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Information on EC 2.7.13.3 - histidine kinase and Organism(s) Streptomyces coelicolor and UniProt Accession Q04943
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2.7.13.3 histidine kinaseIUBMB 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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Word Map
- 2.7.13.3
- autophosphorylation
- photoreceptors
-
far-red
- seedling
-
phosphorelay
- chromophore
-
perception
-
regulons
- hypocotyls
-
quorum
-
perceived
- pfr
-
chemoreceptor
-
senses
-
light-induced
- chey
-
flagellar
- synechocystis
-
etiolated
- caulobacter
-
photomorphogenesis
-
transmitter
-
quorum-sensing
-
fluence
- biliverdin
-
cryptochrome
- crescentus
-
methyl-accepting
-
dark-grown
- radiodurans
-
transphosphorylation
-
autoinducer
-
histidine-containing
-
chemosensory
-
photomorphogenic
-
extracytoplasmic
- arca
- deinococcus
- phototropins
- tetrapyrrole
- ompc
- c-di-gmp
-
diguanylate
- spo0a
-
four-helix
-
gravitropism
-
photoresponses
-
non-cognate
- xanthus
-
photoisomerization
- synthesis
- medicine
The taxonomic range for the selected organisms is: Streptomyces coelicolor
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
histidine kinase, sensor kinase, sensor protein, phytochrome a, ethylene receptor, sensor histidine kinase, bacteriophytochrome, ornithine decarboxylase antizyme, chemotaxis protein, hybrid histidine kinase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SCO3062
two-component system histidine kinase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
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
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)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
?
ATP + DraR L-histidine
ADP + DraR N-phospho-L-histidine
-
-
-
?
ATP + DraR L-histidine
ADP + DraR N-phospho-L-histidine
autophosphorylation of DraK and subsequent phosphotransfer to its cognate response regulator protein DraR
-
-
?
additional information
?
-
the two-component regulatory system afsQ1/afsQ2 is involved in secondary metabolism
-
-
?
additional information
?
-
the cutR-cutS operon regulates copper metabolism in Streptomyces
-
-
?
additional information
?
-
a histidine kinase plays a role not only in the phosphorylation of its cognate response regulator but also in the dephosphorylation of the phosphorylated response regulator, acting as both kinase and phosphatase
-
-
?
additional information
?
-
-
a histidine kinase plays a role not only in the phosphorylation of its cognate response regulator but also in the dephosphorylation of the phosphorylated response regulator, acting as both kinase and phosphatase
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + DraR L-histidine
ADP + DraR N-phospho-L-histidine
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
?
additional information
?
-
the two-component regulatory system afsQ1/afsQ2 is involved in secondary metabolism
-
-
?
additional information
?
-
the cutR-cutS operon regulates copper metabolism in Streptomyces
-
-
?
additional information
?
-
a histidine kinase plays a role not only in the phosphorylation of its cognate response regulator but also in the dephosphorylation of the phosphorylated response regulator, acting as both kinase and phosphatase
-
-
?
additional information
?
