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Information on EC 2.7.13.3 - histidine kinase and Organism(s) Pseudomonas aeruginosa and UniProt Accession Q9HWR3
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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: Pseudomonas aeruginosa
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 + PhoN protein L-histidine
ADP + PhoN protein N-phospho-L-histidine
-
-
-
-
?
ATP + protein L-histidine
ADP + protein N-phospho-L-histidine
-
-
-
?
additional information
?
-
signal transduction mechanism in the bacteriophytochrome, overview
-
-
?
additional information
?
-
-
signal transduction mechanism in the bacteriophytochrome, overview
-
-
?
additional information
?
-
structure-function relationship: the bacteriophytochrome possesses a histidine kinase domain and undergoes conformational changes during photoconversion, local structural changes originating in the photosensory domain modulate interactions between long, crossdomain signaling helices at the dimer interface and are transmitted to the spatially distant effector domain, thereby regulating its histidine kinase activity, overview
-
-
?
additional information
?
-
-
structure-function relationship: the bacteriophytochrome possesses a histidine kinase domain and undergoes conformational changes during photoconversion, local structural changes originating in the photosensory domain modulate interactions between long, crossdomain signaling helices at the dimer interface and are transmitted to the spatially distant effector domain, thereby regulating its histidine kinase activity, overview
-
-
?
additional information
?
-
PilS/PilR is a two-component transcriptional regulatory system controlling expression of type 4 fimbriae in Pseudomonas aeruginosa. PilS is a sensor protein which when stimulated by the appropriate environmental signals activates PilR through kinase activity. PilR then activates transcription of pilA, probably by interacting with RNA polymerase containing RpoN
-
-
?
additional information
?
-
-
PilS/PilR is a two-component transcriptional regulatory system controlling expression of type 4 fimbriae in Pseudomonas aeruginosa. PilS is a sensor protein which when stimulated by the appropriate environmental signals activates PilR through kinase activity. PilR then activates transcription of pilA, probably by interacting with RNA polymerase containing RpoN
-
-
?
additional information
?
-
the two-component regulatory system PfeR/PfeS is involved in the expression of the ferric enterobactin receptor PfeA
-
-
?
additional information
?
-
-
deletion of PilS results in a non-pilated phenotype
-
-
?
additional information
?
-
A two-component system comprises a histidine kinase protein or sensor mostly inserted into the inner membrane and a cognate partner known as the response regulator. The stimulus by the periplasmic or cytoplasmic detection domain of the histidine kinase protein triggers autophosphorylation on a conserved histidine residue of the transmitter domain H1. The phosphoryl group is then transferred on a conserved aspartate residue present in the receiver or D domain of the cognate response regulator. In Pseudomonas aeruginosa, the histidine kinase requires additional domains such as a receiver domain (D1) fused to the histidine kinase. Two-component system mechanism, overview
-
-
?
additional information
?
-
A two-component system comprises a histidine kinase protein or sensor mostly inserted into the inner membrane and a cognate partner known as the response regulator. The stimulus by the periplasmic or cytoplasmic detection domain of the histidine kinase protein triggers autophosphorylation on a conserved histidine residue of the transmitter domain H1. The phosphoryl group is then transferred on a conserved aspartate residue present in the receiver or D domain of the cognate response regulator. In Pseudomonas aeruginosa, the histidine kinase requires additional domains such as a receiver domain (D1) fused to the histidine kinase. Two-component system mechanism, overview
-
-
?
additional information
?
-
-
A two-component system comprises a histidine kinase protein or sensor mostly inserted into the inner membrane and a cognate partner known as the response regulator. The stimulus by the periplasmic or cytoplasmic detection domain of the histidine kinase protein triggers autophosphorylation on a conserved histidine residue of the transmitter domain H1. The phosphoryl group is then transferred on a conserved aspartate residue present in the receiver or D domain of the cognate response regulator. In Pseudomonas aeruginosa, the histidine kinase requires additional domains such as a receiver domain (D1) fused to the histidine kinase. Two-component system mechanism, overview
-
-
?
additional information
?
