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Information on EC 2.7.13.3 - histidine kinase and Organism(s) Staphylococcus aureus and UniProt Accession Q840P7
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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: Staphylococcus aureus
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 + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
-
?
additional information
?
-
-
in vitro autokinase activity of recombinant truncated enzyme mutant AgrCTM5-6C in N,N-dimethyldodecylamine N-oxide proteoliposomes
-
-
?
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 + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
-
-
Zn2+
Zn2+ binding negatively regulates the WalKR regulon. Zn2+ binding directly influences the relative positioning of the PAS and catalytic domains of WalK
additional information
-
YycH and YycI are two auxiliary membrane proteins that inhibit the activity of YycG HK in Bacillus subtilis. Both YycH and YycI are required to inhibit the dimerization of YycG
-
additional information
YycH and YycI are two auxiliary membrane proteins that inhibit the activity of YycG HK in Bacillus subtilis. Both YycH and YycI are required to inhibit the dimerization of YycG
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
auto-inducible protein I
-
dose-dependent activation by autoinducing peptide
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinase activity of recombinant enzyme AgrCTM5-6C in N,N-dimethyldodecylamine N-oxide micelles or proteoliposomes
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
an integral membrane protein, protein transmembrane topology in proteoliposomes is determined using membrane-impermeable and membrane-permeable thiol-reactive reagents, overview
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
the AgrC receptor histidine kinase detects its autoinducing peptide ligand and generates an intracellular signal resulting in secretion of virulence factors
physiological function
-
the integral membrane protein AgrC is a histidine kinase whose sensor domains interact with an autoinducing peptide, resulting in a series of downstream responses
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
oligomer
intact YycG HK can form higher-order oligomers at the cell membrane via combinations of the H- and L-dimeric interacting surfaces
additional information
dimer
-
AgrC forms ligand-independent dimers that undergo trans-autophosphorylation upon interaction with autoinducing peptide
dimer
the extracellular domain of enzyme YycG exhibits two dimerization modes, dimerization configurations, cross-linking experiments, overview. Both YycH and YycI are required to inhibit the dimerization of YycG
additional information
-
Both YycH and YycI are required to inhibit the dimerization of YycG. Genes yycH and yycI are members of the yyc operon. The actions of YycH and YycI on YycG likely occur at the transmembrane helices, in which an octameric complex was formed by an YycG homodimer flanked by YycH-YycI heterodimers
additional information
Both YycH and YycI are required to inhibit the dimerization of YycG. Genes yycH and yycI are members of the yyc operon. The actions of YycH and YycI on YycG likely occur at the transmembrane helices, in which an octameric complex was formed by an YycG homodimer flanked by YycH-YycI heterodimers
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
-
AgrC forms ligand-independent dimers that undergo trans-autophosphorylation upon interaction with autoinducing peptide
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure of the cytoplasmic PAS domain, residues valine 251 to arginine 376. The metal-binding site comprises a single Zn2+ ion bound by the atoms Ndelta1 from His271, Odelta1 from Asp274, Ndelta1 from His364 and Oepsilon2 from Glu368 in a slightly distorted tetrahedral coordination geometry
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H271Y
introducing the mutation into wild-type activates the WalKR regulon. Zn2+ is tetrahedrally-coordinated by four amino acids including H271. The H271Y mutation abrogates metal binding, increasing WalK kinase activity and WalR phosphorylation. The mutant strain shows increased lysostaphin and vancomycin sensitivity
N44C/G142C
site-directed mutagenesis, the monomeric band intensities of the double mutant are dramatically decreased
N44C/G143C
site-directed mutagenesis, the monomeric band intensities of the double mutant are dramatically decreased
N44C/R146C
