phosphotransferase
This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). A number of histones can act as acceptor.
CAS REGISTRY NUMBER
COMMENTARY hide
99283-67-7
protein-histidine kinases, EC 2.7.13.1, EC 2.7.13.2, and EC 2.7.13.3 are not distinguished in Chemical Abstracts
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the CusS histidine kinase has overall sequence identity to putative metal-sensing HKs such as SilS (56%), CopS (42%), PcoS (38%) and CinS (35%)
malfunction
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the wild-type strain experiences copper susceptibility at 2.75 mM CuSO4, whereas DELTAcusS mutant cells show a phenotype at lower concentrations. The growth defects observed in the DELTAcusS strain can be partially rescued by expression of intact CusS from a plasmid
metabolism
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DcuS and CitA are involved in the regulation of carboxylate 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
ArcA + ATP
?
show the reaction diagram
ATP + histidine kinase EnvZ
ADP + histidine kinase EnvZ N-phospho-L-histidine
show the reaction diagram
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autophosphorylation. Probing catalytically essential domain orientation in histidine kinase EnvZ by targeted disulfide crosslinking
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?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
show the reaction diagram
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?
BvgA + ATP
?
show the reaction diagram
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one hybrid histidine kinase consisting of the BvgS transmitter and HPt domains and of the EvgS receiver domain BvgS-TO-EvgS-R is able to phosphorylate BvgA but not EvgA. In contrast, the hybrid protein consisting of the BvgS transmitter and the EvgS receiver and HPt domains BvgS-T-EvgS-RO is unable to phosphorylate BvgA but efficiently phosphorylates EvgA
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?
DcuR + ATP
?
show the reaction diagram
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the phosphoryl group of DcuS is rapidly transferred to the response regulator DcuR. Upon phosphorylation, DcuR binds specifically to dcuB promoter DNA
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?
EvgA + ATP
?
show the reaction diagram
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one hybrid histidine kinase consisting of the BvgS transmitter and HPt domains and of the EvgS receiver domain BvgS-TO-EvgS-R is able to phosphorylate BvgA but not EvgA. In contrast, the hybrid protein consisting of the BvgS transmitter and the EvgS receiver and HPt domains BvgS-T-EvgS-RO is unable to phosphorylate BvgA but efficiently phosphorylates EvgA
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?
protein + ATP
?
show the reaction diagram
regulator protein OmpR + ATP
?
show the reaction diagram
TorR + ATP
?
show the reaction diagram
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TorS is a sensor that contains three phosphorylation sites and transphosphorylates TorR via a four-step phosphorelay, His443 to Asp723 to His850 to Asp(TorR). TorS can dephosphorylate phospho-TorR when trimethylamine N-oxide is removed. Dephosphorylation probably occurs by a reverse phosphorelay, Asp(TorR) to His850 to Asp723
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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
ArcA + ATP
?
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu+
0.14 molecules of Cu+ per enzyme molecule for the purified enzyme, and 0.23 molecules of Cu+ per enzyme molecule after dialysis against Ag+, Ni2+, Zn2+, and Cu+ ions
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(4-[2-[4-(4-cyanobenzyl)-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl]ethoxy]phenyl)methanaminium chloride
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2-(4-[2-[4-(4-chlorobenzyl)-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl]ethoxy]phenyl)ethanaminium chloride
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2-(4-[2-[4-(4-cyanobenzyl)-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl]ethoxy]phenyl)ethanaminium chloride
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Cu2+
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the wild-type strain experiences copper susceptibility at 2.75 mM CuSO4, whereas DELTAcusS mutant cells show a phenotype at lower concentrations
HCl
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cytoplasmic phosphorylated AtoS is sensitive to treatment with 1 N HCl but stable in the presence of 1 N NaOH
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
citrate
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effector of CitA
fumarate
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effector of DcuS
LprF
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direct regulator of KdpD
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LprJ
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direct regulator of KdpD
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UhpC
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UhpC stimulates UhpB autophosphorylation in the presence of D-glucose 6-phosphate
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additional information
