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Information on EC 2.7.13.3 - histidine kinase and Organism(s) Escherichia coli and UniProt Accession P08400

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EC Tree
     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.13 Protein-histidine kinases
                2.7.13.3 histidine kinase
IUBMB Comments
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.
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Select one or more organisms in this record:
This record set is specific for:
Escherichia coli
UNIPROT: P08400
Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The taxonomic range for the selected organisms is: Escherichia coli
Synonyms
33277 FimS, AaHSK1, adaptive-response sensory-kinase A, aerobic respiration control sensor protein arcB, aerobic respiration control sensor protein arcB homolog, aerobic respiration control sensor/response regulatory protein, AfGcHK, AgrC, AHK, AHK5, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aerobic respiration control sensor protein arcB
AtoS-AtoC two-component signal transduction system
246
-
BarA protein
261917
-
chemotaxis protein cheA
chemotaxis-specific histidine autokinase CheA
261967
-
histidine autokinase CheA
261967
-
histidine kinase
246
-
histidine kinase EnvZ
246
-
histidine kinase PilS
246
-
multidomain membrane sensor kinase
262016
-
NarX
290822
-
nitrate-responsive histidine kinase
290822
-
nitrate/nitrite sensor protein narQ
nitrate/nitrite sensor protein narX
nitrogen regulation protein NR(II)
ornithine decarboxylase antizyme
262059
-
osmolarity sensor protein envZ
phosphate regulon sensor protein phoR
sensor kinase cusS
sensor kinase dpiB
262108
-
sensor kinase dpiB (sensor kinase citA)
262050
-
sensor protein atoS
sensor protein baeS
sensor protein basS/pmrB
sensor protein creC
sensor protein dcuS
sensor protein evgS precursor
sensor protein kdpD
sensor protein phoQ
sensor protein qseC
sensor protein rcsC
262100
-
sensor protein rcsC (capsular synthesis regulator)
261983
-
sensor protein rstB
sensor protein torS
sensor protein uhpB
sensor protein zraS
sensory histidine kinase
246
-
TMAO reductase S
262017
-
trimethylamine-N-oxide reductase S
262017
-
additional information
262016
DcuS is a member of the periplasmic sensing histidine kinases
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
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
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
-
autophosphorylation. Probing catalytically essential domain orientation in histidine kinase EnvZ by targeted disulfide crosslinking
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
show the reaction diagram
-
-
-
-
?
BvgA + ATP
?
show the reaction diagram
-
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
-
-
?
DcuR + ATP
?
show the reaction diagram
-
the phosphoryl group of DcuS is rapidly transferred to the response regulator DcuR. Upon phosphorylation, DcuR binds specifically to dcuB promoter DNA
-
-
?
EvgA + ATP
?
show the reaction diagram
-
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
-
-
?
protein + ATP
?
show the reaction diagram
regulator protein OmpR + ATP
?
show the reaction diagram
TorR + ATP
?
show the reaction diagram
-
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
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL 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
additional information
?
-
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
INHIBITOR
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
-
-
2-(4-[2-[4-(4-chlorobenzyl)-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl]ethoxy]phenyl)ethanaminium chloride
-
-
2-(4-[2-[4-(4-cyanobenzyl)-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl]ethoxy]phenyl)ethanaminium chloride
-
-
Cu2+
-
the wild-type strain experiences copper susceptibility at 2.75 mM CuSO4, whereas DELTAcusS mutant cells show a phenotype at lower concentrations
HCl
-
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
-
effector of CitA
fumarate
-
effector of DcuS
LprF
-
direct regulator of KdpD
-
LprJ
-
direct regulator of KdpD
-
UhpC
-
UhpC stimulates UhpB autophosphorylation in the presence of D-glucose 6-phosphate
-
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
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
enzyme is anchored to the cytoplasmic membrane by the amino-terminal region
-
Manually annotated by BRENDA team
-
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
-
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
-
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
-
the structure of the periplasmic sensor domain of the histidine kinase CusS shows unusual metal ion coordination at the dimeric interface
-
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
-
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
-
DcuS and CitA are involved in the regulation of carboxylate metabolism
physiological function
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
49666
-
x * 49666
49772
-
x * 49772, calculation from nucleotide sequence
50000
-
x * 50000
52000
-
x * 52000
55290
-
x * 55290
67275
-
x * 67275, calculation from nucleotide sequence
75000
-
gel filtration
99000
-
x * 99000
102452
-
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 49666
dimer
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
-
crystal structure of the C-terminal HPt domain of ArcB
-
crystal structure of the histidine-containing phosphotransfer domain
-
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
-
crystallization of a complex between a novel C-terminal transmitter, HPt domain, of the anaerobic sensor kinase ArcB and the chemotaxis response regulator CheY
-
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D286C
-
t1/2 at room temperature is 16 min, compared to 12 min for wild-type enzyme. 71% of the wild-type phosphatase activity
E257C
-
