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Information on EC 2.7.13.3 - histidine kinase and Organism(s) Synechocystis sp. and UniProt Accession Q55168

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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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This record set is specific for:
Synechocystis sp.
UNIPROT: Q55168
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Word Map
The taxonomic range for the selected organisms is: Synechocystis sp.
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phytochrome-like protein cph1 (light-regulated histidine)
-
drug sensory protein A
-
Hik34
histidine kinase
-
-
histidine kinase 34
-
histidine kinase Hik10
-
-
histidine kinase Hik16
-
-
histidine kinase Hik33
-
-
histidine kinase Hik34
-
-
histidine kinase Hik41
-
-
Ni2+-sensing histidine kinase NrsS
-
-
phosphate-sensing histidine kinase SphS
-
-
sensory transduction histidine kinase
UniProt
slr1147
locus name
Slr1759
-
Slr1759 is a multidomain hybrid histidine kinase
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
Rcp1 + ATP
?
show the reaction diagram
Cph1 is a light-regulated histidine kinase that mediates red, far-red reversible phosphorylation of the a small response regulator Rcp1
-
-
?
ATP + histidine kinase Hik34
ADP + histidine kinase Hik34 N-phospho-L-histidine
show the reaction diagram
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
show the reaction diagram
additional information
?
-
the enzyme is involved in chemical sensing
-
-
?
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
Rcp1 + ATP
?
show the reaction diagram
Cph1 is a light-regulated histidine kinase that mediates red, far-red reversible phosphorylation of the a small response regulator Rcp1
-
-
?
ATP + histidine kinase Hik34
ADP + histidine kinase Hik34 N-phospho-L-histidine
show the reaction diagram
-
histidine kinase Hik34 might negatively regulate the expression of certain heat shock genes that might by related to thermotolerance in Synechocystis
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
show the reaction diagram
additional information
?
-
the enzyme is involved in chemical sensing
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
-
Slr1759-Var I protein contains 0.11-0.26 mM cofactor per 1 mM protein
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cl-
activates, the signal input domain of Hik2 responds to environmental Cl- concentration, key for induction of activity
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ssl3451 protein
-
enhances the autophosphorylation activity of the histidine kinase Hik33 by associating with it with a 1:1 stoichiometry both in vitro and in vivo, but does not affect its dephosphorylation
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain PCC 6803
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
optimal growth temperature for Synechocystis is 32-38°C, for both wild-type and DELTAHik34 mutant strains showing the same growth rates
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
74500
x * 74500
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
the Cph1 protein forms dimers through the C-terminal region
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D156A
site-directed mutagenesis, the point mutant of recombinant fused sensor, Hik2n-Hik7c construct is inactive in alkaline phosphatase activity
D300A
site-directed mutagenesis, the mutation might change the dimeric configuration of the PAS domain, thereby enhancing the negative effect on kinase activity. The D300A-mutated PAS domain of Hik33 also forms dimer in the assay. The Hik33n-SphSc mutant shows reduced expression under non-stressed and salt-stressed conditions compared to unaltered Hik33n-SphSc
D389A
site-directed mutagenesis, the Hik33n-SphSc mutant shows only slightly reduced expression under non-stressed conditions and highly reduced expression under salt-stressed conditions compared to unaltered Hik33n-SphSc
D412N
site-directed mutagenesis, the Hik33n-SphSc mutant shows only slightly reduced expression under non-stressed conditions and highly reduced expression under salt-stressed conditions compared to unaltered Hik33n-SphSc
E416Q
site-directed mutagenesis, the Hik33n-SphSc mutant shows normal expression under non-stressed conditions and highly reduced expression under salt-stressed conditions compared to unaltered Hik33n-SphSc
G123A
site-directed mutagenesis, the point mutant of recombinant fused sensor, Hik2n-Hik7c construct is inactive in alkaline phosphatase activity
G405A
site-directed mutagenesis, the Hik33n-SphSc mutant shows only slightly reduced expression under non-stressed conditions and highly reduced expression under salt-stressed conditions compared to unaltered Hik33n-SphSc
G405S
site-directed mutagenesis, the Hik33n-SphSc mutant shows only slightly reduced expression under non-stressed conditions and no expression under salt-stressed conditions compared to unaltered Hik33n-SphSc
N309A
site-directed mutagenesis, the Hik33n-SphSc mutant shows only slightly reduced expression under non-stressed conditions and highly reduced expression under salt-stressed conditions compared to unaltered Hik33n-SphSc
P114A
