Entry Name Teichoic acid biosynthesis
Description Teichoic acids (TAs) are a class of cell surface glycopolymers found in the cell wall of Gram-positive bacteria. They are anionic polymers consisting of glycerol phosphate (GroP) or ribitol phosphate (RboP) repeat units linked by phosphodiester bonds. There are two types of teichoic acids: wall teichoic acid (WTA), which is attached to peptidoglycan by a disaccharide linkage unit, and lipoteichoic acid (LTA), which is attached to the plasma membrane by the Glc-DAG anchor. The repat units of both WTA and LTA may further be modified by glycosyl residues and/or D-alanine esters, generating structural variations.
Class Metabolism; Glycan biosynthesis and metabolismBRITE hierarchy
Pathway map Orthology K00712 tagE; poly(glycerol-phosphate) alpha-glucosyltransferase [EC:2.4.1.52 ]
K01005 tagT_U_V; polyisoprenyl-teichoic acid--peptidoglycan teichoic acid transferase
K02851 wecA, tagO, rfe; UDP-GlcNAc:undecaprenyl-phosphate/decaprenyl-phosphate GlcNAc-1-phosphate transferase [EC:2.7.8.33 2.7.8.35 ]
K03367 dltA; D-alanine--poly(phosphoribitol) ligase subunit 1 [EC:6.1.1.13 ]
K03429 ugtP; processive 1,2-diacylglycerol beta-glucosyltransferase [EC:2.4.1.315 ]
K03739 dltB; membrane protein involved in D-alanine export
K03740 dltD; D-alanine transfer protein
K05946 tagA, tarA; N-acetylglucosaminyldiphosphoundecaprenol N-acetyl-beta-D-mannosaminyltransferase [EC:2.4.1.187 ]
K07271 licD; lipopolysaccharide cholinephosphotransferase [EC:2.7.8.-]
K13678 cpoA; 1,2-diacylglycerol-3-alpha-glucose alpha-1,2-galactosyltransferase [EC:2.4.1.-]
K14188 dltC; D-alanine--poly(phosphoribitol) ligase subunit 2 [EC:6.1.1.13 ]
K18704 tarL; CDP-ribitol ribitolphosphotransferase / teichoic acid ribitol-phosphate polymerase [EC:2.7.8.14 2.7.8.47 ]
K19002 mgs, bgsB; 1,2-diacylglycerol 3-alpha-glucosyltransferase [EC:2.4.1.337 ]
K21285 tagB, tarB; teichoic acid glycerol-phosphate primase [EC:2.7.8.44 ]
K21591 tarF; teichoic acid glycerol-phosphate transferase [EC:2.7.8.45 ]
K22708 tarS; poly(ribitol-phosphate) beta-N-acetylglucosaminyltransferase [EC:2.4.1.355 ]
K22709 tarQ; poly(ribitol-phosphate) beta-glucosyltransferase [EC:2.4.1.53 ]
K22710 tarM; poly(ribitol-phosphate) alpha-N-acetylglucosaminyltransferase [EC:2.4.1.70 ]
K24300 wbpM, wbgZ, aatA; UDP-N-acetylglucosamine 4,6-dehydratase
K25599 ltaP; lipoteichoic acid primase
K25617 csbB; lipoteichoic acid polyisoprenyl-phosphate beta-N-acetylglucosaminyltransferase
K25618 gtlA; lipoteichoic acid polyisoprenyl-phosphate galactosyltransferase
K25619 yfhO; lipoteichoic acid glycosylation protein
K25620 gtlB; lipoteichoic acid galactosyltransferase
K25626 aatB, pat, wcfR; UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine / UDP-2-acetamido-4-dehydro-2,6-dideoxyglucose transaminase
K25651 licD3; teichoic acid ribitol-phosphate transferase
K25652 K25652 ; teichoic acid N-acetylgalactosaminyltransferase
K25653 K25653 ; teichoic acid N-acetylgalactosaminyltransferase
K25654 licD2; teichoic acid cholinephosphotransferase
K25658 licC; choline-phosphate cytidylyltransferase
K25660 tacL; lipoteichoic acid ligase
K25669 tarP; poly(ribitiol-phosphate) beta-1,3-N-acetylglucosaminyltransferase
Compound C00043 UDP-N-acetyl-alpha-D-glucosamine
C04574 di-trans,poly-cis-Undecaprenyl diphosphate
C04613 UDP-2-acetamido-4-dehydro-2,6-dideoxyglucose
C17556 di-trans,poly-cis-Undecaprenyl phosphate
G00177 N-Acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
G10610 UDP-N-acetyl-D-glucosamine
G10611 UDP-N-acetyl-D-galactosamine
G11112 UDP-N-acetyl-D-mannosamine
G13163 beta-GlcNAc-P-undecaprenol
G13164 N-Acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
G13165 4-O-[(2R)-1-Glycerophospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
G13168 Und-PP-GlcNAc-ManNAc-GroP-RboP
G13174 alpha-O-GlcNAcylated WTA
G13176 beta-O-GlcNAcylated WTA
G13184 Polyglycerolphosphate lipoteichoic acid
G13190 Polyglycerolphosphate lipoteichoic acid
Reference Authors Rismondo J, Gillis A, Grundling A
Title Modifications of cell wall polymers in Gram-positive bacteria by multi-component transmembrane glycosylation systems.