t1/2 at room temperature is 30 min, compared to 12 min for wild-type enzyme. 31% of the wild-type phosphatase activity
E261C
-
t1/2 at room temperature is 15 min, compared to 12 min for wild-type enzyme. 77% of the wild-type phosphatase activity
E268C
-
t1/2 at room temperature is 23 min, compared to 12 min for wild-type enzyme. 45% of the wild-type phosphatase activity
E275C
-
t1/2 at room temperature is 28 min, compared to 12 min for wild-type enzyme. 34% of the wild-type phosphatase activity
E276C
-
t1/2 at room temperature is 68 min, compared to 12 min for wild-type enzyme. 5% of the wild-type phosphatase activity
E282C
-
t1/2 at room temperature is 15 min, compared to 12 min for wild-type enzyme. 77% of the wild-type phosphatase activity
F43I
-
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
-
t1/2 at room temperature is 10 min, compared to 12 min for wild-type enzyme. 123% of the wild-type phosphatase activity
G264C
-
t1/2 at room temperature is 12 min, compared to 12 min for wild-type enzyme. As active as wild-type enzyme
H176A
-
site-directed mutagenesis, the mutation results in the same growth defects as the construct in which all interface binding site residues are mutated
H243K
-
inactive mutant protein
H243N
-
inactive mutant protein
H243S
-
inactive mutant protein
H243V
-
inactive mutant protein
H243X
-
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
-
inactive mutant protein
H398L
-
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
-
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
-
t1/2 at room temperature is 55 min, compared to 12 min for wild-type enzyme. 10% of the wild-type phosphatase activity
L236C
-
t1/2 at room temperature is 25 min, compared to 12 min for wild-type enzyme. 40% of the wild-type phosphatase activity
L254C
-
inactive mutant enzyme, t1/2 at room temperature is 90 min, compared to 12 min for wild-type enzyme
N248A
-
site-directed mutagenesis, the mutation activates the enzyme
N248D
-
site-directed mutagenesis, the mutation activates the enzyme
N248G
-
site-directed mutagenesis, the mutation activates the enzyme
N271C
-
t1/2 at room temperature is 36 min, compared to 12 min for wild-type enzyme. 23% of the wild-type phosphatase activity
N278C
-
t1/2 at room temperature is 45 min, compared to 12 min for wild-type enzyme. 15% of the wild-type phosphatase activity
Q262C
-
t1/2 at room temperature is 11 min, compared to 12 min for wild-type enzyme. 111% of the wild-type phosphatase activity
Q283C
-
t1/2 at room temperature is 13 min, compared to 12 min for wild-type enzyme. 91% of the wild-type phosphatase activity
R246C
-
t1/2 at room temperature is 62 min, compared to 12 min for wild-type enzyme. 7% of the wild-type phosphatase activity
S242C
-
t1/2 at room temperature is 39 min, compared to 12 min for wild-type enzyme. 20% of the wild-type phosphatase activity
S260C
-
t1/2 at room temperature is 13 min, compared to 12 min for wild-type enzyme. 91% of the wild-type phosphatase activity
S269C
-
t1/2 at room temperature is 20 min, compared to 12 min for wild-type enzyme. 54% of the wild-type phosphatase activity
T235C
-
t1/2 at room temperature is 14 min, compared to 12 min for wild-type enzyme. 84% of the wild-type phosphatase activity
T247R
-
inactive mutant protein
T250C
-
t1/2 at room temperature is 23 min, compared to 12 min for wild-type enzyme. 45% of the wild-type phosphatase activity
T256C
-
t1/2 at room temperature is 27 min, compared to 12 min for wild-type enzyme. 36% of the wild-type phosphatase activity
Y265C
-
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
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
-
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)
-
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
-
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)
-
overexpression of a 36-kDa truncated EnvZ protein, Glu106 to Gly450, that forms inclusion bodies in the cell
-
phoP-phoQ operon cloned and expressed in Escherichia coli
-
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
-
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
15 of the 30 known Escherichia coli histidine kinases contain a single HAMP domain, has an important role in signal transduction
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Roberts, D.L.; Bennett, D.W.; Forst, S.A.
Identification of the site of phosphorylation on the osmosensor, EnvZ, of Escherichia coli
J. Biol. Chem.
269
8728-8733
1994
Escherichia coli, Escherichia coli (P0AEJ4)
Manually annotated by BRENDA team
Pernestig, A.K.; Georgellis, D.; Romeo, T.; Suzuki, K.; Tomenius, H.; Normark, S.; Melefors, O.
The Escherichia coli BarA-UvrY two-component system is needed for efficient switching between glycolytic and gluconeogenic carbon sources
J. Bacteriol.
185
843-853
2003
Escherichia coli, Escherichia coli (P0AEC7)
Manually annotated by BRENDA team
Nagasawa, S.; Tokishita, S.; Aiba, H.; Mizuno, T.
A novel sensor-regulator protein that belongs to the homologous family of signal-transduction proteins involved in adaptive responses in Escherichia coli
Mol. Microbiol.
6
799-807
1992
Escherichia coli, Escherichia coli (P0AEC7)
Manually annotated by BRENDA team
Pernestig, A.K.; Melefors, O.; Georgellis, D.
Identification of UvrY as the cognate response regulator for the BarA sensor kinase in Escherichia coli
J. Biol. Chem.
276
225-231
2001
Escherichia coli, Escherichia coli (P0AEC7)
Manually annotated by BRENDA team
Suzuki, K.; Wang, X.; Weilbacher, T.; Pernestig, A.K.; Melefors, O.; Georgellis, D.; Babitzke, P.; Romeo, T.
Regulatory circuitry of the CsrA/CsrB and BarA/UvrY systems of Escherichia coli
J. Bacteriol.
184
5130-5140
2002
Escherichia coli (P0AEC7)
Manually annotated by BRENDA team
Welch, R.A.; Burland, V.; Plunkett, G.III; Redford, P.; Roesch, P.; Rasko, D.; Buckles, E.L.; Liou, S.R.; Boutin, A.; Hackett, J.; Stroud, D.; Mayhew, G.F.; Rose, D.J.; Zhou, S.; Schwartz, D.C.; Perna, N.T.; Mobley, H.L.T.; Donnenberg, M.S.; Blattner, F.R.
Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli
Proc. Natl. Acad. Sci. USA
99
17020-17024
2002
Escherichia coli (P0AE83), Escherichia coli (P0AEC7), Escherichia coli (P59340), Escherichia coli (Q8CVU5), Escherichia coli (Q8FA38), Escherichia coli (Q8FAU6), Escherichia coli (Q8FB70), Escherichia coli (Q8FBG6), Escherichia coli (Q8FBX4), Escherichia coli (Q8FCU0), Escherichia coli (Q8FD66), Escherichia coli (Q8FDJ7), Escherichia coli (Q8FF85), Escherichia coli (Q8FFP8), Escherichia coli (Q8FFP9), Escherichia coli (Q8FG01), Escherichia coli (Q8FGP1), Escherichia coli (Q8FHA9), Escherichia coli (Q8FHZ2), Escherichia coli (Q8FIB8), Escherichia coli (Q8FJ55), Escherichia coli (Q8FJV6), Escherichia coli (Q8FJZ9), Escherichia coli (Q8FK37), Escherichia coli (Q8FKD0), Escherichia coli O6:H1 (P59340), Escherichia coli O6:H1 (Q8CVU5), Escherichia coli O6:H1 (Q8FA38), Escherichia coli O6:H1 (Q8FAU6), Escherichia coli O6:H1 (Q8FB70), Escherichia coli O6:H1 (Q8FBG6), Escherichia coli O6:H1 (Q8FBX4), Escherichia coli O6:H1 (Q8FCU0), Escherichia coli O6:H1 (Q8FD66), Escherichia coli O6:H1 (Q8FDJ7), Escherichia coli O6:H1 (Q8FF85), Escherichia coli O6:H1 (Q8FFP8), Escherichia coli O6:H1 (Q8FFP9), Escherichia coli O6:H1 (Q8FG01), Escherichia coli O6:H1 (Q8FGP1), Escherichia coli O6:H1 (Q8FHA9), Escherichia coli O6:H1 (Q8FHZ2), Escherichia coli O6:H1 (Q8FIB8), Escherichia coli O6:H1 (Q8FJ55), Escherichia coli O6:H1 (Q8FJV6), Escherichia coli O6:H1 (Q8FJZ9), Escherichia coli O6:H1 (Q8FK37), Escherichia coli O6:H1 (Q8FKD0)
Manually annotated by BRENDA team
Yamamoto, Y.; Aiba, H.; Baba, T.; Hayashi, K.; et al.
Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features
DNA Res.
4
91-113
1997
Escherichia coli (P0AEC7), Escherichia coli (P27896), Escherichia coli (P30855)
Manually annotated by BRENDA team
Comeau, D.E.; Ikenaka, K.; Tsung, K.L.; Inouye, M.
Primary characterization of the protein products of the Escherichia coli ompB locus: structure and regulation of synthesis of the OmpR and EnvZ proteins
J. Bacteriol.
164
578-584
1985
Escherichia coli (P0AEJ4)
Manually annotated by BRENDA team
Forst, S.; Comeau, D.; Norioka, S.; Inouye, M.
Localization and membrane topology of EnvZ, a protein involved in osmoregulation of OmpF and OmpC in Escherichia coli
J. Biol. Chem.
262
16433-16438
1987
Escherichia coli (P0AEJ4)
Manually annotated by BRENDA team
Jin, Q.; Yuan, Z.; Xu, J.; Wang, Y.; et al.
Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157
Nucleic Acids Res.
30
4432-4441
2002
Escherichia coli, Escherichia coli (P0AEC3), Escherichia coli (P0AEJ4), Escherichia coli (P0AFB6), Shigella flexneri (P59341), Shigella flexneri (P59342)
Manually annotated by BRENDA team
Kanamaru, K.; Aiba, H.; Mizuno, T.
Transmembrane signal transduction and osmoregulation in Escherichia coli: I. Analysis by site-directed mutagenesis of the amino acid residues involved in phosphotransfer between the two regulatory components, EnvZ and OmpR
J. Biochem.
108
483-487
1990
Escherichia coli (P0AEJ4)
Manually annotated by BRENDA team
Mizuno, T.; Wurtzel, E.T.; Inouye, M.
Osmoregulation of gene expression. II. DNA sequence of the envZ gene of the ompB operon of Escherichia coli and characterization of its gene product
J. Biol. Chem.
257
13692-13698
1982
Escherichia coli (P0AEJ4)
Manually annotated by BRENDA team
Tanaka, T.; Saha, S.K.; Tomomori, C.; Ishima, R.; et al.
NMR structure of the histidine kinase domain of the E. coli osmosensor EnvZ
Nature
396
88-92
1998
Escherichia coli, Escherichia coli (P0AEJ4)
Manually annotated by BRENDA team
Tokishita, S.; Kojima, A.; Mizuno, T.
Transmembrane signal transduction and osmoregulation in Escherichia coli: functional importance of the transmembrane regions of membrane-located protein kinase, EnvZ
J. Biochem.
111
707-713
1992
Escherichia coli (P0AEJ4)
Manually annotated by BRENDA team
Tomomori, C.; Tanaka, T.; Dutta, R.; Park, H.; et al.
Solution structure of the homodimeric core domain of Escherichia coli histidine kinase EnvZ
Nat. Struct. Biol.
6
729-734
1999
Escherichia coli, Escherichia coli (P0AEJ4)
Manually annotated by BRENDA team
Miranda-Rios, J.; Sanchez-Pescador, R.; Urdea, M.; Covarrubias, A.A.
The complete nucleotide sequence of the glnALG operon of Escherichia coli K12
Nucleic Acids Res.
