2.7.4.1: ATP-polyphosphate phosphotransferase
This is an abbreviated version!
For detailed information about ATP-polyphosphate phosphotransferase, go to the full flat file.
Word Map on EC 2.7.4.1
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2.7.4.1
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phosphorus
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exopolyphosphatase
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molecular biology
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wastewater
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sludge
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polyhydroxyalkanoates
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accumulibacter
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candidatus
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synthesis
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polyphosphatase
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medicine
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phosphoanhydride
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phosphatis
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biotechnology
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drug development
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analysis
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industry
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environmental protection
- 2.7.4.1
- phosphorus
- exopolyphosphatase
- molecular biology
-
wastewater
- sludge
- polyhydroxyalkanoates
- accumulibacter
-
candidatus
- synthesis
- polyphosphatase
- medicine
-
phosphoanhydride
- phosphatis
- biotechnology
- drug development
- analysis
- industry
- environmental protection
Reaction
Synonyms
AAur2811, AjPPK, ATP:polyphosphate phosphotransferase, AUJ86_09545, CHU0107, CHU_0107, class I PPK2, class II polyphosphate kinase, class III PPK2, Deipr_1912, DR0132, DR_0132, ES2, family-2 polyphosphate kinase, FTT_1564, glycogen-bound polyphosphate kinase, GmSuSy, I601_4057, K649_10090, kinase, polyphosphate (phosphorylating), More, MrH2468, Mrub_2488, MXAN_0056, NCg12620, OsIPK2, PA0141, PA3455 protein, paPpx, plyphosphate kinase 1, poly P kinase 1, poly(P) kinase 1, poly(P) kinase 2, poly-P kinase, poly-P kinase 1, polyP kinase, polyphosphate kinase, polyphosphate kinase 1, polyphosphate kinase 2, polyphosphate kinase 3, polyphosphate kinase-1, polyphosphate kinase-2, polyphosphate-dependent nucleoside diphosphate kinase, polyphosphate: ADP phosphotransferase, polyphosphate:ADP phosphotransferase, polyphosphate:nucleotide phosphotransferase, polyphosphoric acid kinase, PPK, PPK-2, PPK1, PPK2, PPK2-1, PPK2-2, PPK2-3, PPK2a, PPK2B, PPK2c, PPK2d, PPK2e, PPK3, Rv3232c, SMc02148, SMc02148 protein, SPO0224, SPO1256, SPO1727
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2.7.4.1 ATP-polyphosphate phosphotransferaseAdvanced search results
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General Information on EC 2.7.4.1 - ATP-polyphosphate phosphotransferase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
drug target
evolution
malfunction
metabolism
physiological function
additional information
drug target
bacterial species, including many pathogens, encode a homolog of a major polyP synthesis enzyme, polyphosphate kinase (PPK) with 2 different genes coding for PPK1 and PPK2. Genetic deletion of the ppk1 gene leads to reduced polyP levels and the consequent loss of virulence and stress adaptation responses. No PPK1 homolog has been identified in higher-order eukaryotes, and, therefore, PPK1 represents a target for chemotherapy
drug target
polyphosphate kinases are involved in many metabolic processes in bacteria, including pathogenic species. As these enzymes are not present in animals, they are a prime target for the development of antibiotics
drug target
polyphosphate kinases are involved in many metabolic processes in bacteria, including pathogenic species. As these enzymes are not present in animals, they are a prime target for the development of antibiotics
drug target
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the absence of a polyphosphate kinase orthologue in humans makes it a potential drug target
drug target
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the absence of a polyphosphate kinase orthologue in humans makes it a potential drug target
drug target
-
the absence of a polyphosphate kinase orthologue in humans makes it a potential drug target
drug target
-
the absence of a polyphosphate kinase orthologue in humans makes it a potential drug target
drug target
-
the absence of a polyphosphate kinase orthologue in humans makes it a potential drug target
drug target
-
the absence of a polyphosphate kinase orthologue in humans makes it a potential drug target
drug target
-
the absence of a polyphosphate kinase orthologue in humans makes it a potential drug target
drug target
-
the absence of a polyphosphate kinase orthologue in humans makes it a potential drug target
drug target
-
the absence of a polyphosphate kinase orthologue in humans makes it a potential drug target
drug target
-
the absence of a polyphosphate kinase orthologue in humans makes it a potential drug target
