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malfunction
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naturally occurring mutation T86I confers resistance to bacitracin and scandium in Bacillus subtilis mutants
malfunction
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the uppS1 mutation increases resistance to vancomycin, fosfomycin, and D-cycloserine in wild-type cells, but this effect is greatly reduced or eliminated in a sigmaM mutant background. Incomplete inhibition of UppS function may lead to increased resistance to some cell wall-active antibiotics. Phenotype, overview
malfunction
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naturally occurring mutation T86I confers resistance to bacitracin and scandium in Bacillus subtilis mutants
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malfunction
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the uppS1 mutation increases resistance to vancomycin, fosfomycin, and D-cycloserine in wild-type cells, but this effect is greatly reduced or eliminated in a sigmaM mutant background. Incomplete inhibition of UppS function may lead to increased resistance to some cell wall-active antibiotics. Phenotype, overview
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metabolism
an essential enzyme in the biosynthesis of bacterial cell wall
metabolism
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essential enzyme in bacterial cell wall synthesis
metabolism
essential enzyme in the biosynthesis of the bacterial cell wall
metabolism
the enzyme is responsible for the biogenesis of undecaprenyl phosphate, an indispensable glycosyl carrier lipid in bacterial cell wall biosynthesis
metabolism
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essential enzyme in the biosynthesis of the bacterial cell wall
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metabolism
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an essential enzyme in the biosynthesis of bacterial cell wall
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metabolism
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the enzyme is responsible for the biogenesis of undecaprenyl phosphate, an indispensable glycosyl carrier lipid in bacterial cell wall biosynthesis
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metabolism
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essential enzyme in bacterial cell wall synthesis
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physiological function
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expression of UPPS in the yeast mutant rer2DELTA, lacking undecaprenyl diphosphate synthase, complements the growth and the hypoglycosylation of carboxypeptidase Y defects. Mutant cells expressing UPPS synthesize dolichyl phosphate of chain length C55 and utilize it to form Man-P-(55)Dol in vitro and in vivo, and they synthesize N-linked glycoprotein
physiological function
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undecaprenyl diphosphate is a key lipid involved in the biosynthesis of peptidoglycan and other cell wall polysaccharide components, such as lipopolysaccharides, enterobacterial common antigen, capsule polysaccharides and teichoic acids. In the cell wall synthetic pathway, UPP is needed for the synthesis and transport of hydrophilic GlcNAc-MurNAc-pentapeptides across the hydrophobic environment of the cytoplasmic membrane to the externally located sites of polymerization
physiological function
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UPPS is a cis- and trans-type prenyltransferase catalyzing consecutive condensation reactions of FPP with specific numbers of IPP to generate linear products with designate chain lengths, UPPS utilizes a concerted mechanism for IPP condensation, structures and mechanisms of the cis-prenyltransferase undecaprenyl diphosphate synthase, overview. Structures of different forms of UPPS with or without ligands reveal conformational changes upon substrate binding, catalysis and product release. A disordered loop in Escherichia coli UPPS, invisible in crystal structures without ligand, is essential for catalysis
physiological function
bactoprenyl diphosphate (BPP), a two-E eight-Z configuration C55 isoprenoid, serves as a critical anchor for the biosynthesis of complex glycans central to bacterial survival and pathogenesis. BPP is formed by the polymerase undecaprenyl diphosphate synthase (UppS), which catalyzes the elongation of a single farnesyl diphosphate (FPP) with eight Z-configuration isoprene units from eight isopentenyl diphosphates
physiological function
bactoprenyl diphosphate (BPP), a two-E eight-Z configuration C55 isoprenoid, serves as a critical anchor for the biosynthesis of complex glycans central to bacterial survival and pathogenesis. BPP is formed by the polymerase undecaprenyl diphosphate synthase (UppS), which catalyzes the elongation of a single farnesyl diphosphate (FPP) with eight Z-configuration isoprene units from eight isopentenyl diphosphates
physiological function
bactoprenyl diphosphate (BPP), a two-E eight-Z configuration C55 isoprenoid, serves as a critical anchor for the biosynthesis of complex glycans central to bacterial survival and pathogenesis. BPP is formed by the polymerase undecaprenyl diphosphate synthase (UppS), which catalyzes the elongation of a single farnesyl diphosphate (FPP) with eight Z-configuration isoprene units from eight isopentenyl diphosphates