15
2757-2770
1987
Escherichia coli (P0AFB6)
Manually annotated by BRENDA team
Ninfa, A.J.; Bennett, R.L.
Identification of the site of autophosphorylation of the bacterial protein kinase/phosphatase NRII
J. Biol. Chem.
266
6888-6893
1991
Escherichia coli (P0AFB6)
Manually annotated by BRENDA team
Plunkett, G.3rd; Burland, V.; Daniels, D.L.; Blattner, F.R.
Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes
Nucleic Acids Res.
21
3391-3398
1993
Escherichia coli (P0AE83), Escherichia coli (P0AFB6)
Manually annotated by BRENDA team
Rocha, M.; Vazquez, M.; Garciarrubio, A.; Covarrubias, A.A.
Nucleotide sequence of the glnA-glnL intercistronic region of Escherichia coli
Gene
37
91-99
1985
Escherichia coli (P0AFB6)
Manually annotated by BRENDA team
Ueno-Nishio, S.; Mango, S.; Reitzer, L.J.; Magasanik, B.
Identification and regulation of the glnL operator-promoter of the complex glnALG operon of Escherichia coli
J. Bacteriol.
160
379-384
1984
Escherichia coli (P0AFB6)
Manually annotated by BRENDA team
Kofoid, E.C.; Parkinson, J.S.
Tandem translation starts in the cheA locus of Escherichia coli
J. Bacteriol.
173
2116-2119
1991
Escherichia coli (P07363)
Manually annotated by BRENDA team
McEvoy, M.M.; Hausrath, A.C.; Randolph, G.B.; Remington, S.J.; Dahlquist, F.W.
Two binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathway
Proc. Natl. Acad. Sci. USA
95
7333-7338
1998
Escherichia coli (P07363)
Manually annotated by BRENDA team
McEvoy, M.M.; Muhandiram, D.R.; Kay, L.E.; Dahlquist, F.W.
Structure and dynamics of a CheY-binding domain of the chemotaxis kinase CheA determined by nuclear magnetic resonance spectroscopy
Biochemistry
35
5633-5640
1996
Escherichia coli, Escherichia coli (P07363)
Manually annotated by BRENDA team
McNally, D.F.; Matsumura, P.
Bacterial chemotaxis signaling complexes: formation of a CheA/CheW complex enhances autophosphorylation and affinity for CheY
Proc. Natl. Acad. Sci. USA
88
6269-6273
1991
Escherichia coli (P07363)
Manually annotated by BRENDA team
Mutoh, N.; Simon, M.I.
Nucleotide sequence corresponding to five chemotaxis genes in Escherichia coli
J. Bacteriol.
165
161-166
1986
Escherichia coli (P07363)
Manually annotated by BRENDA team
Oosawa, K.; Hess, J.F.; Simon, M.I.
Mutants defective in bacterial chemotaxis show modified protein phosphorylation
Cell
53
89-96
1988
Escherichia coli (P07363)
Manually annotated by BRENDA team
Welch, M.; Chinardet, N.; Mourey, L.; Birck, C.; Samama, J.P.
Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY
Nat. Struct. Biol.
5
25-29
1998
Escherichia coli (P07363)
Manually annotated by BRENDA team
Zhou, H.; Dahlquist, F.W.
Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NMR
Biochemistry
36
699-710
1997
Escherichia coli, Escherichia coli (P07363)
Manually annotated by BRENDA team
Zhou, H.; McEvoy, M.M.; Lowry, D.F.; Swanson, R.V.; Simon, M.I.; Dahlquist, F.W.
Phosphotransfer and CheY-binding domains of the histidine autokinase CheA are joined by a flexible linker
Biochemistry
35
433-443
1996
Escherichia coli, Escherichia coli (P07363)
Manually annotated by BRENDA team
Albin, R.; Weber, R.; Silverman, P.M.
The Cpx proteins of Escherichia coli K12. Immunologic detection of the chromosomal cpxA gene product
J. Biol. Chem.
261
4698-4705
1986
Escherichia coli (P0AE83)
Manually annotated by BRENDA team
Rainwater, S.; Silverman, P.M.
The Cpx proteins of Escherichia coli K-12: evidence that cpxA, ecfB, ssd, and eup mutations all identify the same gene
J. Bacteriol.
172
2456-2461
1990
Escherichia coli (P0AE83)
Manually annotated by BRENDA team
Weber, R.F.; Silverman, P.M.
The cpx proteins of Escherichia coli K12. Structure of the cpxA polypeptide as an inner membrane component
J. Mol. Biol.
203
467-478
1988
Escherichia coli (P0AE83)
Manually annotated by BRENDA team
Makino, K.; Shinagawa, H.; Amemura, M.; Nakata, A.
Nucleotide sequence of the phoR gene, a regulatory gene for the phosphate regulon of Escherichia coli
J. Mol. Biol.
192
549-556
1986
Escherichia coli (P08400)
Manually annotated by BRENDA team
Scholten, M.; Tommassen, J.
Topology of the PhoR protein of Escherichia coli and functional analysis of internal deletion mutants
Mol. Microbiol.
8
269-275
1993
Escherichia coli (P08400)
Manually annotated by BRENDA team
Yamada, M.; Makino, K.; Shinagawa, H.; Nakata, A.
Regulation of the phosphate regulon of Escherichia coli: properties of phoR deletion mutants and subcellular localization of PhoR protein
Mol. Gen. Genet.
220
366-372
1990
Escherichia coli (P08400)
Manually annotated by BRENDA team
Amemura, M.; Makino, K.; Shinagawa, H.; Nakata, A.