-
-
a histidine kinase plays a role not only in the phosphorylation of its cognate response regulator but also in the dephosphorylation of the phosphorylated response regulator, acting as both kinase and phosphatase
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
mechanism for the pH-dependent conformational change of the extracellular sensor domain of the DraK protein involving residues E83, E105, and E107 with very high pKa values, overview
additional information
-
mechanism for the pH-dependent conformational change of the extracellular sensor domain of the DraK protein involving residues E83, E105, and E107 with very high pKa values, overview
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
additional information
physiological function
DraK is a sensory histidine kinase involved in the differential regulation of antibiotics in Streptomyces coelicolor through the DraR/DraK two-component system
physiological function
the DraR/DraK two-component system (TCS) of Streptomyces coelicolor is involved in the differential regulation of antibiotic biosynthesis. The extracellular sensory domain of histidine kinase DraK shows a pH-dependent conformational change involved in signal transduction process of DraR/DraK TCS. At low pH, the extracellular sensory domain is more structured than that at high pH. In particular, the glutamate at position 83 is an important residue for the pH-dependent conformational change
physiological function
the DraR/DraK two-component system is involved in the differential regulation of antibiotic biosynthesis in a medium-dependent manner, the DraR/DraK two-component system plays an important role in the pH regulation of Streptomyces coelicolor growth medium. The enzyme and the DraR/DraK two-component system are essential for the recovery of the pH of Streptomyces coelicolor growth medium after acid shock, overview
additional information
mechanism for the pH-dependent conformational change of the extracellular sensor domain of DraK protein involving residues E83, E105, and E107 with very high pKa values, overview
additional information
-
mechanism for the pH-dependent conformational change of the extracellular sensor domain of DraK protein involving residues E83, E105, and E107 with very high pKa values, overview
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
histidine kinases are composed of an N-terminal sensory (or input) domain, which senses external stimuli, and a conserved kinase domain, which contains an N-terminal dimerization and histidine phosphotransfer domain and a catalytic and ATP binding (CA) domain
additional information
additional information
enzyme DraK consists of an extracellular domain flanked by two transmembrane helices (Leu5-Val27 and Leu126-Ile145), a sensory domain (Glu28-Thr125), a HAMP (histidine kinases, adenylyl cyclases, methyl-accepting chemotaxis proteins and phosphatases) domain (Asn149-Thr201) and a kinase domain (Ala202-Pro410) composed of His KA and CA domains
additional information
-
enzyme DraK consists of an extracellular domain flanked by two transmembrane helices (Leu5-Val27 and Leu126-Ile145), a sensory domain (Glu28-Thr125), a HAMP (histidine kinases, adenylyl cyclases, methyl-accepting chemotaxis proteins and phosphatases) domain (Asn149-Thr201) and a kinase domain (Ala202-Pro410) composed of His KA and CA domains
additional information
mechanism for the pH-dependent conformational change of the the extracellular sensor domain protein of DraK, overview. The structure contains a mixed alpha-beta fold, adopting a fold similar to the ubiquitous sensor domain of histidine kinase
additional information
-
mechanism for the pH-dependent conformational change of the the extracellular sensor domain protein of DraK, overview. The structure contains a mixed alpha-beta fold, adopting a fold similar to the ubiquitous sensor domain of histidine kinase
additional information
monomer-dimer equilibrium of the shortened extracellular sensing domain of DraK in solution, with MWs of 9.7 kDa for the monomeric and 19.4 kDa for the dimeric form
additional information
-
monomer-dimer equilibrium of the shortened extracellular sensing domain of DraK in solution, with MWs of 9.7 kDa for the monomeric and 19.4 kDa for the dimeric form
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant N-terminally His6-tagged extracellular sensory domain of DraK, sitting drop vapour diffusion method, mixing 200 nl of of 12 mg/ml protein in 10 mM sodium acetate, pH 4.5, and 100 mM NaCl with reservoir solution containing 0.2 M potassium/sodium tartrate, and 20% PEG 3350, and equilibration against 0.070 ml of reservoir solution, 20°C, X-ray diffraction structure determination and analysis at 2.2 A resolution, molecular replacement
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E105A
site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type
E105L
site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type
E105Q
site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type
E107A
site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type
E107L
site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type
E107Q
site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type
E83A
site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type
E83L
site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type
E83L/E105L/E107A
site-directed mutagenesis, the mutant is pH-independent and mimics the low pH structure
E83Q
site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type
additional information
additional information
generation of and draK gene deletion mutants, the gene disruption plasmids pKC-3063A and pKC-3062B are delivered into Streptomyces coelicolor A3(2) cells by conjugation with Escherichia coli ET12567(pUZ8002), and intergeneric conjugation between Escherichia coli and Streptomyces is performed, altered pH profile after acidic pH shock cultivation of the draR and draK gene deletion mutants, overview
additional information
-
generation of and draK gene deletion mutants, the gene disruption plasmids pKC-3063A and pKC-3062B are delivered into Streptomyces coelicolor A3(2) cells by conjugation with Escherichia coli ET12567(pUZ8002), and intergeneric conjugation between Escherichia coli and Streptomyces is performed, altered pH profile after acidic pH shock cultivation of the draR and draK gene deletion mutants, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA resin column chromatography, Q-Sepharose resin column chromatography, and Superdex 75 gel filtration
-
recombinant GST-tagged extracellular sensing domain proteins from Escherichia coli strain BL21 by glutathione affinity chromatography, tag cleavage by thrombin
recombinant N-terminally His6-tagged extracellular sensory domain of DraK from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, gel filtration, and ultrafiltration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of the extracellular sensory domain of DraK, consisting of 88 residues (Glu28-Arg115) from genomic DNA, and overexpression as N-terminally His6-tagged protein in Escherichia coli strain BL21(DE3)
gene SCO3062, recombinant expression of N-terminally GST-tagged extracellular sensing domain (residues 28E-124R), and cytoplasmic domain (residues 146R-424R) of DraK in Escherichia coli strain BL21. Because the extracellular sensing domain of DraK is sensitive to proteolysis during purification, the C-terminal truncated short form (residues 28E-115R) is also constructed without the unstable C-terminal sequence (residues 116S-124R) after determination of the cleavage site (residues 115R-116S) in the extracellular sensing domain
recombinant expression of wild-type and mutant enzymes in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tseng, H.C.; Chen, C.W.