a high concentration of alkali metals (Na+, K+) in addition to low pH is essential for the activation of histidine kinase EvgS. EvgS/EvgA is activated under mildly acidic conditions at pH 5.0-5.5. EvgS has a large periplasmic sensor region consisting of two tandem bacterial periplasmic solute-binding protein (PBPb) domains at its N-terminus. The periplasmic sensor region of EvgS is necessary for EvgS activation, and Leu152, located within the first PBPb domain, is involved in the activation. Alkali metals are perceived at the periplasmic sensor region, whereas the cytoplasmic linker domain, connecting the transmembrane region and the histidine kinase domain, is required for low-pH perception
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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enzyme is anchored to the cytoplasmic membrane by the amino-terminal region
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Manually annotated by BRENDA team
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structure-function relationship in the cytoplasmic PAS domain, the multidomain protein DcuS possesses functional domains in the periplasm, within the membrane and in the cytoplasm, the localization depends on the functional state, overview
Manually annotated by BRENDA team
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the multidomain protein DcuS possesses functional domains in the periplasm, within the membrane and in the cytoplasm, the localization depends on the functional state, overview
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Manually annotated by BRENDA team
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the multidomain protein DcuS possesses functional domains in the periplasm, within the membrane and in the cytoplasm, the localization depends on the functional state, overview
Manually annotated by BRENDA team
additional information
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the structure of the periplasmic sensor domain of the histidine kinase CusS shows unusual metal ion coordination at the dimeric interface
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
49666
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x * 49666
49772
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x * 49772, calculation from nucleotide sequence
50000
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x * 50000
52000
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x * 52000
55290
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x * 55290
67275
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x * 67275, calculation from nucleotide sequence
75000
gel filtration
99000
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x * 99000
102452
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x * 102452, calculation from nucleotide sequence
additional information
CusSs samples for analytical ultracentrifugation experiments are prepared by dialysis against 5fold molar excesses of AgNO3, ZnCl2 or NiCl2
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
gel filtration
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure at 2.0 A resolution of the complex of the Escherichia coli chemotaxis response regulator CheY and the phosphoacceptor-binding domain P2 of the kinase CheA
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crystal structure of the C-terminal HPt domain of ArcB
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crystal structure of the histidine-containing phosphotransfer domain
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crystal structure, at 2.95 A resolution, of the response regulator of bacterial chemotaxis, CheY, bound to the recognition domain from its cognate histidine kinase, CheA
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crystallization of a complex between a novel C-terminal transmitter, HPt domain, of the anaerobic sensor kinase ArcB and the chemotaxis response regulator CheY
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free and in complex with nitrate, hanging drop vapor diffusion method, using 0.1 M Tris-HCl (pH 8.5) and 2 M NH4H2PO4 at 4C (enzyme in complex with nitrate) or using 23% (w/v) polyethylene glycol 3350, 1% (v/v) isopropanol, and 0.1 M HEPES (pH 7.5) at 4C (free apo-enzyme)
hanging drop vapor diffusion method, at 4C against a buffer containing 5%10% (v/v) 1-4 butanediol, 0.1 M Na-aetate (pH 5.5), 25100 mM NH4SO4
purified recombinant Ag(I)-bound periplasmic sensor domain, Ag(I)-CusS(39-187), sitting drop vapor diffusion method, mixing of 200 nl of 7-8 mg/ml protein in 25 mM MES, pH 6.0, with 200 nl of precipitant solution containing 100 mM Tris-HCl, pH 8.5, 200 mM ammonium acetate, and 25% PEG 3350, 4C, equilibration against 1 ml precipitant solution, method optimization, X-ray diffraction structure determination and analysis, single anomalous diffraction (SAD) method at 2.15 A resolution. There are four Ag(I)-CusS(39-187) molecules in the asymmetric unit that interact to form two homodimers