physiological function
the enzyme is an essential enzyme in a key bacterial cell wall synthesis pathway. It catalyzes the consecutive condensations of isopentenyl diphosphate groups on to a trans-farnesyl diphosphate to produce the C55 isoprenoid undecaprenyl diphosphate
physiological function
undecaprenyl diphosphate synthase catalyzes the synthesis of a polyisoprenoid that is essential for both peptidoglycan and cell wall teichoic acid, WTA, synthesis. UppS might be an auxiliary factor involved in methicillin resistance of methicillin-resistant Staphylococcus aureus
physiological function
undecaprenyl diphosphate synthase catalyzes the synthesis of a polyisoprenoid that is essential for both peptidoglycan and cell wall teichoic acid, WTA, synthesis. UppS might be an auxiliary factor involved in methicillin resistance of methicillin-resistant Staphylococcus aureus
physiological function
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bactoprenyl diphosphate (BPP), a two-E eight-Z configuration C55 isoprenoid, serves as a critical anchor for the biosynthesis of complex glycans central to bacterial survival and pathogenesis. BPP is formed by the polymerase undecaprenyl diphosphate synthase (UppS), which catalyzes the elongation of a single farnesyl diphosphate (FPP) with eight Z-configuration isoprene units from eight isopentenyl diphosphates
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physiological function
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bactoprenyl diphosphate (BPP), a two-E eight-Z configuration C55 isoprenoid, serves as a critical anchor for the biosynthesis of complex glycans central to bacterial survival and pathogenesis. BPP is formed by the polymerase undecaprenyl diphosphate synthase (UppS), which catalyzes the elongation of a single farnesyl diphosphate (FPP) with eight Z-configuration isoprene units from eight isopentenyl diphosphates
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physiological function
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undecaprenyl diphosphate synthase catalyzes the synthesis of a polyisoprenoid that is essential for both peptidoglycan and cell wall teichoic acid, WTA, synthesis. UppS might be an auxiliary factor involved in methicillin resistance of methicillin-resistant Staphylococcus aureus
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physiological function
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undecaprenyl diphosphate is a key lipid involved in the biosynthesis of peptidoglycan and other cell wall polysaccharide components, such as lipopolysaccharides, enterobacterial common antigen, capsule polysaccharides and teichoic acids. In the cell wall synthetic pathway, UPP is needed for the synthesis and transport of hydrophilic GlcNAc-MurNAc-pentapeptides across the hydrophobic environment of the cytoplasmic membrane to the externally located sites of polymerization
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physiological function
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bactoprenyl diphosphate (BPP), a two-E eight-Z configuration C55 isoprenoid, serves as a critical anchor for the biosynthesis of complex glycans central to bacterial survival and pathogenesis. BPP is formed by the polymerase undecaprenyl diphosphate synthase (UppS), which catalyzes the elongation of a single farnesyl diphosphate (FPP) with eight Z-configuration isoprene units from eight isopentenyl diphosphates
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physiological function
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undecaprenyl diphosphate synthase catalyzes the synthesis of a polyisoprenoid that is essential for both peptidoglycan and cell wall teichoic acid, WTA, synthesis. UppS might be an auxiliary factor involved in methicillin resistance of methicillin-resistant Staphylococcus aureus
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additional information
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overexpression of the wild-type uppS gene results in increased susceptibilities to both scandium and bacitracin, which prevents cell wall synthesis by inhibiting the dephosphorylation of undecaprenyl diphosphate, in addition to enhanced amylase production. Accumulation of undecaprenyl diphosphate renders cells more susceptible to rare earth elements
additional information
molecular docking and homology modeling of UPP synthase
additional information
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molecular docking and homology modeling of UPP synthase
additional information
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molecular docking and homology modeling of UPP synthase
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additional information
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overexpression of the wild-type uppS gene results in increased susceptibilities to both scandium and bacitracin, which prevents cell wall synthesis by inhibiting the dephosphorylation of undecaprenyl diphosphate, in addition to enhanced amylase production. Accumulation of undecaprenyl diphosphate renders cells more susceptible to rare earth elements
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