Cross talk to the phosphate regulon of Escherichia coli by PhoM protein: PhoM is a histidine protein kinase and catalyzes phosphorylation of PhoB and PhoM-open reading frame 2
J. Bacteriol.
172
6300-6307
1990
Escherichia coli (P08401)
Manually annotated by BRENDA team
Amemura, M.; Makino, K.; Shinagawa, H.; Nakata, A.
Nucleotide sequence of the phoM region of Escherichia coli: four open reading frames may constitute an operon
J. Bacteriol.
168
294-302
1986
Escherichia coli (P08401)
Manually annotated by BRENDA team
Burland, V.; Plunkett, G.; Sofia, H.J.; Daniels, D.L.; Blattner, F.R.
Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes
Nucleic Acids Res.
23
2105-2119
1995
Escherichia coli (P08401), Escherichia coli (P0AEC8), Escherichia coli (P30844), Escherichia coli (P39453)
Manually annotated by BRENDA team
Drury, L.S.; Buxton, R.S.
Identification and sequencing of the Escherichia coli cet gene which codes for an inner membrane protein, mutation of which causes tolerance to colicin E2
Mol. Microbiol.
2
109-119
1988
Escherichia coli (P08401)
Manually annotated by BRENDA team
Burland, V.; Plunkett, G.; Daniels, D.L.; Blattner, F.R.
DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication
Genomics
16
551-561
1993
Escherichia coli (P09835)
Manually annotated by BRENDA team
Friedrich, M.J.; Kadner, R.J.
Nucleotide sequence of the uhp region of Escherichia coli
J. Bacteriol.
169
3556-3563
1987
Escherichia coli (P09835)
Manually annotated by BRENDA team
Island, M.D.; Wei, B.Y.; Kadner, R.J.
Structure and function of the uhp genes for the sugar phosphate transport system in Escherichia coli and Salmonella typhimurium
J. Bacteriol.
174
2754-2762
1992
Escherichia coli (P09835), Salmonella enterica subsp. enterica serovar Typhimurium (P27668)
Manually annotated by BRENDA team
Nohno, T.; Noji, S.; Taniguchi, S.; Saito, T.
The narX and narL genes encoding the nitrate-sensing regulators of Escherichia coli are homologous to a family of prokaryotic two-component regulatory genes
Nucleic Acids Res.
17
2947-2957
1989
Escherichia coli
Manually annotated by BRENDA team
Noji, S.; Nohno, T.; Saito, T.; Taniguchi, S.
The narK gene product participates in nitrate transport induced in Escherichia coli nitrate-respiring cells
FEBS Lett.
252
139-143
1989
Escherichia coli
Manually annotated by BRENDA team
Stewart, V.; Parales, J.Jr.; Merkel, S.M.
Structure of genes narL and narX of the nar (nitrate reductase) locus in Escherichia coli K-12
J. Bacteriol.
171
2229-2234
1989
Escherichia coli
Manually annotated by BRENDA team
Stout, V.; Gottesman, S.
RcsB and RcsC: a two-component regulator of capsule synthesis in Escherichia coli
J. Bacteriol.
172
659-669
1990
Escherichia coli (P0DMC5)
Manually annotated by BRENDA team
Blattner, F.R.; Burland, V.; Plunkett, G.; Sofia, H.J.; Daniels, D.L.
Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes
Nucleic Acids Res.
21
5408-5417
1993
Escherichia coli (P14377)
Manually annotated by BRENDA team
Leonhartsberger, S.; Huber, A.; Lottspeich, F.; Bock, A.
The hydH/G Genes from Escherichia coli code for a zinc and lead responsive two-component regulatory system
J. Mol. Biol.
307
93-105
2001
Escherichia coli (P14377), Klebsiella oxytoca (Q9APE0)
Manually annotated by BRENDA team
Stoker, K.; Reijnders, W.N.; Oltmann, L.F.; Stouthamer, A.H.
Initial cloning and sequencing of hydHG, an operon homologous to ntrBC and regulating the labile hydrogenase activity in Escherichia coli K-12
J. Bacteriol.
171
4448-4456
1989
Escherichia coli (P0AEC8), Escherichia coli (P14377)
Manually annotated by BRENDA team
Perraud, A.L.; Kimmel, B.; Weiss, V.; Gross, R.
Specificity of the BvgAS and EvgAS phosphorelay is mediated by the C-terminal HPt domains of the sensor proteins
Mol. Microbiol.
27
875-887
1998
Bordetella pertussis (P16575), Escherichia coli (P30855)
Manually annotated by BRENDA team
Aiba, H.; Baba, T.; Hayashi, K.; et al.
A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map
DNA Res.
3
363-377
1996
Escherichia coli (P18392)
Manually annotated by BRENDA team
Hill, T.M.; Tecklenburg, M.L.; Pelletier, A.J.; Kuempel, P.L.
Tus, the trans-acting gene required for termination of DNA replication in Escherichia coli, encodes a DNA-binding protein
Proc. Natl. Acad. Sci. USA
86
1593-1597
1989
Escherichia coli (P18392)
Manually annotated by BRENDA team
Roecklein, B.; Pelletier, A.; Kuempel, P.
The tus gene of Escherichia coli: autoregulation, analysis of flanking sequences and identification of a complementary system in Salmonella typhimurium
Res. Microbiol.
142
169-175
1991
Escherichia coli (P18392)
Manually annotated by BRENDA team
Roecklein, B.A.; Kuempel, P.L.
In vivo characterization of tus gene expression in Escherichia coli
Mol. Microbiol.
6
1655-1661
1992
Escherichia coli (P18392)
Manually annotated by BRENDA team
Walderhaug, M.O.; Polarek, J.W.; Voelkner, P.; Daniel, J.M.; Hesse, J.E.; Altendorf, K.; Epstein, W.