-
a two-component system comprises a histidine kinase protein or sensor mostly inserted into the inner membrane and a cognate partner known as the response regulator. The stimulus by the periplasmic or cytoplasmic detection domain of the histidine kinase protein triggers autophosphorylation on a conserved histidine residue of the transmitter domain H1. The phosphoryl group is then transferred on a conserved aspartate residue present in the receiver or D domain of the cognate response regulator. In Pseudomonas aeruginosa, the histidine kinase requires additional domains such as a receiver domain (D1) fused to the histidine kinase. Two-component system mechanism, overview. GacS is an unorthodox histidine kinase with H1/D1/H2 domains. GacA is an response regulator functioning as a transcriptional regulator, which positively and exclusively controls the expression of two unique target genes encoding two small noncoding RNAs, RsmY and RsmZ
-
-
?
additional information
?
-
a two-component system comprises a histidine kinase protein or sensor mostly inserted into the inner membrane and a cognate partner known as the response regulator. The stimulus by the periplasmic or cytoplasmic detection domain of the histidine kinase protein triggers autophosphorylation on a conserved histidine residue of the transmitter domain H1. The phosphoryl group is then transferred on a conserved aspartate residue present in the receiver or D domain of the cognate response regulator. In Pseudomonas aeruginosa, the histidine kinase requires additional domains such as a receiver domain (D1) fused to the histidine kinase. Two-component system mechanism, overview. GacS is an unorthodox histidine kinase with H1/D1/H2 domains. GacA is an response regulator functioning as a transcriptional regulator, which positively and exclusively controls the expression of two unique target genes encoding two small noncoding RNAs, RsmY and RsmZ
-
-
?
additional information
?
-
-
a two-component system comprises a histidine kinase protein or sensor mostly inserted into the inner membrane and a cognate partner known as the response regulator. The stimulus by the periplasmic or cytoplasmic detection domain of the histidine kinase protein triggers autophosphorylation on a conserved histidine residue of the transmitter domain H1. The phosphoryl group is then transferred on a conserved aspartate residue present in the receiver or D domain of the cognate response regulator. In Pseudomonas aeruginosa, the histidine kinase requires additional domains such as a receiver domain (D1) fused to the histidine kinase. Two-component system mechanism, overview. GacS is an unorthodox histidine kinase with H1/D1/H2 domains. GacA is an response regulator functioning as a transcriptional regulator, which positively and exclusively controls the expression of two unique target genes encoding two small noncoding RNAs, RsmY and RsmZ
-
-
?
additional information
?
-
in vitro transphosphorylation of GacS H2 domain by LadS histidine kinase. The enzyme performs autophosphorylation using ATP
-
-
?
additional information
?
-
in vitro transphosphorylation of GacS H2 domain by LadS histidine kinase. The enzyme performs autophosphorylation using ATP
-
-
?
additional information
?
-
-
in vitro transphosphorylation of GacS H2 domain by LadS histidine kinase. The enzyme performs autophosphorylation using ATP
-
-
?
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
-
-
-
?
additional information
?
-
signal transduction mechanism in the bacteriophytochrome, overview
-
-
?
additional information
?
-
-
signal transduction mechanism in the bacteriophytochrome, overview
-
-
?
additional information
?
-
PilS/PilR is a two-component transcriptional regulatory system controlling expression of type 4 fimbriae in Pseudomonas aeruginosa. PilS is a sensor protein which when stimulated by the appropriate environmental signals activates PilR through kinase activity. PilR then activates transcription of pilA, probably by interacting with RNA polymerase containing RpoN
-
-
?
additional information
?
-
-
PilS/PilR is a two-component transcriptional regulatory system controlling expression of type 4 fimbriae in Pseudomonas aeruginosa. PilS is a sensor protein which when stimulated by the appropriate environmental signals activates PilR through kinase activity. PilR then activates transcription of pilA, probably by interacting with RNA polymerase containing RpoN
-
-
?
additional information
?
