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EC Tree
IUBMB Comments Involved in the biosynthesis of poly glycerol phosphate teichoic acids in bacterial cell walls. This enzyme adds 30--50 glycerol units to the linker molecule, but only after it has been primed with the first glycerol unit by EC 2.7.8.44, teichoic acid poly(glycerol phosphate) primase. cf. EC 2.7.8.45, teichoic acid glycerol-phosphate transferase.
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
tagf protein, poly(glycerol phosphate) polymerase, teichoic acid polymerase, cgptase, cdp-glycerol glycerophosphotransferase, glycerophosphate synthetase,
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CDP-glycerol glycerophosphotransferase
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CDPglycerol glycerophosphotransferase
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CDPglycerol:poly(glycerophosphate) glycerophosphotransferase
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glycerophosphate synthetase
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glycerophosphotransferase, cytidine diphosphoglycerol
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poly(glycerol phosphate) polymerase
poly(glycerol phosphate)polymerase
teichoic acid glycerol transferase
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teichoic acid polymerase
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teichoic-acid synthase
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poly(glycerol phosphate) polymerase
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poly(glycerol phosphate) polymerase
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poly(glycerol phosphate)polymerase
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poly(glycerol phosphate)polymerase
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TagF protein
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n CDP-glycerol + 4-O-[(2R)-glycerophospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = n CMP + 4-O-{poly[(2R)-glycerophospho]-(2R)-glycerophospho}-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
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substituted phospho group transfer
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CDP-glycerol:4-O-[(2R)-glycerophospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol glycerophosphotransferase
Involved in the biosynthesis of poly glycerol phosphate teichoic acids in bacterial cell walls. This enzyme adds 30--50 glycerol units to the linker molecule, but only after it has been primed with the first glycerol unit by EC 2.7.8.44, teichoic acid poly(glycerol phosphate) primase. cf. EC 2.7.8.45, teichoic acid glycerol-phosphate transferase.
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CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
CDP-glycerol + membrane acceptor
CMP + ?
additional information
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CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
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crude extract of protoplast membrane preparation, CMP postulated
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CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
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involved in teichoic acid synthesis
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?
CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
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crude extract of protoplast membrane preparation, CMP postulated
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CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
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crude extract of membrane preparation
?
CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
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involved in teichoic acid synthesis
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?
CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
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the enzyme is responsible for the synthesis of wall teichoic acid
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?
CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
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the enzyme is responsible for the synthesis of wall teichoic acid
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?
CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
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crude extract of membrane preparation
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CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
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involved in teichoic acid synthesis
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?
CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
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?
CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
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?
CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
involved in teichoic acid synthesis
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?
CDP-glycerol + membrane acceptor
CMP + ?
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?
CDP-glycerol + membrane acceptor
CMP + ?
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?
additional information
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the enzyme plays a role in thermosensitivity
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?
additional information
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the enzyme plays a role in thermosensitivity
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?
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CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
additional information
?
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CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
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involved in teichoic acid synthesis
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?
CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
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involved in teichoic acid synthesis
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?
CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
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the enzyme is responsible for the synthesis of wall teichoic acid
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?
CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
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the enzyme is responsible for the synthesis of wall teichoic acid
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?
CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
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involved in teichoic acid synthesis
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?
CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
involved in teichoic acid synthesis
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?
additional information
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the enzyme plays a role in thermosensitivity
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?
additional information
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the enzyme plays a role in thermosensitivity
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?
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Ca2+
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0.01 M: optimal, requirement for a divalent cation
Mg2+
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0.04 M: optimal, requirement for a divalent cation
Mn2+
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slight stimulation, in presence of Mg2+ inhibition
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bacitracin
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94% of maximal activity
Cetylpyridinium chloride
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47% of maximal activity
CTP
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excess concentration causes slight inhibition
Mn2+
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slight stimulation, in presence of Mg2+ inhibition
novobiocin
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complete inhibition
penicillin
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27% of maximal activity
Ristocetin
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90% of maximal activity
spermidine
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78% of maximal activity
streptomycin
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89% of maximal activity
Vancomycin
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31% of maximal activity
Crystal violet
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22% of maximal activity
Crystal violet
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22% of maximal activity
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teichoic acid poly(glycerol phosphate) polymerase deficiency
CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase, which is involved in the synthesis of the major wall teichoic acid in Bacillus subtilis 168, is encoded by tagF (rodC).
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0.00083 - 0.75
CDP-glycerol
0.00083
CDP-glycerol
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0.23
CDP-glycerol
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wild-type enzyme
0.23
CDP-glycerol
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mutant enzyme E604A
0.39
CDP-glycerol
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mutant enzyme D630A
0.7
CDP-glycerol
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mutant enzyme E639A
0.75
CDP-glycerol
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mutant enzyme D645A
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0.12 - 0.233
CDP-glycerol
0.12
CDP-glycerol
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mutant enzyme D630A
0.167
CDP-glycerol
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mutant enzyme E604A
0.167
CDP-glycerol
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mutant enzyme E639A
0.217
CDP-glycerol
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mutant enzyme D645A
0.233
CDP-glycerol
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wild-type enzyme
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6.5 - 9.5
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50% of maximal activity at pH 6.5, 25% of maximal activity at pH 8.0, 70% of maximal activity at pH 9.5
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37
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assay at
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ATCC 9945
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brenda
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brenda
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ATCC 6051
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brenda
NCTC 3610
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brenda
wild-type
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brenda
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wild-type
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brenda
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UniProt
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ATCC 14990
SwissProt
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brenda
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brenda
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protoplast membrane
brenda
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brenda
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cell or protoplast
brenda
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cell or protoplast
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brenda
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malfunction
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a tagF1-tagF2 deletion mutant of Lactobacillus plantarum, strain WCFS1, lacks poly(glycerol phosphate) polymerase activity required for glycerol-type wall teichoic acid biosynthesis. The mutant activates an alternative genetic locus, tarIJKL, encoding the enzymes for nucleotide activation and incorporation of ribitol in the wall teichoic acid backbone polymer, structure analysis of the alternative ribitol-type wall teichoic acid backbone by HPAEC, UPLC-mass spectrometry, NMR spectroscopy, and MALDI-TOF mass spectrometry, overview, revealing a 1,5-linked poly(ribitol phosphate) which is substituted at the C-2 hydroxyl group of the ribitol residue with alpha-D-glucosyl at a frequency of 28%
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90400
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x * 90400, SDS-PAGE
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?