-
drug target
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polyphosphate kinases are involved in many metabolic processes in bacteria, including pathogenic species. As these enzymes are not present in animals, they are a prime target for the development of antibiotics
-
drug target
-
polyphosphate kinases are involved in many metabolic processes in bacteria, including pathogenic species. As these enzymes are not present in animals, they are a prime target for the development of antibiotics
-
drug target
-
bacterial species, including many pathogens, encode a homolog of a major polyP synthesis enzyme, polyphosphate kinase (PPK) with 2 different genes coding for PPK1 and PPK2. Genetic deletion of the ppk1 gene leads to reduced polyP levels and the consequent loss of virulence and stress adaptation responses. No PPK1 homolog has been identified in higher-order eukaryotes, and, therefore, PPK1 represents a target for chemotherapy
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evolution
a polyphosphate kinase from the polyphosphate kinase 2 (PPK2) family. The enzyme structure consists of a six-stranded parallelbeta-sheet surrounded by 12 alpha-helices, with a high degree of similarity to other members of the PPK2 family and the thymidylate kinase superfamily
evolution
in general, all PPKs are ancient enzymes, and phylogenetic analysis indicates that the polyphosphate degradation process is older than polyphosphate synthesis. Additionally, PPK2 proteins are older than PPK1 enzymes
evolution
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in general, all PPKs are ancient enzymes, and phylogenetic analysis indicates that the polyphosphate degradation process is older than polyphosphate synthesis. Additionally, PPK2 proteins are older than PPK1 enzymes
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malfunction
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a mutant lacking ppk is more than 10fold less competitive against wild type Pf0-1 in sterile loam soil low in inorganic phosphate, while a ppk and nonpredicted antisense RNA mutant of Pf0-1 does not have increased sensitivity to osmotic, oxidative, and acid stress, it is more sensitive to elevated temperatures in laboratory medium and during growth in sterile soil
malfunction
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mutants lacking PPK1 are defective in motility, quorum sensing, biofilm formation, and virulence
malfunction
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PPK1 knockout mutant cells lacking polyphosphate survive poorly during growth in the stationary phase and are less resistant to heat, oxidants, osmotic challenge, antibiotics and UV
malfunction
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ppk1-knockout mutant is deficient in poly-P accumulation, which is associated with a decreased ability to form viable-but-nonculturable cells under acid stress. The ppk1-deficient mutant shows a significant increase in susceptibility to erythromycin, cefotaxime, ciprofloxacin, rifampin, polymyxin B, tetracycline, cholic acid, taurocholic acid, deoxycholic acid, ethidium bromide, and SDS
malfunction
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the isogenic in-frame ppk1 deletion mutant PD44 shows poor survival rates during osmotic shock and acidic challenge and is defective in bacterial adhesion and translocation across the blood-brain-barrier
malfunction
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the polyphosphate kinase mutant is susceptible to hydrogen peroxide in an oxidative stress condition, unable to perform swimming, swarming motilities, and has lower density biofilm forming capacity than the wild type strain
malfunction
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under phosphate limitation conditions, the double polyphosphate kinase/phosphate-binding protein mutant shows a higher production of the endogenous antibiotic actinorhodin and the heterologous antitumor 8-demethyl-tetracenomycin (up to 10fold with respect to the wild type strain)
malfunction
deletion of gene ppk results in a deficiencyin polyphosphate accumulation rather than cell growth in Luria-Bertani medium. The cell growth is evidently retarded and the ilvBHC expression is significantly reduced when the ppk mutant is transferred from LB to limited-amino acid medium. These phenotypes are significantly restored in the ppk-complemented strain
malfunction
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planktonic cells of a ppk knockout strain (DELTAppk) are more susceptible to antibiotics than the wild-type strain, while biofilm-grown DELTAppk cells show similar susceptibility compared to the wild-type and are more tolerant than the planktonic cells. Phenotypes, overview
malfunction
Q9S646
Pseudomonas aeruginosa strains wild-type MPAO1 and enzyme-deficient PW9825 survival in oxidative stress, overview
malfunction
the isogenic deletion mutant is defective for intracellular growth in macrophages and is attenuated in mice. The DELTAFTT1564 strain shows significantly increased sensitivity to a range of antibiotics in a manner independent of the mode of action of the antibiotic
malfunction