-
the two-component regulatory system PfeR/PfeS is involved in the expression of the ferric enterobactin receptor PfeA
-
-
?
additional information
?
-
-
deletion of PilS results in a non-pilated phenotype
-
-
?
additional information
?
-
A two-component system comprises a histidine kinase protein or sensor mostly inserted into the inner membrane and a cognate partner known as the response regulator. The stimulus by the periplasmic or cytoplasmic detection domain of the histidine kinase protein triggers autophosphorylation on a conserved histidine residue of the transmitter domain H1. The phosphoryl group is then transferred on a conserved aspartate residue present in the receiver or D domain of the cognate response regulator. In Pseudomonas aeruginosa, the histidine kinase requires additional domains such as a receiver domain (D1) fused to the histidine kinase. Two-component system mechanism, overview
-
-
?
additional information
?
-
A two-component system comprises a histidine kinase protein or sensor mostly inserted into the inner membrane and a cognate partner known as the response regulator. The stimulus by the periplasmic or cytoplasmic detection domain of the histidine kinase protein triggers autophosphorylation on a conserved histidine residue of the transmitter domain H1. The phosphoryl group is then transferred on a conserved aspartate residue present in the receiver or D domain of the cognate response regulator. In Pseudomonas aeruginosa, the histidine kinase requires additional domains such as a receiver domain (D1) fused to the histidine kinase. Two-component system mechanism, overview
-
-
?
additional information
?
-
-
A two-component system comprises a histidine kinase protein or sensor mostly inserted into the inner membrane and a cognate partner known as the response regulator. The stimulus by the periplasmic or cytoplasmic detection domain of the histidine kinase protein triggers autophosphorylation on a conserved histidine residue of the transmitter domain H1. The phosphoryl group is then transferred on a conserved aspartate residue present in the receiver or D domain of the cognate response regulator. In Pseudomonas aeruginosa, the histidine kinase requires additional domains such as a receiver domain (D1) fused to the histidine kinase. Two-component system mechanism, overview
-
-
?
additional information
?
-
a two-component system comprises a histidine kinase protein or sensor mostly inserted into the inner membrane and a cognate partner known as the response regulator. The stimulus by the periplasmic or cytoplasmic detection domain of the histidine kinase protein triggers autophosphorylation on a conserved histidine residue of the transmitter domain H1. The phosphoryl group is then transferred on a conserved aspartate residue present in the receiver or D domain of the cognate response regulator. In Pseudomonas aeruginosa, the histidine kinase requires additional domains such as a receiver domain (D1) fused to the histidine kinase. Two-component system mechanism, overview. GacS is an unorthodox histidine kinase with H1/D1/H2 domains. GacA is an response regulator functioning as a transcriptional regulator, which positively and exclusively controls the expression of two unique target genes encoding two small noncoding RNAs, RsmY and RsmZ
-
-
?
additional information
?
-
a two-component system comprises a histidine kinase protein or sensor mostly inserted into the inner membrane and a cognate partner known as the response regulator. The stimulus by the periplasmic or cytoplasmic detection domain of the histidine kinase protein triggers autophosphorylation on a conserved histidine residue of the transmitter domain H1. The phosphoryl group is then transferred on a conserved aspartate residue present in the receiver or D domain of the cognate response regulator. In Pseudomonas aeruginosa, the histidine kinase requires additional domains such as a receiver domain (D1) fused to the histidine kinase. Two-component system mechanism, overview. GacS is an unorthodox histidine kinase with H1/D1/H2 domains. GacA is an response regulator functioning as a transcriptional regulator, which positively and exclusively controls the expression of two unique target genes encoding two small noncoding RNAs, RsmY and RsmZ
-
-
?
additional information
?