KdpD and KdpE, proteins that control expression of the kdpABC operon, are members of the two-component sensor-effector class of regulators
J. Bacteriol.
174
2152-2159
1992
Escherichia coli (P21865)
Manually annotated by BRENDA team
Zimmann, P.; Puppe, W.; Altendorf, K.
Membrane topology analysis of the sensor kinase KdpD of Escherichia coli
J. Biol. Chem.
270
28282-28288
1995
Escherichia coli, Escherichia coli (P21865)
Manually annotated by BRENDA team
Georgellis, D.; Kwon, O.; De Wulf, P.; Lin, E.C.
Signal decay through a reverse phosphorelay in the Arc two-component signal transduction system
J. Biol. Chem.
273
32864-32869
1998
Escherichia coli, Escherichia coli (P0AEC3)
Manually annotated by BRENDA team
Georgellis, D.; Lynch, A.S.; Lin, E.C.
In vitro phosphorylation study of the arc two-component signal transduction system of Escherichia coli
J. Bacteriol.
179
5429-5435
1997
Escherichia coli, Escherichia coli (P0AEC3)
Manually annotated by BRENDA team
Iuchi, S.; Matsuda, Z.; Fujiwara, T.; Lin, E.C.
The arcB gene of Escherichia coli encodes a sensor-regulator protein for anaerobic repression of the arc modulon
Mol. Microbiol.
4
715-727
1990
Escherichia coli, Escherichia coli (P0AEC3)
Manually annotated by BRENDA team
Kato, M.; Mizuno, T.; Hakoshima, T.
Crystallization of a complex between a novel C-terminal transmitter, HPt domain, of the anaerobic sensor kinase ArcB and the chemotaxis response regulator CheY
Acta Crystallogr. Sect. D
54
140-142
1998
Escherichia coli (P0AEC3)
Manually annotated by BRENDA team
Kato, M.; Mizuno, T.; Shimizu, T.; Hakoshima, T.
Insights into multistep phosphorelay from the crystal structure of the C-terminal HPt domain of ArcB
Cell
88
717-723
1997
Escherichia coli (P0AEC3)
Manually annotated by BRENDA team
Kato, M.; Mizuno, T.; Shimizu, T.; Hakoshima, T.
Refined structure of the histidine-containing phosphotransfer (HPt) domain of the anaerobic sensor kinase ArcB from Escherichia coli at 1.57 A resolution
Acta Crystallogr. Sect. D
55
1842-1849
1999
Escherichia coli, Escherichia coli (P0AEC3)
Manually annotated by BRENDA team
Kwon, O.; Georgellis, D.; Lin, E.C.
Phosphorelay as the sole physiological route of signal transmission by the arc two-component system of Escherichia coli
J. Bacteriol.
182
3858-3862
2000
Escherichia coli, Escherichia coli (P0AEC3)
Manually annotated by BRENDA team
Kasahara, M.; Nakata, A.; Shinagawa, H.
Molecular analysis of the Escherichia coli phoP-phoQ operon
J. Bacteriol.
174
492-498
1992
Escherichia coli (P23837)
Manually annotated by BRENDA team
Chiang, R.C.; Cavicchioli, R.; Gunsalus, R.P.
Identification and characterization of narQ, a second nitrate sensor for nitrate-dependent gene regulation in Escherichia coli
Mol. Microbiol.
6
1913-1923
1992
Escherichia coli (P27896)
Manually annotated by BRENDA team
Rabin, R.S.; Stewart, V.
Either of two functionally redundant sensor proteins, NarX and NarQ, is sufficient for nitrate regulation in Escherichia coli K-12
Proc. Natl. Acad. Sci. USA
89
8419-8423
1992
Escherichia coli (P27896)
Manually annotated by BRENDA team
Nagasawa, S.; Ishige, K.; Mizuno, T.
Novel members of the two-component signal transduction genes in Escherichia coli
J. Biochem.
114
350-357
1993
Escherichia coli (P30844), Escherichia coli (P30847)
Manually annotated by BRENDA team
Kato, A.; Ohnishi, H.; Yamamoto, K.; Furuta, E.; Tanabe, H.; Utsumi, R.
Transcription of emrKY is regulated by the EvgA-EvgS two-component system in Escherichia coli K-12
Biosci. Biotechnol. Biochem.
64
1203-1209
2000
Escherichia coli, Escherichia coli (P30855)
Manually annotated by BRENDA team
Utsumi, R.; Katayama, S.; Ikeda, M.; Igaki, S.; Nakagawa, H.; Miwa, A.; Taniguchi, M.; Noda, M.
Cloning and sequence analysis of the evgAS genes involved in signal transduction of Escherichia coli K-12
Nucleic Acids Symp. Ser.
1992
149-150
1992
Escherichia coli (P30855)
-
Manually annotated by BRENDA team
Utsumi, R.; Katayama, S.; Taniguchi, M.; Horie, T.; Ikeda, M.; Igaki, S.; Nakagawa, H.; Miwa, A.; Tanabe, H.; Noda, M.
Newly identified genes involved in the signal transduction of Escherichia coli K-12
Gene
140
73-77
1994
Escherichia coli (P30855)
Manually annotated by BRENDA team
Golby, P.; Davies, S.; Kelly, D.J.; Guest, J.R.; Andrews, S.C.
Identification and characterization of a two-component sensor-kinase and response-regulator system (DcuS-DcuR) controlling gene expression in response to C4-dicarboxylates in Escherichia coli
J. Bacteriol.
181
1238-1248
1999
Escherichia coli (P0AEC8)
Manually annotated by BRENDA team
Janausch, I.G.; Garcia-Moreno, I.; Unden, G.