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x * 90400, SDS-PAGE
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x * 90400, SDS-PAGE
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structure of Staphylococcus epidermidis TagF is determined to 2.7 A resolution from a construct that includes both the membrane-targeting region and the glycerol-phosphate polymerase domains. TagF possesses a helical region for interaction with the lipid bilayer, placing the active site at a suitable distance for access to the membrane-bound substrate
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D630A
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the ratio of turnover number to KM-value is 3.3fold lower than the wild-type ratio
D645A
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the ratio of turnover number to KM-value is 3.5fold lower than the wild-type ratio
E604A
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the ratio of turnover number to KM-value is 1.3fold lower than the wild-type ratio
E639A
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the ratio of turnover number to KM-value is 3.9fold lower than the wild-type ratio
H474A
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the ratio of turnover number to KM-value is 4900fold lower than the wild-type ratio
H612A
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the ratio of turnover number to KM-value is more than 4900fold lower than the wild-type ratio
D630A
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the ratio of turnover number to KM-value is 3.3fold lower than the wild-type ratio
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E604A
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the ratio of turnover number to KM-value is 1.3fold lower than the wild-type ratio
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E639A
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the ratio of turnover number to KM-value is 3.9fold lower than the wild-type ratio
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H474A
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the ratio of turnover number to KM-value is 4900fold lower than the wild-type ratio
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H612A
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the ratio of turnover number to KM-value is more than 4900fold lower than the wild-type ratio
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DELTA 312-721
truncated construct contains membrane binding region, truncated construct shows same activity as full-length wild-type
H444N
mutant crystallizes identical to wild-type, mutant shows no detectable activity compared to wild-type
H584A
mutant crystallizes identical to wild-type, mutant shows no detectable activity compared to wild-type
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-70°C, little loss of activity after 6 months
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-80°C, 20% glycerol, stable for several months
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-80°C, the carboxy-terminal His6-tagged TagF protein is stable for several months
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frozen, no essential loss of activity within several weeks
frozen, no essential loss of activity within several weeks
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frozen, no essential loss of activity within several weeks
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fusion protein with glutathione S-transferase
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fusion protein with glutathione S-transferase
N-terminally truncated construct comprising the catalytic glycerol-phosphate transferase region of the enzyme (residues 312-721) is expressed
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Burger, M.M.; Glaser, L.
The synthesis of teichoic acids. I. POLYGLYCEROPHOSPHATE
J. Biol. Chem.
239
3168-3177
1964
Bacillus subtilis, Bacillus licheniformis
brenda
Pooley, H.M.; Abellan, F.X.; Karamata, D.
CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase, which is involved in the synthesis of the major wall teichoic acid in Bacillus subtilis 168, is encoded by tagF (rodC)
J. Bacteriol.
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646-649
1992
Bacillus subtilis, Bacillus subtilis 168
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brenda
Fitzgerald, S.N.; Foster, T.J.
Molecular analysis of the tagF gene, encoding CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase of Staphylococcus epidermidis ATCC 14990
J. Bacteriol.
182
1046-1052
2000
Staphylococcus epidermidis (Q9RPD1), Staphylococcus epidermidis
brenda
Schertzer, J.W.; Brown, E.D.
Purified, recombinant TagF protein from Bacillus subtilis 168 catalyzes the polymerization of glycerol phosphate onto a membrane acceptor in vitro
J. Biol. Chem.
278
18002-18007
2003
Bacillus subtilis, Bacillus subtilis 168
brenda
Schertzer, J.W.; Bhavsar, A.P.; Brown, E.D.
Two conserved histidine residues are critical to the function of the TagF-like family of enzymes
J. Biol. Chem.
280
36683-36690
2005
Bacillus subtilis, Bacillus subtilis 168
brenda
Lovering, A.L.; Lin, L.Y.; Sewell, E.W.; Spreter, T.; Brown, E.D.; Strynadka, N.C.
Structure of the bacterial teichoic acid polymerase TagF provides insights into membrane association and catalysis
Nat. Struct. Mol. Biol.
17
582-589
2010
Staphylococcus epidermidis (Q5HLM5), Staphylococcus epidermidis
brenda
Tomita, S.; de Waard, P.; Bakx, E.J.; Schols, H.A.; Kleerebezem, M.; Bron, P.A.
The structure of an alternative wall teichoic acid produced by a Lactobacillus plantarum WCFS1 mutant contains a 1,5-linked poly(ribitol phosphate) backbone with 2-alpha-D-glucosyl substitutions
Carbohydr. Res.
370
67-71
2013
Lactiplantibacillus plantarum
brenda
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