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Information on EC 2.7.13.3 - histidine kinase and Organism(s) Caulobacter vibrioides and UniProt Accession Q9RQQ9
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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: Caulobacter vibrioides
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
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 + a protein
ADP + a phosphoprotein
the tyrosine kinase DivL function in cell cycle and developmental regulation is mediated, at least in part, by the global response regulator CtrA, the enzyme is essential for cell viability and division
-
-
?
protein + ATP
?
DivL protein is homologous to the ubiquitous bacterial histidine protein kinases, it differs from previously studied members of this protein kinase family in that it contains a tyrosine residue Tyr550 in the conserved H-box instead of a histidine residue, which is the expected site of autophosphorylation. DivL is autophosphorylated on Tyr-550 in vitro, and this tyrosine residue is essential for cell viability and regulation of the cell division cycle
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
histidine kinases DivJ and PleC initiate signal transduction pathways that regulate an early cell division cycle step and the gain of motility later in the Caulobacter crescentus cell cycle
-
-
?
additional information
?
-
measurement of the enzyme's ATPase activity
-
-
?
additional information
?
-
-
measurement of the enzyme's ATPase activity
-
-
?
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 + a protein
ADP + a phosphoprotein
the tyrosine kinase DivL function in cell cycle and developmental regulation is mediated, at least in part, by the global response regulator CtrA, the enzyme is essential for cell viability and division
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
histidine kinases DivJ and PleC initiate signal transduction pathways that regulate an early cell division cycle step and the gain of motility later in the Caulobacter crescentus cell cycle
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
CckA has a central role in establishing the cell cycle periodicity of CtrA activity by controlling both its phosphorylation and stability
additional information
additional information
effect of the nonconserved flanking sequence on the signaling lifetime of LovK, the effects of structure outside the LOV core on its signaling lifetime do not combine in a simple, additive way. Kinetics of recovery from the adduct state depend not only on the buffer environment but also on the structural context in which the LOV domain is contained. Full-length LovK (residues 1-368) has a long recovery, with a half-life of 2 h, the isolated LOV core (residues 25-138) recovers more quickly, with a half-life of 37 min. LovK (25-163), which contains the LOV core and the nonconserved linker sequence at its C-terminus, has a recovery half-life of 28 min. A construct containing the LOV core and the nonconserved N-terminal flanking sequence, LovK(1-138), has a half-life of only 2 min, but this N-terminal region has not a general rate enhancement effect. LovK(1-163), a construct with fully intact N- and C-termini (but missing the kinase domain), is slower to recover than either LovK(25-138), LovK(1-138), or LovK(25-163)
additional information
-
effect of the nonconserved flanking sequence on the signaling lifetime of LovK, the effects of structure outside the LOV core on its signaling lifetime do not combine in a simple, additive way. Kinetics of recovery from the adduct state depend not only on the buffer environment but also on the structural context in which the LOV domain is contained. Full-length LovK (residues 1-368) has a long recovery, with a half-life of 2 h, the isolated LOV core (residues 25-138) recovers more quickly, with a half-life of 37 min. LovK (25-163), which contains the LOV core and the nonconserved linker sequence at its C-terminus, has a recovery half-life of 28 min. A construct containing the LOV core and the nonconserved N-terminal flanking sequence, LovK(1-138), has a half-life of only 2 min, but this N-terminal region has not a general rate enhancement effect. LovK(1-163), a construct with fully intact N- and C-termini (but missing the kinase domain), is slower to recover than either LovK(25-138), LovK(1-138), or LovK(25-163)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
-
phosphorylation of CckA is required for function but is not important for polar localization
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the disruption of a PAS-like motif in the sensor domain affects the stability of CckA accumulation at the poles accompanied by a partial loss in CckA function. Shortening of an extended linker between beta-sheets within the CckA catalysis-assisting ATP-binding domain leads to a dramatic cell-to-cell variability in CpdR levels and CtrA cell cycle periodicity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type enzyme, enzyme fragments, and mutant C70A enzyme from Escherichia coli strain Rosetta(DE3)pLysS by nickel affinity chromatography, ultrafiltration, and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene CC_0285, recombinant expression of His-tagged wild-type enzyme, enzyme fragments, and mutant C70A enzyme in Escherichia coli strain Rosetta(DE3)pLysS
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nierman, W.C.; Feldblyum, T.V.; Laub, M.T.; et al.
Complete genome sequence of Caulobacter crescentus
Proc. Natl. Acad. Sci. USA
98
4136-4141
2001
Caulobacter vibrioides (Q9RQQ9)
Wu, J.; Ohta, N.; Zhao, J.L.; Newton, A.
A novel bacterial tyrosine kinase essential for cell division and differentiation
Proc. Natl. Acad. Sci. USA
96
13068-13073
1999
Caulobacter vibrioides (Q9RQQ9)
Ohta, N.; Newton, A.
The core dimerization domains of histidine kinases contain recognition specificity for the cognate response regulator
J. Bacteriol.
185
4424-4431
2003
Caulobacter vibrioides
Angelastro, P.S.; Sliusarenko, O.; Jacobs-Wagner, C.
Polar localization of the CckA histidine kinase and cell cycle periodicity of the essential master regulator CtrA in Caulobacter crescentus
J. Bacteriol.
192
539-552
2010
Caulobacter vibrioides
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)
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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