Function of DcuS from Escherichia coli as a fumarate-stimulated histidine protein kinase in vitro
J. Biol. Chem.
277
39809-39814
2002
Escherichia coli, Escherichia coli (P0AEC8)
Manually annotated by BRENDA team
Zientz, E.; Bongaerts, J.; Unden, G.
Fumarate regulation of gene expression in Escherichia coli by the DcuSR (dcuSR genes) two-component regulatory system
J. Bacteriol.
180
5421-5425
1998
Escherichia coli, Escherichia coli (P0AEC8)
Manually annotated by BRENDA team
Ansaldi, M.; Jourlin-Castelli, C.; Lepelletier, M.; Theraulaz, L.; Mejean, V.
Rapid dephosphorylation of the TorR response regulator by the TorS unorthodox sensor in Escherichia coli
J. Bacteriol.
183
2691-2695
2001
Escherichia coli (P39453)
Manually annotated by BRENDA team
Jourlin, C.; Ansaldi, M.; Mejean, V.
Transphosphorylation of the TorR response regulator requires the three phosphorylation sites of the TorS unorthodox sensor in Escherichia coli
J. Mol. Biol.
267
770-777
1997
Escherichia coli (P39453)
Manually annotated by BRENDA team
Jourlin, C.; Bengrine, A.; Chippaux, M.; Mejean, V.
An unorthodox sensor protein (TorS) mediates the induction of the tor structural genes in response to trimethylamine N-oxide in Escherichia coli
Mol. Microbiol.
20
1297-1306
1996
Escherichia coli, Escherichia coli (P39453)
Manually annotated by BRENDA team
Simon, G.; Mejean, V.; Jourlin, C.; Chippaux, M.; Pascal, M.C.
The torR gene of Escherichia coli encodes a response regulator protein involved in the expression of the trimethylamine N-oxide reductase genes
J. Bacteriol.
176
5601-5606
1994
Escherichia coli (P39453)
Manually annotated by BRENDA team
Sperandio, V.; Torres, A.G.; Kaper, J.B.
Quorum sensing Escherichia coli regulators B and C (QseBC): a novel two-component regulatory system involved in the regulation of flagella and motility by quorum sensing in E. coli
Mol. Microbiol.
43
809-821
2002
Escherichia coli, Escherichia coli (P40719), Escherichia coli (Q8X524)
Manually annotated by BRENDA team
Munson, G.P.; Lam, D.L.; Outten, F.W.; O'Halloran, T.V.
Identification of a copper-responsive two-component system on the chromosome of Escherichia coli K-12
J. Bacteriol.
182
5864-5871
2000
Escherichia coli (P77485)
Manually annotated by BRENDA team
Ingmer, H.; Miller, C.A.; Cohen, S.N.
Destabilized inheritance of pSC101 and other Escherichia coli plasmids by DpiA, a novel two-component system regulator
Mol. Microbiol.
29
49-59
1998
Escherichia coli, Escherichia coli (P77510)
Manually annotated by BRENDA team
Canellakis, E.S.; Paterakis, A.A.; Huang, S.C.; Panagiotidis, C.A.; Kyriakidis, D.A.
Identification, cloning, and nucleotide sequencing of the ornithine decarboxylase antizyme gene of Escherichia coli
Proc. Natl. Acad. Sci. USA
90
7129-7133
1993
Escherichia coli, Escherichia coli (Q06067)
Manually annotated by BRENDA team
Perna, N.T.; Plunkett, G.; Burland, V.; Mau, B.; Glasner, J.D.; et al.
Genome sequence of enterohaemorrhagic Escherichia coli O157:H7
Nature
409
529-533
2001
Escherichia coli, Escherichia coli (P0AE83), Escherichia coli (P0AEC7), Escherichia coli (P0AEC8), Escherichia coli (P0AFB6), Escherichia coli (P58356), Escherichia coli (P58363), Escherichia coli (P58402), Escherichia coli (Q8X524), Escherichia coli (Q8X614)
Manually annotated by BRENDA team
Hayashi, T.; Makino, K.; Ohnishi, M.; Kurokawa, K.; Ishii, K.; et al.
Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12
DNA Res.
8
11-22
2001
Escherichia coli, Escherichia coli (P0AE83), Escherichia coli (P0AEC7), Escherichia coli (P0AFB6), Escherichia coli (P58356), Escherichia coli (P58363), Escherichia coli (P58402), Escherichia coli (Q8X524)
Manually annotated by BRENDA team
Blattner, F.R.; Plunkett, G.; Bloch, C.A.; Perna, N.T.; et al.
The complete genome sequence of Escherichia coli K-12
Science
277
1453-1474
1997
Escherichia coli, Escherichia coli (P07363), Escherichia coli (P08400), Escherichia coli (P0AEC3), Escherichia coli (P0AEC7), Escherichia coli (P0AEJ4), Escherichia coli (P0DMC5), Escherichia coli (P18392), Escherichia coli (P21865), Escherichia coli (P23837), Escherichia coli (P27896), Escherichia coli (P30847), Escherichia coli (P30855), Escherichia coli (P39453), Escherichia coli (P40719), Escherichia coli (P77485), Escherichia coli (P77510), Escherichia coli (Q06067), Escherichia coli (Q8X614)
Manually annotated by BRENDA team
Oshima, T.; Aiba, H.; Baba, T.; Fujita, K.; Hayashi, K.; Honjo, A.; et al.
A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map
DNA Res.