site-directed mutagenesis, introducing cysteine substitution at Arg146 of YycG N44C mutant does not show any high molecular weight bands, but it shows only the dimeric band of YycG N44C
additional information
additional information
a point mutation in SaeS of strain Newman is responsible for increased expression of Eap upon exposure to sublethal Perform and SDS concentrations, leading to increased extracellular adherence protein-dependent cellular invasiveness
additional information
-
a point mutation in SaeS of strain Newman is responsible for increased expression of Eap upon exposure to sublethal Perform and SDS concentrations, leading to increased extracellular adherence protein-dependent cellular invasiveness
additional information
-
construction of a truncated AgrCTM5-6C enzyme version, a hydrophobic polypeptide of 297 amino acids, that has two transmembrane helices connected by a small polar loop that is exposed to the periplasm
additional information
-
cross-linking of the recombinant the SeMet-substituted YycG enzyme
additional information
cross-linking of the recombinant the SeMet-substituted YycG enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged truncated enzyme from Escherichia coli strain C43(DE3) membranes by ultracentrifugation and affinity chromatography, followed by gel filtration
-
recombinant wild-type and mutant His-tagged enzymes from Escherichia coli strain BL21(DE3) by ultracentrifugation, nickel affinity chromatography, and dialysis. His-tag removal by tobacco etch virus protease is followed by nickel affinity chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene agrC, recombinant overexpression of His-tagged and GFP-tagged truncated enzyme from pET-28a-AgrCTM5-6C or pET-28-AgrCTM5-6C-GFP vector in Escherichia coli strain C43(DE3)
-
gene yycG, recombinant expression of wild-type and mutant His-tagged enzymes in Escherichia coli strain BL21(DE3), the SeMet-substituted YycG is produced in Escherichia coli methionine auxotrophic strain B834(DE3)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
2.5fold enhanced transcription of SaeS after incubation with Perform and SDS
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
purified recombinant truncated enzyme proteins are reconstituted into liposomes by a detergent-mediated method, effect of different detergents on protein reconstitution efficiency, overview. The highest incorporation is found with N,N-dimethyldode-cylamine N-oxide resulting in a yield of 85%, liposomes are consisting of dioleoyl-phosphatidyl-choline : 1,2-dipalmitoyl-sn-glycero-3-phosphocholine : egg L-alpha-phosphatidic acid : cholesterol at molar ratios of 4:4:1:1, pH 7.4. Determination of the morphology and size of liposome, overview
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Escherichia coli, Enterococcus faecalis, Staphylococcus aureus, Pseudomonas aeruginosa
Schaefer, D.; Lam, T.T.; Geiger, T.; Mainiero, M.; Engelmann, S.; Hussain, M.; Bosserhoff, A.; Frosch, M.; Bischoff, M.; Wolz, C.; Reidl, J.; Sinha, B.
A point mutation in the sensor histidine kinase SaeS of Staphylococcus aureus strain Newman alters the response to biocide exposure
J. Bacteriol.
191
7306-7314
2009
Staphylococcus aureus (Q840P7), Staphylococcus aureus, Staphylococcus aureus Newman (Q840P7)
George Cisar, E.A.; Geisinger, E.; Muir, T.W.; Novick, R.P.
Symmetric signalling within asymmetric dimers of the Staphylococcus aureus receptor histidine kinase AgrC
Mol. Microbiol.
74
44-57
2009
Staphylococcus aureus
Kim, T.; Choi, J.; Lee, S.; Yeo, K.J.; Cheong, H.K.; Kim, K.K.
Structural studies on the extracellular domain of sensor histidine kinase YycG from Staphylococcus aureus and its functional implications
J. Mol. Biol.
428
3074-3089
2016
Staphylococcus aureus, Staphylococcus aureus (Q2G2U4), Staphylococcus aureus NCTC 8325 (Q2G2U4), Staphylococcus aureus RN4220
Wang, L.; Quan, C.; Liu, B.; Wang, J.; Xiong, W.; Zhao, P.; Fan, S.
Functional reconstitution of Staphylococcus aureus truncated AgrC histidine kinase in a model membrane system
PLoS ONE
8
e80400
2013
Staphylococcus aureus
Monk, I.; Shaikh, N.; Begg, S.; Gajdiss, M.; Sharkey, L.; Lee, J.; Pidot, S.; Seemann, T.; Kuiper, M.; Winnen, B.; Hvorup, R.; Collins, B.; Bierbaum, G.; Udagedara, S.; Morey, J.; Pulyani, N.; Howden, B.; Maher, M.; McDevitt, C.; King, G.; Stinear, T.
Zinc-binding to the cytoplasmic PAS domain regulates the essential WalK histidine kinase of Staphylococcus aureus
Nat. Commun.
10
3067
2019
Staphylococcus aureus (Q9RDT3), Staphylococcus aureus
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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