the ppk-deficient mutant is deficient in resistance to oxidative, hyperosmotic and heat stress. The swarming and biofilm formation abilities of Proteus mirabilis are also attenuated after the ppk interruption. Negative phenotypes of the ppk mutant can be restored by ppk gene complementation
malfunction
a mutant lacking the enzyme (PPK) makes no detectable polyP under any condition
malfunction
gene deletion alters specific metabolic pathways, changing the metabolic fingerprint, and suppressing the ability of Escherichia coli to form a biofilm
malfunction
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mutation of ES2/OsIPK2 gene results to increased H2O2 and malondialdehyde content and catalase (CAT), superoxide dismutase (SOD), peroxidase (POD) and ascorbate peroxidase (APX) activity, and to reduced chlorophyll and Net photosynthetic rate, which eventually leads to leaf senescence and reduced rice yield
malfunction
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polyphosphate kinase deletion causes decreased resistance to oxidative, heat and hyperosmotic stress, attenuated swarming and biofilm formation, increased production of prolyl isomerase, phosphotransferase and peptidoglycan synthase repressor proteins
malfunction
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polyphosphate kinase deletion causes decreased virulence and low invasiveness
malfunction
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polyphosphate kinase deletion causes loss of biofilm formation on polyvinyl chloride (PVC) or borosilicate
malfunction
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polyphosphate kinase deletion decreases sporulation, motility and biofilm formation
malfunction
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polyphosphate kinase deletion increases sensitivity to H2O2 and reduces polyphosphate accumulation. Polyphosphate kinase deletion upregulates fermentation, aerobic and anaerobic respiration, enhances catalase and Clp protease activity, down-regulates ATP-dependent RNA helicase, DNA polymerase III and pyruvate kinase I
malfunction
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polyphosphate kinase ppk1 deletion causes loss of virulence and biofilm formation, impaired motility and increased susceptibility to antibiotics. Polyphosphate kinase ppk2 deletion causes increased susceptibility to antibiotics
malfunction
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polyphosphate kinase ppk1 deletion causes low polyphosphate accumulation, loss of virulence, reduced colonization in mice and decreased motility
malfunction
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polyphosphate kinase ppk1 deletion causes poor survival during osmotic shock and acid challenge
malfunction
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polyphosphate kinase ppk1 deletion increases serum sensitivity
malfunction
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polyphosphate kinase ppk2 deletion causes increased sensitivity to antibiotics
malfunction
ppk-2 mutant strain infected guinea pigs have significantly reduced bacterial loads and tissue pathology in comparison to wild type infected guinea pigs at later stages of infection. The ppk-2 mutant strainis more tolerant to isoniazid and impaired for survival in THP-1 macrophages
malfunction
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the isogenic in-frame ppk1 deletion mutant PD44 shows poor survival rates during osmotic shock and acidic challenge and is defective in bacterial adhesion and translocation across the blood-brain-barrier
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malfunction
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polyphosphate kinase deletion increases sensitivity to H2O2 and reduces polyphosphate accumulation. Polyphosphate kinase deletion upregulates fermentation, aerobic and anaerobic respiration, enhances catalase and Clp protease activity, down-regulates ATP-dependent RNA helicase, DNA polymerase III and pyruvate kinase I
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malfunction
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polyphosphate kinase ppk1 deletion causes poor survival during osmotic shock and acid challenge
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malfunction
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the ppk-deficient mutant is deficient in resistance to oxidative, hyperosmotic and heat stress. The swarming and biofilm formation abilities of Proteus mirabilis are also attenuated after the ppk interruption. Negative phenotypes of the ppk mutant can be restored by ppk gene complementation
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malfunction
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under phosphate limitation conditions, the double polyphosphate kinase/phosphate-binding protein mutant shows a higher production of the endogenous antibiotic actinorhodin and the heterologous antitumor 8-demethyl-tetracenomycin (up to 10fold with respect to the wild type strain)
-
malfunction
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a mutant lacking ppk is more than 10fold less competitive against wild type Pf0-1 in sterile loam soil low in inorganic phosphate, while a ppk and nonpredicted antisense RNA mutant of Pf0-1 does not have increased sensitivity to osmotic, oxidative, and acid stress, it is more sensitive to elevated temperatures in laboratory medium and during growth in sterile soil