site-directed mutagenesis, the point mutant of recombinant fused sensor, Hik2n-Hik7c construct is inactive in alkaline phosphatase activity
Q141A
site-directed mutagenesis, the point mutant of recombinant fused sensor, Hik2n-Hik7c construct is inactive in alkaline phosphatase activity
Q22A
site-directed mutagenesis, the point mutant of recombinant fused sensor, Hik2nHik7c construct is inactive in alkaline phosphatase activity
Q411E
site-directed mutagenesis, the Hik33n-SphSc mutant shows normal expression under non-stressed conditions and highly reduced expression under salt-stressed conditions compared to unaltered Hik33n-SphSc
R129K
site-directed mutagenesis, the point mutant of recombinant fused sensor, Hik2n-Hik7c construct is inactive in alkaline phosphatase activity
R377A
site-directed mutagenesis, the Hik33n-SphSc mutant shows only slightly reduced expression under non-stressed conditions and highly reduced expression under salt-stressed conditions compared to unaltered Hik33n-SphSc
R400S/R404A
site-directed mutagenesis, the Hik33n-SphSc mutant shows normal expression under non-stressed conditions and highly reduced expression under salt-stressed conditions compared to unaltered Hik33n-SphSc
R404A
site-directed mutagenesis, the Hik33n-SphSc mutant shows normal expression under non-stressed conditions and highly reduced expression under salt-stressed conditions compared to unaltered Hik33n-SphSc
R415E
site-directed mutagenesis, the mutation might change the dimeric configuration of the PAS domain, thereby enhancing the negative effect on kinase activity. The Hik33n-SphSc mutant shows reduced expression under non-stressed and salt-stressed conditions compared to unaltered Hik33n-SphSc
T409V
site-directed mutagenesis, the Hik33n-SphSc mutant shows only slightly reduced expression under non-stressed conditions and no expression under salt-stressed conditions compared to unaltered Hik33n-SphSc
T414V
site-directed mutagenesis, the Hik33n-SphSc mutant shows only slightly reduced expression under non-stressed conditions and no expression under salt-stressed conditions compared to unaltered Hik33n-SphSc
V395A
site-directed mutagenesis, the Hik33n-SphSc mutant shows only slightly reduced expression under non-stressed conditions and highly reduced expression under salt-stressed conditions compared to unaltered Hik33n-SphSc
W134F
site-directed mutagenesis, the point mutant of recombinant fused sensor, Hik2n-Hik7c construct is inactive in alkaline phosphatase activity
W318A
site-directed mutagenesis, the mutation might change the dimeric configuration of the PAS domain, thereby enhancing the negative effect on kinase activity. The W318A-mutated PAS domain of Hik33 also forms dimer in the assay. The Hik33n-SphSc mutant shows reduced expression under non-stressed and salt-stressed conditions compared to unaltered Hik33n-SphSc
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
coexpressed with a bacterial thioredoxin in Escherichia coli
HiTrap chelating column chromatography
-
Ni-NTA column chromatography
-
Ni-NTA column chromatography and glutathione Sepharose column chromatography
-
recombinant
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
-
gene hik33, the chimeric gene for Hik33n-SphSc, integrated into the chromosomes, is expressed in Synechocystis from the original promoter of the sphS gene, and the copy number of each chimeric gene is exactly one per chromosome, subcloning in Escherichia coli strain JM109. Quantitative expression analysis of unaltered Hik33n-SphSc chimera and mutants under non-stressed conditions and salt-stressed conditions, overview
gene sphS, the chimeric gene for Hik33n-SphSc, integrated into the chromosomes, is expressed in Synechocystis from the original promoter of the sphS gene, and the copy number of each chimeric gene is exactly one per chromosome, subcloning in Escherichia coli strain JM109. Quantitative expression analysis of unaltered Hik33n-SphSc chimera and mutants under non-stressed conditions and salt-stressed conditions, overview
overexpression in Escherichia coli, histidine kinase Hik34
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
the refolded recombinant protein is obtained by gradual removal of 6 M urea by sequential dialysis
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bartsevich, V.V.; Shestakov, S.V.
The dspA gene product of the cyanobacterium Synechocystis sp. strain PCC 6803 influences sensitivity to chemically different growth inhibitors and has amino acid similarity to histidine protein kinases
Microbiology
141
2915-2920
1995
Synechocystis sp. (P20169)
-
Manually annotated by BRENDA team
Kaneko, T.; Sato, S.; Kotani, H.; et al.
Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions
DNA Res.
3
109-136
1996
Synechocystis sp. (P20169)
Manually annotated by BRENDA team
Reilly, P.; Hulmes, J.D.; Pan, Y.C.; Nelson, N.
Molecular cloning and sequencing of the psaD gene encoding subunit II of photosystem I from the cyanobacterium, Synechocystis sp. PCC 6803
J. Biol. Chem.
263
17658-17662
1988
Synechocystis sp. (P20169)
Manually annotated by BRENDA team
Kaneko, T.; Tanaka, A.; Sato, S.; Kotani, H.; Sazuka, T.; Miyajima, N.; Sugiura, M.; Tabata, S.
Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64% to 92% of the genome
DNA Res.