-
-
a two-component system comprises a histidine kinase protein or sensor mostly inserted into the inner membrane and a cognate partner known as the response regulator. The stimulus by the periplasmic or cytoplasmic detection domain of the histidine kinase protein triggers autophosphorylation on a conserved histidine residue of the transmitter domain H1. The phosphoryl group is then transferred on a conserved aspartate residue present in the receiver or D domain of the cognate response regulator. In Pseudomonas aeruginosa, the histidine kinase requires additional domains such as a receiver domain (D1) fused to the histidine kinase. Two-component system mechanism, overview. GacS is an unorthodox histidine kinase with H1/D1/H2 domains. GacA is an response regulator functioning as a transcriptional regulator, which positively and exclusively controls the expression of two unique target genes encoding two small noncoding RNAs, RsmY and RsmZ
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
the sensor domain of CzcS senses the Zn(II) stimulus at micromole level in a tetrahedral geometry through its symmetry-related residues His55 and Asp60 on the dimer interface
additional information
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
-
-
Mg2+
-
PhoQ is strongly repressed in divalent cation-replete medium at 10 mM Mg2+
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
-
bound, PilS is retained to the poles of Pseudomonas aeruginosa
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
while the GacS/GacA two-component system is widely distributed throughout the bacterial kingdom, the molecular switch formed by the hybrid LadS, PA1611 and RetS histifine kinases is unique to the Pseudomonas species, though it can function in very different ways in phylogenetically related Pseudomonas species
malfunction
gacS or gacA mutations are epistasic to ladS mutation
physiological function
physiological function
in response to environmental changes, Pseudomonas aeruginosa is able to switch from a planktonic (free swimming) to a sessile (biofilm) lifestyle. The two-component system GacS/GacA activates the production of two small non-coding RNAs, RsmY and RsmZ, but four histidine kinases, RetS, GacS, LadS and PA1611, are instrumental in this process. RetS hybrid histidine kinase blocks GacS unorthodox histidine kinase autophosphorylation through the formation of a heterodimer. PA1611 hybrid histidine kinase, which is structurally related to GacS, interacts with RetS in Pseudomonas aeruginosa in a very similar manner to GacS. LadS hybrid histidine kinase phenotypically antagonizes the function of RetS by a mechanism that has never been investigated. The four sensors are found in most Pseudomonas species but their characteristics and mode of signaling may differ from one species to another. In Pseudomonas aeruginosa, LadS controls both rsmY and rsmZ gene expression and this regulation occurs through the GacS/GacA two-component system. In contrast to RetS, LadS signals through GacS/GacA without forming heterodimers, either with GacS or with RetS. Enzyme LadS is involved in a genuine phospho relay, which requires both transmitter and receiver LadS domains. LadS signaling ultimately requires the alternative histidine-phosphotransfer domain of GacS. LadS histidine kinase forms, with the GacS/GacA two-component system, a multicomponent signal transduction system with an original phosphorelay cascade, i.e. H1LadS -> D1LadS -> H2GacS -> D2GacA. This highlights an original strategy in which a unique output, i.e. the modulation of sRNA levels, is controlled by a complex multi-sensing network to fine-tune an adapted biofilm and virulence response. H1 and D1 domain involvement of the LadS hybrid histidine kinase in the LadS signaling pathway, and involvement of the H2 domain of the GacS unorthodox histidine kinase in the LadS signaling pathway, overview
physiological function
