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IUBMB Comments Involved in the biosynthesis of poly(ribitol-phosphate) teichoic acids in the cell wall of the bacterium Staphylococcus aureus . This enzyme adds an N -acetyl-β-D -glucosamine to the OH group at the 2 position of the ribitol phosphate units. cf . EC 2.4.1.70 [poly(ribitol-phosphate) α-N -acetylglucosaminyltransferase].
Synonyms SAV0258 , TarS,
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SAV0258
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TarS
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n UDP-N-acetyl-alpha-D-glucosamine + 4-O-(D-ribitylphospho)n-di[(2R)-1-glycerophospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = n UDP + 4-O-(2-N-acetyl-beta-D-glucosaminyl-D-ribitylphospho)n-di[(2R)-1-glycerophospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
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MetaCyc
poly(ribitol phosphate) wall teichoic acid biosynthesis II (S. aureus)
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UDP-N-acetyl-alpha-D-glucosamine:4-O-(D-ribitylphospho)n-di[(2R)-1-glycerophospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol beta-N-acetyl-D-glucosaminyltransferase (configuration-inverting)
Involved in the biosynthesis of poly(ribitol-phosphate) teichoic acids in the cell wall of the bacterium Staphylococcus aureus. This enzyme adds an N-acetyl-beta-D-glucosamine to the OH group at the 2 position of the ribitol phosphate units. cf. EC 2.4.1.70 [poly(ribitol-phosphate) alpha-N-acetylglucosaminyltransferase].
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UDP-N-acetyl-D-glucosamine + D-alanyl-N-acetyl-alpha-D-glucosaminylpolyribitol phosphate
N-acetyl-beta-D-glucosaminyl-D-alanyl-N-acetyl-alpha-D-glucosaminylpolyribitol phosphate + UDP
UDP-N-acetyl-D-glucosamine + polyribitol phosphate
UDP + N-acetyl-beta-D-glucosaminyl-polyribitol phosphate
additional information
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UDP-N-acetyl-D-glucosamine + D-alanyl-N-acetyl-alpha-D-glucosaminylpolyribitol phosphate
N-acetyl-beta-D-glucosaminyl-D-alanyl-N-acetyl-alpha-D-glucosaminylpolyribitol phosphate + UDP
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Substrates: 50% of the activity with polyribitol phosphate
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UDP-N-acetyl-D-glucosamine + D-alanyl-N-acetyl-alpha-D-glucosaminylpolyribitol phosphate
N-acetyl-beta-D-glucosaminyl-D-alanyl-N-acetyl-alpha-D-glucosaminylpolyribitol phosphate + UDP
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Substrates: 50% of the activity with polyribitol phosphate
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UDP-N-acetyl-D-glucosamine + polyribitol phosphate
UDP + N-acetyl-beta-D-glucosaminyl-polyribitol phosphate
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Substrates: -
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UDP-N-acetyl-D-glucosamine + polyribitol phosphate
UDP + N-acetyl-beta-D-glucosaminyl-polyribitol phosphate
Substrates: -
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UDP-N-acetyl-D-glucosamine + polyribitol phosphate
UDP + N-acetyl-beta-D-glucosaminyl-polyribitol phosphate
Substrates: -
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UDP-N-acetyl-D-glucosamine + polyribitol phosphate
UDP + N-acetyl-beta-D-glucosaminyl-polyribitol phosphate
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Substrates: -
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additional information
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Substrates: enzyme catalyzes addition of N-acetylglucosamine in both alpha- and beta-position
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additional information
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Substrates: enzyme catalyzes addition of N-acetylglucosamine in both alpha- and beta-position. No substrate: teichoic acid, D-ribitiol 5-phosphate, CDP-ribitol
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additional information
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Substrates: enzyme catalyzes addition of N-acetylglucosamine in both alpha- and beta-position
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additional information
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Substrates: enzyme catalyzes addition of N-acetylglucosamine in both alpha- and beta-position. No substrate: teichoic acid, D-ribitiol 5-phosphate, CDP-ribitol
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UDP-N-acetyl-D-glucosamine + polyribitol phosphate
UDP + N-acetyl-beta-D-glucosaminyl-polyribitol phosphate
additional information
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UDP-N-acetyl-D-glucosamine + polyribitol phosphate
UDP + N-acetyl-beta-D-glucosaminyl-polyribitol phosphate
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Substrates: -
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UDP-N-acetyl-D-glucosamine + polyribitol phosphate
UDP + N-acetyl-beta-D-glucosaminyl-polyribitol phosphate
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Substrates: -
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additional information
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Substrates: enzyme catalyzes addition of N-acetylglucosamine in both alpha- and beta-position
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additional information
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Substrates: enzyme catalyzes addition of N-acetylglucosamine in both alpha- and beta-position
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Mn2+
may substitute for Mg2+
additional information
Ca2+ may not substitute for Mg2+
Mg2+
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required
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1.24 - 2.84
polyribitol phosphate
0.021 - 0.045
UDP-N-acetyl-D-glucosamine