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malfunction
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ppk-2 mutant strain infected guinea pigs have significantly reduced bacterial loads and tissue pathology in comparison to wild type infected guinea pigs at later stages of infection. The ppk-2 mutant strainis more tolerant to isoniazid and impaired for survival in THP-1 macrophages
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malfunction
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ppk-2 mutant strain infected guinea pigs have significantly reduced bacterial loads and tissue pathology in comparison to wild type infected guinea pigs at later stages of infection. The ppk-2 mutant strainis more tolerant to isoniazid and impaired for survival in THP-1 macrophages
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malfunction
Oryza sativa Japonica Group cv. Wuyugeng 7
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mutation of ES2/OsIPK2 gene results to increased H2O2 and malondialdehyde content and catalase (CAT), superoxide dismutase (SOD), peroxidase (POD) and ascorbate peroxidase (APX) activity, and to reduced chlorophyll and Net photosynthetic rate, which eventually leads to leaf senescence and reduced rice yield
-
malfunction
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planktonic cells of a ppk knockout strain (DELTAppk) are more susceptible to antibiotics than the wild-type strain, while biofilm-grown DELTAppk cells show similar susceptibility compared to the wild-type and are more tolerant than the planktonic cells. Phenotypes, overview
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malfunction
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ppk1-knockout mutant is deficient in poly-P accumulation, which is associated with a decreased ability to form viable-but-nonculturable cells under acid stress. The ppk1-deficient mutant shows a significant increase in susceptibility to erythromycin, cefotaxime, ciprofloxacin, rifampin, polymyxin B, tetracycline, cholic acid, taurocholic acid, deoxycholic acid, ethidium bromide, and SDS
-
malfunction
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a mutant lacking the enzyme (PPK) makes no detectable polyP under any condition
-
malfunction
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gene deletion alters specific metabolic pathways, changing the metabolic fingerprint, and suppressing the ability of Escherichia coli to form a biofilm
-
malfunction
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the polyphosphate kinase mutant is susceptible to hydrogen peroxide in an oxidative stress condition, unable to perform swimming, swarming motilities, and has lower density biofilm forming capacity than the wild type strain
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metabolism
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cell growth, hydrogen productivity and cellular metabolism of Enterobacter aerogenes IAM1183 are affected by the external addition of diphosphate and the overexpression of the enzyme at different initial glucose concentrations
metabolism
identification of a protein PhaX as a putative link between poly(3-hydroxybutyrate) and polyphospate metabolism, the A2274 (phaX) gene product is annotated as a hypothetical putative phosphate transport regulator, regulation, overview. Polyphosphate granules in Ralstonia eutropha are often located in the neighborhood of polyhydroxybutyrate granules if both biopolymers are present simultaneously
metabolism
PPK is a primary enzyme involved in polyphosphate biosynthesis
metabolism
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
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identification of a protein PhaX as a putative link between poly(3-hydroxybutyrate) and polyphospate metabolism, the A2274 (phaX) gene product is annotated as a hypothetical putative phosphate transport regulator, regulation, overview. Polyphosphate granules in Ralstonia eutropha are often located in the neighborhood of polyhydroxybutyrate granules if both biopolymers are present simultaneously
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physiological function
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polyphosphate kinase is necessary for optimal competitive fitness in LB broth culture and sterile loam soil
physiological function
PPK1 regulates error-prone DNA replication by DNA polymerase IV, leading to adaptive mutation
physiological function
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polyphosphate kinase 1 is required for the pathogenesis process of meningitic Escherichia coli K1 (RS218) and plays an important role in stress adaption and virulence
physiological function
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polyphosphate kinase plays a role in virulence, such as in oxidative stress response, motilities and biofilm formation. Polyphosphate kinase is also essential and independently involved in biofilm formation
physiological function