in response to environmental changes, Pseudomonas aeruginosa is able to switch from a planktonic (free swimming) to a sessile (biofilm) lifestyle. The two-component system GacS/GacA activates the production of two small non-coding RNAs, RsmY and RsmZ, but four histidine kinases, RetS, GacS, LadS and PA1611, are instrumental in this process. RetS hybrid histidine kinase blocks GacS unorthodox histidine kinase autophosphorylation through the formation of a heterodimer. PA1611 hybrid histidine kinase, which is structurally related to GacS, interacts with RetS in Pseudomonas aeruginosa in a very similar manner to GacS. LadS hybrid histidine kinase phenotypically antagonizes the function of RetS. The four sensors are found in most Pseudomonas species but their characteristics and mode of signaling may differ from one species to another. In Pseudomonas aeruginosa, LadS controls both rsmY and rsmZ gene expression and this regulation occurs through the GacS/GacA two-component system. In contrast to RetS, LadS signals through GacS/GacA without forming heterodimers, either with GacS or with RetS. Enzyme LadS is involved in a genuine phospho relay, which requires both transmitter and receiver LadS domains. LadS signaling ultimately requires the alternative histidine-phosphotransfer domain of GacS. LadS histidine kinase forms, with the GacS/GacA two-component system, a multicomponent signal transduction system with an original phosphorelay cascade, i.e. H1LadS -> D1LadS -> H2GacS -> D2GacA. This highlights an original strategy in which a unique output, i.e. the modulation of sRNA levels, is controlled by a complex multi-sensing network to fine-tune an adapted biofilm and virulence response. In vitro transphosphorylation of GacS H2 domain by LadS histidine kinase, involvement of the H2 domain of the GacS unorthodox histidine kinase in the LadS signaling pathway
physiological function
a GacS mutant devoid of the periplasmic detector domain is severely defective in biofilm formation accompanied by concomitant changes in the expression of small RNAs RsmY/Z that control activation of GacA-regulated genes. Point mutations in a putative ligand binding pocket lined by positively-charged residues originating primarily from the major loop impair biofilm formation
physiological function
free-standing PilZ protein PA2799 interacts directly with the histidine kinase SagS. PA2799 binds directly to the phosphoreceiver domain of SagS, and the SagS-HapZ interaction is further enhanced at elevated c-di-GMP concentration. Binding of HapZ to SagS inhibits the phosphotransfer between SagS and the downstream protein HptB in a c-di-GMP-dependent manner. HapZ impacts surface attachment and biofilm formation most likely by regulating the expression of a large number of genes
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimeric PaBphP-PCD structure with PAS, GAF, and PHY domains, interdomain and histidine kinase domain, domain structure, overview
additional information
additional information
modeling of the full-length bacteriophytochrome structure, including its output histidine kinase domain, structure-function relationship, overview
additional information
-
modeling of the full-length bacteriophytochrome structure, including its output histidine kinase domain, structure-function relationship, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
additional information
phosphoprotein
in the presence of [gamma-32P]ATP, the purified COOH-terminal KinB protein undergoes progressive autophosphorylation in vitro. Substitutions of the residues conserved among histidine protein kinases abolishes KinB autophosphorylation
additional information
in vitro transphosphorylation of GacS H2 domain by LadS histidine kinase
additional information
in vitro transphosphorylation of GacS H2 domain by LadS histidine kinase
additional information
-
in vitro transphosphorylation of GacS H2 domain by LadS histidine kinase
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type and mutant bacteriophytochrome with an intact, fully photoactive photosensory core domain in its darkadapted Pfr state, X-ray diffraction structure determination and analysis at 2.9 A resolution, molecular replacement
crystal structure of the CzcS sensor domain in complex with Zn(II) at 1.7 A resolution. The sensor domain is an alpha/beta-fold and senses the Zn(II) stimulus at micromole level in a tetrahedral geometry through its symmetry-related residues His55 and Asp60 on the dimer interface. The sensor domain interacts with the effector with the N-terminal alpha-helices rather than the conserved beta-sheets pocket. The dimerization of the N-terminal H1 and H1' alpha-helices is of primary importance for the activity of histidine kinase activity
NMR solution structure, the GacS periplasmic domain displays a distinct PDC/PAS alpha/beta fold characterized by a three-stranded beta-sheet flanked by alpha-helices and an atypical major loop
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Q188L
site-directed mutagenesis, crystal structure determination and analysis
A143G
-