1.24
polyribitol phosphate
recombinant full-length protein, pH not specified in the publication, temperature not specified in the publication
2.84
polyribitol phosphate
truncated protein, residues 1-349, pH not specified in the publication, temperature not specified in the publication
0.021
UDP-N-acetyl-D-glucosamine
truncated protein, residues 1-349, pH not specified in the publication, temperature not specified in the publication
0.045
UDP-N-acetyl-D-glucosamine
recombinant full-length protein, pH not specified in the publication, temperature not specified in the publication
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0.6 - 1.1
polyribitol phosphate
0.053 - 0.062
UDP-N-acetyl-D-glucosamine
0.6
polyribitol phosphate
recombinant full-length protein, pH not specified in the publication, temperature not specified in the publication
1.1
polyribitol phosphate
truncated protein, residues 1-349, pH not specified in the publication, temperature not specified in the publication
0.053
UDP-N-acetyl-D-glucosamine
recombinant full-length protein, pH not specified in the publication, temperature not specified in the publication
0.062
UDP-N-acetyl-D-glucosamine
truncated protein, residues 1-349, pH not specified in the publication, temperature not specified in the publication
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UniProt
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UniProt
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Highest Expressing Human Cell Lines
Filter by:
Cell Line Links
Gene Links
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physiological function
methicillin-resistant Staphylococcus aureus is sensitized to beta-lactams upon tarS deletion. Strains lacking tarS have no growth or cell division defects
physiological function
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methicillin-resistant Staphylococcus aureus is sensitized to beta-lactams upon tarS deletion. Strains lacking tarS have no growth or cell division defects
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TARS_STAAM
573
0
66257
Swiss-Prot
other Location (Reliability: 1 )
TARS_STAAW
573
0
66255
Swiss-Prot
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200000
size exclusion chromatography-multiangle light scattering
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trimer
3 * 66000, calculated
trimer
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3 * 66000, calculated
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TarS shows an architecture with closely-associated trimerization domains connected by a linker region to three protruding catalytic domains that face away from each other
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D178N
severe decrease in activity
D91A
active-site mutant, complete loss of activity
D93A
active-site mutant, complete loss of activity
D94A
active-site mutant, complete loss of activity
E177A
active-site mutant, complete loss of activity
H210A
active-site mutant, complete loss of activity
M521R
structure-guided mutant, aimed at disrupting the trimerization interface. Mutation results in the expression of insoluble protein aggregates
M532R
structure-guided mutant, aimed at disrupting the trimerization interface. Mutation results in the expression of insoluble protein aggregates
R206A
severe decrease in activity
R75A
active-site mutant, complete loss of activity
S212A
severe decrease in activity
D91A
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active-site mutant, complete loss of activity
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D93A
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active-site mutant, complete loss of activity
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M521R
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structure-guided mutant, aimed at disrupting the trimerization interface. Mutation results in the expression of insoluble protein aggregates
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M532R
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structure-guided mutant, aimed at disrupting the trimerization interface. Mutation results in the expression of insoluble protein aggregates
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R75A
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active-site mutant, complete loss of activity
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medicine
methicillin-resistant Staphylococcus aureus is sensitized to beta-lactams upon tarS deletion. Strains lacking tarS have no growth or cell division defects
medicine
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methicillin-resistant Staphylococcus aureus is sensitized to beta-lactams upon tarS deletion. Strains lacking tarS have no growth or cell division defects
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Nathesnon, S.; Strominger, J.
Enzymatic synthesis of N-acetylglucosaminylribitol linkages in teichoic acid from Staphylococcus aureus, strain Copenhagen
J. Biol. Chem.
238
3161-3169
1963
Staphylococcus aureus, Staphylococcus aureus Copenhagen
brenda
Sobhanifar, S.; Worrall, L.; King, D.; Wasney, G.; Baumann, L.; Gale, R.; Nosella, M.; Brown, E.; Withers, S.; Strynadka, N.
Structure and mechanism of Staphylococcus aureus TarS, the wall teichoic acid beta-glycosyltransferase involved in methicillin resistance
PLoS Pathog.
12
e10066067
2016
Staphylococcus aureus (A0A0H3JPC6), Staphylococcus aureus ATCC 700699 (A0A0H3JPC6)
brenda
Brown, S.; Xia, G.; Luhachack, L.; Campbell, J.; Meredith, T.; Chen, C.; Winstel, V.; Gekeler, C.; Irazoqui, J.; Peschel, A.; Walker, S.
Methicillin resistance in Staphylococcus aureus requires glycosylated wall teichoic acids
Proc. Natl. Acad. Sci. USA
109
18909-18914
2012
Staphylococcus aureus (A0A0H3JPC6), Staphylococcus aureus ATCC 700699 (A0A0H3JPC6)
brenda
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