3
137-155
1996
Escherichia coli, Escherichia coli (P21865), Escherichia coli (P23837), Escherichia coli (P77485), Escherichia coli (P77510), Pseudomonas aeruginosa (P33639)
Manually annotated by BRENDA team
Itoh, T.; Aiba, H.; Baba, T.; Hayashi, K.; Inada, T.; Isono, K.; et al.
A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map
DNA Res.
3
379-392
1996
Escherichia coli (P07363), Escherichia coli (P0DMC5), Escherichia coli (P30847), Escherichia coli (Q06067)
Manually annotated by BRENDA team
Khorchid, A.; Inouye, M.; Ikura, M.
Structural characterization of Escherichia coli sensor histidine kinase EnvZ: the periplasmic C-terminal core domain is critical for homodimerization
Biochem. J.
385
255-264
2005
Escherichia coli
Manually annotated by BRENDA team
Qin, L.; Cai, S.; Zhu, Y.; Inouye, M.
Cysteine-scanning analysis of the dimerization domain of EnvZ, an osmosensing histidine kinase
J. Bacteriol.
185
3429-3435
2003
Escherichia coli
Manually annotated by BRENDA team
Cai, S.J.; Khorchid, A.; Ikura, M.; Inouye, M.
Probing catalytically essential domain orientation in histidine kinase EnvZ by targeted disulfide crosslinking
J. Mol. Biol.
328
409-418
2003
Escherichia coli (P0AEJ4)
Manually annotated by BRENDA team
Boyd, J.M.
Localization of the histidine kinase PilS to the poles of Pseudomonas aeruginosa and identification of a localization domain
Mol. Microbiol.
36
153-162
2000
Escherichia coli, Pseudomonas aeruginosa
Manually annotated by BRENDA team
Khorchid, A.; Ikura, M.
Bacterial histidine kinase as signal sensor and transducer
Int. J. Biochem. Cell Biol.
38
307-312
2006
Escherichia coli, Salmonella enterica, Sinorhizobium meliloti
Manually annotated by BRENDA team
Etzkorn, M.; Kneuper, H.; Duennwald, P.; Vijayan, V.; Kraemer, J.; Griesinger, C.; Becker, S.; Unden, G.; Baldus, M.
Plasticity of the PAS domain and a potential role for signal transduction in the histidine kinase DcuS
Nat. Struct. Mol. Biol.
15
1031-1039
2008
Escherichia coli (P0AEC8)
Manually annotated by BRENDA team
Moore, J.O.; Hendrickson, W.A.
Structural analysis of sensor domains from the TMAO-responsive histidine kinase receptor TorS
Structure
17
1195-1204
2009
Escherichia coli, Escherichia coli (P39453), Vibrio parahaemolyticus, Vibrio parahaemolyticus EB101
Manually annotated by BRENDA team
Filippou, P.S.; Kasemian, L.D.; Panagiotidis, C.A.; Kyriakidis, D.A.
Functional characterization of the histidine kinase of the E. coli two-component signal transduction system AtoS-AtoC
Biochim. Biophys. Acta
1780
1023-1031
2008
Escherichia coli
Manually annotated by BRENDA team
Mueller-Premru, M.; Zidar, N.; Spik, V.C.; Krope, A.; Kikelj, D.
Benzoxazine series of histidine kinase inhibitors as potential antimicrobial agents with activity against enterococci
Chemotherapy
55
414-417
2009
Enterococcus faecalis, Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus
Manually annotated by BRENDA team
Scheu, P.; Sdorra, S.; Liao, Y.F.; Wegner, M.; Basche, T.; Unden, G.; Erker, W.
Polar accumulation of the metabolic sensory histidine kinases DcuS and CitA in Escherichia coli
Microbiology
154
2463-2472
2008
Escherichia coli
Manually annotated by BRENDA team
Buelow, D.R.; Raivio, T.L.
Three (and more) component regulatory systems - auxiliary regulators of bacterial histidine kinases
Mol. Microbiol.
75
547-566
2010
Bacillus subtilis, Bordetella pertussis, Caulobacter vibrioides, Escherichia coli, Sinorhizobium meliloti, Vibrio harveyi (P54302)
Manually annotated by BRENDA team
Cheung, J.; Hendrickson, W.A.
Structural analysis of ligand stimulation of the histidine kinase NarX
Structure
17
190-201
2009
Escherichia coli, Escherichia coli (P0AFA2)
Manually annotated by BRENDA team
Affandi, T.; Issaian, A.V.; McEvoy, M.M.
The structure of the periplasmic sensor domain of the histidine kinase CusS shows unusual metal ion coordination at the dimeric interface
Biochemistry
55
5296-5306
2016
Escherichia coli, Escherichia coli (P77485)
Manually annotated by BRENDA team
Gudipaty, S.A.; McEvoy, M.M.
The histidine kinase CusS senses silver ions through direct binding by its sensor domain
Biochim. Biophys. Acta
1844
1656-1661
2014
Escherichia coli, Escherichia coli (P77485)
Manually annotated by BRENDA team
Eguchi, Y.; Utsumi, R.
Alkali metals in addition to acidic pH activate the EvgS histidine kinase sensor in Escherichia coli
J. Bacteriol.
196
3140-3149
2014
Escherichia coli, Escherichia coli (P30855)
Manually annotated by BRENDA team
Ferris, H.U.; Coles, M.; Lupas, A.N.; Hartmann, M.D.
Crystallographic snapshot of the Escherichia coli EnvZ histidine kinase in an active conformation
J. Struct. Biol.
186
376-379
2014
Escherichia coli, Escherichia coli (P0AEJ4)
Manually annotated by BRENDA team
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