enzyme PPK is an important regulator and plays a crucial role in stress tolerance and virulence in uropathogenic Proteus mirabilis, overview. Gene ppk is required for Proteus mirabilis to invade the bladder
physiological function
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enzyme PPK is important for the antibiotic stress response during the planktonic growth of extraintestinal pathogenic Escherichia coli
physiological function
important role for polyphosphate in the virulence of Francisella
physiological function
polyphosphate is essential for cell growth and responses to nutritional stringen-cies and environmental stresses and branched-chain amino acids are useful intracellular signals for bacterial adaption to nutritional environments. Enzyme PPK plays a rolein polyphosphate accumulation and expression of genes involved in branched-chain amino acids biosynthesis
physiological function
polyphosphate kinase 1 is a central node in the stress response network of Mycobacterium tuberculosis, it connects the two-component systems MprAB and SenX3-RegX3 and the extracytoplasmic function sigma factor, sigma E, overview. Role of SigE in ppk1 transcription, while enzyme PPK1 is itself capable of regulating sigE expression via the MprAB TCS, presence of multiple positive feedback loops in this signalling circuit. Gene ppk1 is induced during phosphate limitation in Mycobacterium tuberculosis
physiological function
Q9S646
polyphosphate kinase 1 plays an important role in virulence, antibiotic resistance and survival under stress conditions
physiological function
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substrate level phosphorylation is essential for the survival of amastigote forms of Leishmania donovani
physiological function
a PPK2 mutant strain shows significantly increased sensitivity to a range of antibiotics in a manner independent of the mode of action of the antibiotic
physiological function
besides adenosine 5'-triphosphate, PPK2s also catalyses the synthesis of highly phosphorylated nucleotides in vitro, such as adenosine 5'-tetraphosphate and adenosine 5'-pentaphosphate
physiological function
besides adenosine 5'-triphosphate, PPK2s also catalyses the synthesis of highly phosphorylated nucleotides in vitro, such as adenosine 5'-tetraphosphate and adenosine 5'-pentaphosphate
physiological function
besides adenosine 5'-triphosphate, PPK2s also catalyses the synthesis of highly phosphorylated nucleotides in vitro, such as adenosine 5'-tetraphosphate and adenosine 5'-pentaphosphate
physiological function
besides adenosine 5'-triphosphate, PPK2s also catalyses the synthesis of highly phosphorylated nucleotides in vitro, such as adenosine 5'-tetraphosphate and adenosine 5'-pentaphosphate
physiological function
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in Escherichia coli polyphosphate levels are controlled via the polyphosphate-synthesizing enzyme polyphosphate kinase (PPK1) and exopolyphosphatases (PPX and GPPA), and are temporarily enhanced by PPK1 overexpression and reduced by PPX overexpression
physiological function
polyphosphate kinase is a negative regulator of virulence gene expression in Francisella tularensis
physiological function
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polyphosphate kinases catalyzes the polyphosphate formation or ATP formation, to store energy or to regenerate ATP, respectively
physiological function
polyphosphate kinases catalyzes the polyphosphate formation or ATP formation, to store energy or to regenerate ATP, respectively
physiological function
PPK-2 enzyme is required for Mycobacterium tuberculosis growth during acute and chronic stage of infection. PPK-2 enzyme contributes to the ability of Mycobacterium tuberculosis to cause disease in guinea pigs
physiological function
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the enzyme has wide distribution among pathogens and is involved in promoting pathogenesis, stress management and susceptibility to antibiotics
physiological function
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the enzyme has wide distribution among pathogens and is involved in promoting pathogenesis, stress management and susceptibility to antibiotics
physiological function
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the enzyme has wide distribution among pathogens and is involved in promoting pathogenesis, stress management and susceptibility to antibiotics
physiological function
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the enzyme has wide distribution among pathogens and is involved in promoting pathogenesis, stress management and susceptibility to antibiotics
physiological function
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the enzyme has wide distribution among pathogens and is involved in promoting pathogenesis, stress management and susceptibility to antibiotics
physiological function
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the enzyme has wide distribution among pathogens and is involved in promoting pathogenesis, stress management and susceptibility to antibiotics
physiological function
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the enzyme has wide distribution among pathogens and is involved in promoting pathogenesis, stress management and susceptibility to antibiotics