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recombinant chimeric protein formed by the EnvZ catalytic domain with the HAMP domain of the Archaeoglobus fulgidus Af1503 receptor, with or without the point mutation A291F, sitting drop vapor diffusion method, mixing of 400 nl of 2 and 20 mg/mlprotein, respectively, in 30 mM MOPS, pH 7.0 and 50 mM NaCl, for the wild-type construct and in a buffer containing 20 mM MOPS, pH 7.0 and 100 mM NaCl for the A291F mutant, with 400 nl of reservoir solution and equilibration against 0.05 mL reservoir solution, containing 0.1 M MMT buffer, pH 4.0, and 25% (w/v) PEG 1500 for the wild-type fusion and 0.2 M lithium acetate and 20% w/v PEG 3350 for the A291F variant, 22C, X-ray diffraction tructure determination and analysis. The structure shows a putatively active conformation of the catalytic domain, molecular replacement
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
HiTrap Ni2+-chelating column chromatography, Mono Q column chromatography, and Superdex 75 gel filtration
IMAC and Ni2+-NTA agarose column chromatography
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Ni2+-affinity column chromatography, MonoQ column chromatography, glutathione Sepharose column chromatography, Superdex 200 gel filtration, and Superdex 75 gel filtration
recombinant CBD-tagged enzyme from Escherichia coli strain BL21(DE3) by chitin affinity chromatography with DTT thiol-induced cleavage and gel filtration to over 95% purity
recombinant periplasmic domain of histidine kinase EnvZ(Ala38-Arg162)
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cytoplasmic expression of TorSS as a fusion protein, containing a hexahistidine tag on the N-terminus separated by a separated by a thrombin protease recognition sequence, in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
expression of the periplasmic domain of histidine kinase EnvZ(Ala38-Arg162) in Escherichia coli
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gene cusS, recombinant expression of the enzyme's periplasmic domain from pTXB3CusSs plasmid, encoding CusS amino acids 39-187 with a chitin binding domain (CBD) affinity tag, in Escherichia coli strain BL21(DE3)
mutant enzymes cloned and expressed in Escherichia coli strain BL21(DE3)
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overexpression of a 36-kDa truncated EnvZ protein, Glu106 to Gly450, that forms inclusion bodies in the cell
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phoP-phoQ operon cloned and expressed in Escherichia coli
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recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli. The expression of CusS from a plasmid does not result in the same growth phenotype on copper-containing media as the strain that expresses chromosomal CusS
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D286C
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t1/2 at room temperature is 16 min, compared to 12 min for wild-type enzyme. 71% of the wild-type phosphatase activity
E257C
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t1/2 at room temperature is 30 min, compared to 12 min for wild-type enzyme. 31% of the wild-type phosphatase activity
E261C
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t1/2 at room temperature is 15 min, compared to 12 min for wild-type enzyme. 77% of the wild-type phosphatase activity
E268C
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t1/2 at room temperature is 23 min, compared to 12 min for wild-type enzyme. 45% of the wild-type phosphatase activity
E275C
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t1/2 at room temperature is 28 min, compared to 12 min for wild-type enzyme. 34% of the wild-type phosphatase activity
E276C
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t1/2 at room temperature is 68 min, compared to 12 min for wild-type enzyme. 5% of the wild-type phosphatase activity
E282C
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t1/2 at room temperature is 15 min, compared to 12 min for wild-type enzyme. 77% of the wild-type phosphatase activity
F43I
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site-directed mutagenesis, the mutation results in a slightly reduced growth defect compared to the construct in which all interface binding site residues are mutated
G240C
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t1/2 at room temperature is 10 min, compared to 12 min for wild-type enzyme. 123% of the wild-type phosphatase activity
G264C
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t1/2 at room temperature is 12 min, compared to 12 min for wild-type enzyme. As active as wild-type enzyme
H176A
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site-directed mutagenesis, the mutation results in the same growth defects as the construct in which all interface binding site residues are mutated
H243K
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inactive mutant protein
H243N
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inactive mutant protein
H243S
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inactive mutant protein
H243V
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inactive mutant protein
H243X
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the His residue at position 243 of the EnvZ protein is changed by means of site-directed mutagenesis. The mutant EnvZ protein is defective in its in vitro ability not only as to EnvZ-autophosphorylation but also OmpR-phosphorylation and OmpR-dephosphorylation. This particular mutant EnvZ protein seems to exhibit null functions as to the in vivo osmoregulatory phenotype
H243Y
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inactive mutant protein
H398L