A cloned ompR-like gene of Streptomyces lividans 66 suppresses defective melC1, a putative copper-transfer gene
Mol. Microbiol.
5
1187-1196
1991
Streptomyces coelicolor (P0A4I7)
Ishizuka, H.; Horinouchi, S.; Kieser, H.M.; Hopwood, D.A.; Beppu, T.
A putative two-component regulatory system involved in secondary metabolism in Streptomyces spp
J. Bacteriol.
174
7585-7594
1992
Streptomyces coelicolor (Q04943)
Bentley, S.D.; Chater, K.F.; Cerdeno-Tarraga, A.M.; et al.
Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)
Nature
417
141-147
2002
Streptomyces coelicolor (P0A4I7), Streptomyces coelicolor (Q04943)
Yeo, K.J.; Kwak, S.N.; Kim, H.J.; Cheong, C.; Kim, M.H.; Jeon, Y.H.
Expression and characterization of the integral membrane domain of bacterial histidine kinase SCO3062 for structural studies
Biochem. Biophys. Res. Commun.
376
409-413
2008
Streptomyces coelicolor, Streptomyces coelicolor A3(2)
Yeo, K.J.; Han, Y.H.; Eo, Y.; Cheong, H.K.
Expression, purification, crystallization and preliminary X-ray analysis of the extracellular sensory domain of DraK histidine kinase from Streptomyces coelicolor
Acta Crystallogr. Sect. F
69
909-911
2013
Streptomyces coelicolor (Q9KZ83), Streptomyces coelicolor, Streptomyces coelicolor ATCC BAA-471D (Q9KZ83)
Yeo, K.J.; Kim, E.H.; Hwang, E.; Han, Y.H.; Eo, Y.; Kim, H.J.; Kwon, O.; Hong, Y.S.; Cheong, C.; Cheong, H.K.
pH-Dependent structural change of the extracellular sensor domain of the DraK histidine kinase from Streptomyces coelicolor
Biochem. Biophys. Res. Commun.
431
554-559
2013
Streptomyces coelicolor (Q9KZ83), Streptomyces coelicolor, Streptomyces coelicolor A3(2) (Q9KZ83)
Yeo, K.J.; Hong, Y.S.; Jee, J.G.; Lee, J.K.; Kim, H.J.; Park, J.W.; Kim, E.H.; Hwang, E.; Kim, S.Y.; Lee, E.G.; Kwon, O.; Cheong, H.K.
Mechanism of the pH-induced conformational change in the sensor domain of the DraK histidine kinase via the E83, E105, and E107 residues
PLoS ONE
9
e107168
2014
Streptomyces coelicolor (Q9KZ83), Streptomyces coelicolor, Streptomyces coelicolor ATCC BAA-471 (Q9KZ83)
EXTERNAL LINKS (specific for EC-Number 2.7.13.3)
Transporter Classification Database (TCDB): 9.B.33.1.1, 9.B.238.3.5, 9.B.33.1.2, 2.A.21.9.1, 2.A.21.9.2, 2.A.123.2.13
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