physiological function
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the enzyme has wide distribution among pathogens and is involved in promoting pathogenesis, stress management and susceptibility to antibiotics
physiological function
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the enzyme has wide distribution among pathogens and is involved in promoting pathogenesis, stress management and susceptibility to antibiotics
physiological function
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the ES2 gene, encoding an inositol polyphosphate kinase localized in the nucleus and plasma membrane of cells, is essential for leaf senescence in rice
physiological function
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polyphosphate kinase is a negative regulator of virulence gene expression in Francisella tularensis
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physiological function
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polyphosphate kinase 1 is required for the pathogenesis process of meningitic Escherichia coli K1 (RS218) and plays an important role in stress adaption and virulence
-
physiological function
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the enzyme has wide distribution among pathogens and is involved in promoting pathogenesis, stress management and susceptibility to antibiotics
-
physiological function
-
enzyme PPK is an important regulator and plays a crucial role in stress tolerance and virulence in uropathogenic Proteus mirabilis, overview. Gene ppk is required for Proteus mirabilis to invade the bladder
-
physiological function
-
substrate level phosphorylation is essential for the survival of amastigote forms of Leishmania donovani
-
physiological function
-
polyphosphate kinase is necessary for optimal competitive fitness in LB broth culture and sterile loam soil
-
physiological function
-
polyphosphate kinase 1 is a central node in the stress response network of Mycobacterium tuberculosis, it connects the two-component systems MprAB and SenX3-RegX3 and the extracytoplasmic function sigma factor, sigma E, overview. Role of SigE in ppk1 transcription, while enzyme PPK1 is itself capable of regulating sigE expression via the MprAB TCS, presence of multiple positive feedback loops in this signalling circuit. Gene ppk1 is induced during phosphate limitation in Mycobacterium tuberculosis
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physiological function
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PPK-2 enzyme is required for Mycobacterium tuberculosis growth during acute and chronic stage of infection. PPK-2 enzyme contributes to the ability of Mycobacterium tuberculosis to cause disease in guinea pigs
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physiological function
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PPK-2 enzyme is required for Mycobacterium tuberculosis growth during acute and chronic stage of infection. PPK-2 enzyme contributes to the ability of Mycobacterium tuberculosis to cause disease in guinea pigs
-
physiological function
Oryza sativa Japonica Group cv. Wuyugeng 7
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the ES2 gene, encoding an inositol polyphosphate kinase localized in the nucleus and plasma membrane of cells, is essential for leaf senescence in rice
-
physiological function
-
enzyme PPK is important for the antibiotic stress response during the planktonic growth of extraintestinal pathogenic Escherichia coli
-
physiological function
-
besides adenosine 5'-triphosphate, PPK2s also catalyses the synthesis of highly phosphorylated nucleotides in vitro, such as adenosine 5'-tetraphosphate and adenosine 5'-pentaphosphate
-
physiological function
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polyphosphate kinase plays a role in virulence, such as in oxidative stress response, motilities and biofilm formation. Polyphosphate kinase is also essential and independently involved in biofilm formation
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physiological function
Francisella tularensis Schu 4
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besides adenosine 5'-triphosphate, PPK2s also catalyses the synthesis of highly phosphorylated nucleotides in vitro, such as adenosine 5'-tetraphosphate and adenosine 5'-pentaphosphate
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additional information
a lid-loop and the conserved Walker A and B motifs are important for substrate binding and enzyme catalysis
additional information
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homology structural model of full-length paPpx, in closed conformation, and of the N-terminal domain of paPpx in an open state, constructed by comparative modeling, molecular dynamic simulations, overview. Docking study with bound metals and/or ADP defining the N-paPpx(1-314) model in open conformation as receptor, docking with polyphosphate and ADP. Enzyme electrostatic potential calculations. A model of the paPpx N-terminal domain in complex with a polyP chain of 7 residues long and a molecule of ADP explains the phosphotransferase activity through docking techniques, overview