the mutant still has some divalent cation-mediated repression and therefore likely has some ability to bind cations
D110A
-
the mutant exhibits strong de-repression in medium containing 10 mM Mg2+, and activity is approximately the same regardless of the cation content in the growth medium
D131A
D60C
contrary to wild-type, mutant strain displays Co(II)-inducible resistance to antibiotic meropenem
E115A
-
the mutant still has some divalent cation-mediated repression and therefore likely has some ability to bind cations
E133A
-
the mutant exhibits strong de-repression in medium containing 10 mM Mg2+, and activity is approximately the same regardless of the cation content in the growth medium
E77A
-
the mutant still has some divalent cation-mediated repression and therefore likely has some ability to bind cations
G139A
-
the mutant still has some divalent cation-mediated repression and therefore likely has some ability to bind cations
H124A
no change in overall periplasmic domain fold, mutant shows an altered biofilm morphology compared to the wild-type strain
H133A
no change in overall periplasmic domain fold, mutant abolishes biofilm formation
H55A
mutant loses its intrinsic resistance to Zn(II) and meropenem due to the destruction of Zn(II) binding site
L137A
-
the mutant exhibits strong de-repression in medium containing 10 mM Mg2+, and activity is approximately the same regardless of the cation content in the growth medium
L158A
-
the mutant exhibits strong de-repression in medium containing 10 mM Mg2+, and activity is approximately the same regardless of the cation content in the growth medium
L38C/H55A
mutation L38C restores the lost responsiveness of mutation H55A to Zn(II) stimulus
R94A
mutant strain shows biofilm morphology similar to wild-type
S145A
-
the mutant exhibits strong de-repression in medium containing 10 mM Mg2+, and activity is approximately the same regardless of the cation content in the growth medium
additional information
D131A
-
the mutant exhibits strong de-repression in medium containing 10 mM Mg2+, and activity is approximately the same regardless of the cation content in the growth medium
D131A
-
the purified mutant enzyme shows no fluorescence change well into the mM range of Mg2+, suggesting that this mutation renders the protein incapable of binding Mg2+
additional information
construction of diverse point, truncation, and deletion mutants of enzyme GacS, and generation of diverse two-hybrid constructs of enzyme GacS domains
additional information
construction of diverse point, truncation, and deletion mutants of enzyme GacS, and generation of diverse two-hybrid constructs of enzyme GacS domains
additional information
-
construction of diverse point, truncation, and deletion mutants of enzyme GacS, and generation of diverse two-hybrid constructs of enzyme GacS domains
additional information
construction of diverse point, truncation, and deletion mutants of enzyme LadS, and generation of diverse two-hybrid constructs of enzyme LadS domains
additional information
construction of diverse point, truncation, and deletion mutants of enzyme LadS, and generation of diverse two-hybrid constructs of enzyme LadS domains
additional information
-
construction of diverse point, truncation, and deletion mutants of enzyme LadS, and generation of diverse two-hybrid constructs of enzyme LadS domains
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His-tagged forms of enzyme domains GacSD1, GacSH1D1, GacSH2, and GacSH2H->Q from Escherichia coli strain BTH101 by nickel affinity chromatography
recombinant C-terminally His-tagged forms of enzyme domains LadSH1D1, LadSH1D1D->A, and LadSD1 from Escherichia coli strain BTH101 by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of C-terminally His-tagged forms of enzyme domains GacSD1, GacSH1D1, GacSH2, and GacSH2H->Q in Escherichia coli strain BTH101, expression of N-terminally FLAG or Strep tagged enzyme fragment constructs
recombinant expression of C-terminally His-tagged forms of enzyme domains LadSH1D1, LadSH1D1D->A, and LadSD1 in Escherichia coli strain BTH101, expression of N-terminally FLAG or Strep tagged enzyme fragment constructs
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ma, S.; Wozniak, D.J.; Ohman, D.E.
Identification of the histidine protein kinase KinB in Pseudomonas aeruginosa and its phosphorylation of the alginate regulator algB
J. Biol. Chem.
272
17952-17960
1997
Pseudomonas aeruginosa (O34206), Pseudomonas aeruginosa
Anba, J.; Bidaud, M.; Vasil, M.L.; Lazdunski, A.