2; 153-166
191-158
1995
Synechocystis sp. (Q55168)
-
Manually annotated by BRENDA team
Park, C.M.; Shim, J.Y.; Yang, S.S.; Kang, J.G.; Kim, J.I.; Luka, Z.; Song, P.S.
Chromophore-apoprotein interactions in Synechocystis sp. PCC6803 phytochrome Cph1
Biochemistry
39
6349-6356
2000
Synechocystis sp. (Q55168)
Manually annotated by BRENDA team
Yeh, K.C.; Wu, S.H.; Murphy, J.T.; Lagarias, J.C.
A cyanobacterial phytochrome two-component light sensory system
Science
277
1505-1508
1997
Synechocystis sp. (Q55168)
Manually annotated by BRENDA team
Paithoonrangsarid, K.; Shoumskaya, M.A.; Kanesaki, Y.; Satoh, S.; Tabata, S.; Los, D.A.; Zinchenko, V.V.; Hayashi, H.; Tanticharoen, M.; Suzuki, I.; Murata, N.
Five histidine kinases perceive osmotic stress and regulate distinct sets of genes in Synechocystis
J. Biol. Chem.
279
53078-53086
2004
Synechocystis sp.
Manually annotated by BRENDA team
Suzuki, I.; Kanesaki, Y.; Hayashi, H.; Hall, J.J.; Simon, W.J.; Slabas, A.R.; Murata, N.
The histidine kinase Hik34 is involved in thermotolerance by regulating the expression of heat shock genes in Synechocystis
Plant Physiol.
138
1409-1421
2005
Synechocystis sp.
Manually annotated by BRENDA team
Marin, K.; Suzuki, I.; Yamaguchi, K.; Ribbeck, K.; Yamamoto, H.; Kanesaki, Y.; Hagemann, M.; Murata, N.
Identification of histidine kinases that act as sensors in the perception of salt stress in Synechocystis sp. PCC 6803
Proc. Natl. Acad. Sci. USA
100
9061-9066
2003
Synechocystis sp.
Manually annotated by BRENDA team
Murata, N.; Los, D.A.
Histidine kinase Hik33 is an important participant in cold-signal transduction in cyanobacteria
Physiol. Plant.
126
17-27
2006
Synechocystis sp.
-
Manually annotated by BRENDA team
Kanesaki, Y.; Yamamoto, H.; Paithoonrangsarid, K.; Shoumskaya, M.; Suzuki, I.; Hayashi, H.; Murata, N.
Histidine kinases play important roles in the perception and signal transduction of hydrogen peroxide in the cyanobacterium, Synechocystis sp. PCC 6803
Plant J.
49
313-324
2007
Synechocystis sp.
Manually annotated by BRENDA team
Michel, K.P.; Schroeder, A.K.; Zimmermann, M.; Brandt, S.; Pistorius, E.K.; Frankenberg-Dinkel, N.; Staiger, D.
The hybrid histidine kinase Slr1759 of the cyanobacterium Synechocystis sp. PCC 6803 contains FAD at its PAS domain
Arch. Microbiol.
191
553-559
2009
Synechocystis sp.
Manually annotated by BRENDA team
Kimura, S.; Shiraiwa, Y.; Suzuki, I.
Function of the N-terminal region of the phosphate-sensing histidine kinase, SphS, in Synechocystis sp. PCC 6803
Microbiology
155
2256-2264
2009
Synechocystis sp.
Manually annotated by BRENDA team
Sakayori, T.; Shiraiwa, Y.; Suzuki, I.
A Synechocystis homolog of SipA protein, Ssl3451, enhances the activity of the histidine kinase Hik33
Plant Cell Physiol.
50
1439-1448
2009
Synechocystis sp.
Manually annotated by BRENDA team
Kotajima, T.; Shiraiwa, Y.; Suzuki, I.
Functional analysis of the N-terminal region of an essential histidine kinase, Hik2, in the cyanobacterium Synechocystis sp. PCC 6803
FEMS Microbiol. Lett.
351
88-94
2014
Synechocystis sp. (P73276), Synechocystis sp.
Manually annotated by BRENDA team
Cerveny, J.; Sinetova, M.A.; Zavrel, T.; Los, D.A.
Mechanisms of high temperature resistance of Synechocystis sp. PCC 6803: an impact of histidine kinase 34
Life
5
676-699
2015
Synechocystis sp. (P73276), Synechocystis sp.
Manually annotated by BRENDA team
Shimura, Y.; Shiraiwa, Y.; Suzuki, I.
Characterization of the subdomains in the N-terminal region of histidine kinase Hik33 in the cyanobacterium Synechocystis sp. PCC 6803
Plant Cell Physiol.
53
1255-1266
2012
Synechocystis sp., Synechocystis sp. (Q55586)
Manually annotated by BRENDA team