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the mutant retains itscapability to bind ATP and is competent to catalyze the transphosphorylation of an AtoS G-box (G565A) mutant protein which otherwise fails to autophosphorylate due to its inability to bind ATP
H42A
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site-directed mutagenesis, the mutation results in the same growth defects as the construct in which all interface binding site residues are mutated
K152A
site-directed mutagenesis, the mutant is expressed in the membrane at levels comparable to the wild-type EvgS strain. The mutant shows moderate activation by KCl-supplemented M9 medium, pH 5.5
K152E
site-directed mutagenesis, the mutant is expressed in the membrane at levels comparable to the wild-type EvgS strain. The mutant shows strong activation by KCl-supplemented M9 medium, pH 5.5
K152F
naturally occuring mutation and site-directed mutagenesis, in the mutant, EvgS activation is observed only by complementation with pBADevgS, mutation L152F leads to the desensitization of EvgS in strain KMY1. The mutant shows no activation by KCl-supplemented M9 medium, pH 5.5. The L152F mutation is found in only two Escherichia coli strains, MC4100 and DH1
K152I
site-directed mutagenesis, the mutant is expressed in the membrane at levels comparable to the wild-type EvgS strain. The mutant shows strong activation by KCl-supplemented M9 medium, pH 5.5
K152R
site-directed mutagenesis, the mutant is expressed in the membrane at levels comparable to the wild-type EvgS strain. The mutant shows moderate activation by KCl-supplemented M9 medium, pH 5.5
K152Y
site-directed mutagenesis, the mutant is expressed in the membrane at levels comparable to the wild-type EvgS strain. The mutant shows no activation by KCl-supplemented M9 medium, pH 5.5
K272C
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t1/2 at room temperature is 55 min, compared to 12 min for wild-type enzyme. 10% of the wild-type phosphatase activity
L236C
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t1/2 at room temperature is 25 min, compared to 12 min for wild-type enzyme. 40% of the wild-type phosphatase activity
L254C
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inactive mutant enzyme, t1/2 at room temperature is 90 min, compared to 12 min for wild-type enzyme
N248A
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site-directed mutagenesis, the mutation activates the enzyme
N248D
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site-directed mutagenesis, the mutation activates the enzyme
N248G
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site-directed mutagenesis, the mutation activates the enzyme
N271C
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t1/2 at room temperature is 36 min, compared to 12 min for wild-type enzyme. 23% of the wild-type phosphatase activity
N278C
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t1/2 at room temperature is 45 min, compared to 12 min for wild-type enzyme. 15% of the wild-type phosphatase activity
Q262C
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t1/2 at room temperature is 11 min, compared to 12 min for wild-type enzyme. 111% of the wild-type phosphatase activity
Q283C
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t1/2 at room temperature is 13 min, compared to 12 min for wild-type enzyme. 91% of the wild-type phosphatase activity
R246C
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t1/2 at room temperature is 62 min, compared to 12 min for wild-type enzyme. 7% of the wild-type phosphatase activity
S242C
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t1/2 at room temperature is 39 min, compared to 12 min for wild-type enzyme. 20% of the wild-type phosphatase activity
S260C
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t1/2 at room temperature is 13 min, compared to 12 min for wild-type enzyme. 91% of the wild-type phosphatase activity
S269C
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t1/2 at room temperature is 20 min, compared to 12 min for wild-type enzyme. 54% of the wild-type phosphatase activity
T235C
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t1/2 at room temperature is 14 min, compared to 12 min for wild-type enzyme. 84% of the wild-type phosphatase activity
T247R
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inactive mutant protein
T250C
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t1/2 at room temperature is 23 min, compared to 12 min for wild-type enzyme. 45% of the wild-type phosphatase activity
T256C
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t1/2 at room temperature is 27 min, compared to 12 min for wild-type enzyme. 36% of the wild-type phosphatase activity
Y265C
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t1/2 at room temperature is 20 min, compared to 12 min for wild-type enzyme. 54% of the wild-type phosphatase activity
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
protein refolding is achieved by dialysis in storage buffer (50 mM Tris-HCl pH 7.6, 0.5 mM dithiothreitol, 50% (v/v) glycerol) containing 0.01% (v/v) Triton X-100
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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15 of the 30 known Escherichia coli histidine kinases contain a single HAMP domain, has an important role in signal transduction