Nucleotide sequence of the Pseudomonas aeruginosa phoB gene, the regulatory gene for the phosphate regulon
J. Bacteriol.
172
4685-4689
1990
Pseudomonas aeruginosa (P23621)
Stover, C.K.; Pham, X.Q.; Erwin, A.L.; et al.
Complete genome sequence of Pseudomonas aeruginosa PA01, an opportunistic pathogen
Nature
406
959-964
2000
Pseudomonas aeruginosa (P23621), Pseudomonas aeruginosa (Q04804)
Hobbs, M.; Collie, E.S.; Free, P.D.; Livingston, S.P.; Mattick, J.S.
PilS and PilR, a two-component transcriptional regulatory system controlling expression of type 4 fimbriae in Pseudomonas aeruginosa
Mol. Microbiol.
7
669-682
1993
Pseudomonas aeruginosa (P33639), Pseudomonas aeruginosa
Dean, C.R.; Poole, K.
Expression of the ferric enterobactin receptor (PfeA) of Pseudomonas aeruginosa: involvement of a two-component regulatory system
Mol. Microbiol.
8
1095-1103
1993
Pseudomonas aeruginosa (Q04804)
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)
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
Yang, X.; Kuk, J.; Moffat, K.
Crystal structure of Pseudomonas aeruginosa bacteriophytochrome: photoconversion and signal transduction
Proc. Natl. Acad. Sci. USA
105
14715-14720
2008
Pseudomonas aeruginosa (Q9HWR3), Pseudomonas aeruginosa
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
Prost, L.R.; Daley, M.E.; Bader, M.W.; Klevit, R.E.; Miller, S.I.
The PhoQ histidine kinases of Salmonella and Pseudomonas spp. are structurally and functionally different: evidence that pH and antimicrobial peptide sensing contribute to mammalian pathogenesis
Mol. Microbiol.
69
503-519
2008
Pseudomonas aeruginosa, Salmonella enterica subsp. enterica serovar Typhimurium
Chambonnier, G.; Roux, L.; Redelberger, D.; Fadel, F.; Filloux, A.; Sivaneson, M.; de Bentzmann, S.; Bordi, C.
The hybrid histidine kinase LadS forms a multicomponent signal transduction system with the GacS/GacA two-component system in Pseudomonas aeruginosa
PLoS Genet.
12
e1006032
2016
Pseudomonas aeruginosa (G3XD98), Pseudomonas aeruginosa (Q9HX42), Pseudomonas aeruginosa
Xu, L.; Venkataramani, P.; Ding, Y.; Liu, Y.; Deng, Y.; Yong, G.L.; Xin, L.; Ye, R.; Zhang, L.; Yang, L.; Liang, Z.X.
A cyclic di-GMP-binding adaptor protein interacts with histidine kinase to regulate two-component signaling
J. Biol. Chem.
291
16112-16123
2016
Pseudomonas aeruginosa (Q9I019), Pseudomonas aeruginosa
Wang, D.; Chen, W.; Huang, S.; He, Y.; Liu, X.; Hu, Q.; Wei, T.; Sang, H.; Gan, J.; Chen, H.
Structural basis of Zn(II) induced metal detoxification and antibiotic resistance by histidine kinase CzcS in Pseudomonas aeruginosa
PLoS Pathog.
13
e1006533
2017
Pseudomonas aeruginosa (Q9I0V9), Pseudomonas aeruginosa, Pseudomonas aeruginosa DSM 22644 (Q9I0V9)
Ali-Ahmad, A.; Fadel, F.; Sebban-Kreuzer, C.; Ba, M.; Pelissier, G.D.; Bornet, O.; Guerlesquin, F.; Bourne, Y.; Bordi, C.; Vincent, F.
Structural and functional insights into the periplasmic detector domain of the GacS histidine kinase controlling biofilm formation in Pseudomonas aeruginosa
Sci. Rep.
7
11262
2017
Pseudomonas aeruginosa (G3XD98), Pseudomonas aeruginosa, Pseudomonas aeruginosa DSM 22644 (G3XD98)
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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