Journal Reference Authors Guo Y, Pfahler NM, Volpel SL, Stehle T
Title Cell wall glycosylation in Staphylococcus aureus: targeting the tar glycosyltransferases.
Journal Reference Authors Han X, Sun R, Sandalova T, Achour A.
Title Structural and functional studies of Spr1654: an essential aminotransferase in teichoic acid biosynthesis in Streptococcus pneumoniae.
Journal Reference Authors Rismondo J, Percy MG, Grundling A.
Title Discovery of genes required for lipoteichoic acid glycosylation predicts two distinct mechanisms for wall teichoic acid glycosylation.
Journal Reference Authors Gisch N, Schwudke D, Thomsen S, Hess N, Hakenbeck R, Denapaite D.
Title Lipoteichoic acid of Streptococcus oralis Uo5: a novel biochemical structure comprising an unusual phosphorylcholine substitution pattern compared to Streptococcus pneumoniae.
Journal Reference Authors Percy MG, Grundling A.
Title Lipoteichoic acid synthesis and function in gram-positive bacteria.
Journal Reference Authors Brown S, Santa Maria JP Jr, Walker S.
Title Wall teichoic acids of gram-positive bacteria.
Journal Reference Authors Reichmann NT, Cassona CP, Grundling A.
Title Revised mechanism of D-alanine incorporation into cell wall polymers in Gram-positive bacteria.
Journal Reference Authors Brown S, Xia G, Luhachack LG, Campbell J, Meredith TC, Chen C, Winstel V, Gekeler C, Irazoqui JE, Peschel A, Walker S
Title Methicillin resistance in Staphylococcus aureus requires glycosylated wall teichoic acids.
Journal Reference Authors Allison SE, D'Elia MA, Arar S, Monteiro MA, Brown ED
Title Studies of the genetics, function, and kinetic mechanism of TagE, the wall teichoic acid glycosyltransferase in Bacillus subtilis 168.
Journal Reference Authors Reichmann NT, Grundling A.
Title Location, synthesis and function of glycolipids and polyglycerolphosphate lipoteichoic acid in Gram-positive bacteria of the phylum Firmicutes.
Journal Reference Authors Brown S, Meredith T, Swoboda J, Walker S
Title Staphylococcus aureus and Bacillus subtilis W23 make polyribitol wall teichoic acids using different enzymatic pathways.
Journal Reference Authors Webb AJ, Karatsa-Dodgson M, Grundling A.
Title Two-enzyme systems for glycolipid and polyglycerolphosphate lipoteichoic acid synthesis in Listeria monocytogenes.
Journal Reference Authors Sewell EW, Pereira MP, Brown ED
Title The wall teichoic acid polymerase TagF is non-processive in vitro and amenable to study using steady state kinetic analysis.
Journal Reference Authors Meredith TC, Swoboda JG, Walker S.
Title Late-stage polyribitol phosphate wall teichoic acid biosynthesis in Staphylococcus aureus.
Journal Reference Authors Brown S, Zhang YH, Walker S
Title A revised pathway proposed for Staphylococcus aureus wall teichoic acid biosynthesis based on in vitro reconstitution of the intracellular steps.
Journal Reference Authors Zhang YH, Ginsberg C, Yuan Y, Walker S
Title Acceptor substrate selectivity and kinetic mechanism of Bacillus subtilis TagA.
Journal Reference Authors Bhavsar AP, Truant R, Brown ED
Title The TagB protein in Bacillus subtilis 168 is an intracellular peripheral membrane protein that can incorporate glycerol phosphate onto a membrane-bound acceptor in vitro.
Journal Reference Authors Soldo B, Lazarevic V, Karamata D
Title tagO is involved in the synthesis of all anionic cell-wall polymers in Bacillus subtilis 168.
Journal Related ko00900 Terpenoid backbone biosynthesis
