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evolution
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proteins with PGT activity occur as monofunctional glycosyltransferases (MGTs) and as bifunctional penicillin-binding proteins (PBPs) designated as class A PBPs
evolution
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proteins with PGT activity occur as monofunctional glycosyltransferases (MGTs) and as bifunctional penicillin-binding proteins (PBPs) designated as class A PBPs
evolution
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proteins with PGT activity occur as monofunctional glycosyltransferases (MGTs) and as bifunctional penicillin-binding proteins (PBPs) designated as class A PBPs. Both forms contain a single transmembrane span at the N-terminus followed by the glycosyltransferase domain. In the class A PBPs, the C-terminus contains the transpeptidase domain. Bacterial species typically have multiple forms of these enzymes. Escherichia coli has 3 class A PBPs (PBP1a, PBP1b, and PBP1c) and 2 MGT proteins
evolution
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proteins with PGT activity occur as monofunctional glycosyltransferases (MGTs) and as bifunctional penicillin-binding proteins (PBPs) designated as class A PBPs. Both forms contain a single transmembrane span at the N-terminus followed by the glycosyltransferase domain. In the class A PBPs, the C-terminus contains the transpeptidase domain. Bacterial species typically have multiple forms of these enzymes. Staphylococcus aureus has a single class A PBP (PBP2) and 2 MGT proteins (SgtA, SgtB/MGT)
evolution
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the enzyme belongs to the glycosyltransferases of family 51 (GT51), the glycosyltransferases of family 51 are essential enzymes found in bacteria with peptidoglycan cell wall. They exist in two forms: as a monofunctional domain or linked to the N-terminal end of penicillin-binding (PB) domain in bifunctional PB proteins. Both forms catalyze the polymerization of lipid II (undecaprenyl pyrophosphate-MurNAc(pentapeptide)-GlcNAc) precursor to form linear glycan chains
evolution
Streptococcus pneumoniae contains three class A (PBP1a, PBP2a and PBP1b) and two class B (PBP2x and PBP2b) enzymes. PBP1a and PBP2a are not equivalent
evolution
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the enzyme belongs to the peptidoglycan glycosyltransferase family 51
evolution
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proteins with PGT activity occur as monofunctional glycosyltransferases (MGTs) and as bifunctional penicillin-binding proteins (PBPs) designated as class A PBPs
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evolution
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proteins with PGT activity occur as monofunctional glycosyltransferases (MGTs) and as bifunctional penicillin-binding proteins (PBPs) designated as class A PBPs. Both forms contain a single transmembrane span at the N-terminus followed by the glycosyltransferase domain. In the class A PBPs, the C-terminus contains the transpeptidase domain. Bacterial species typically have multiple forms of these enzymes. Escherichia coli has 3 class A PBPs (PBP1a, PBP1b, and PBP1c) and 2 MGT proteins
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evolution
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Streptococcus pneumoniae contains three class A (PBP1a, PBP2a and PBP1b) and two class B (PBP2x and PBP2b) enzymes. PBP1a and PBP2a are not equivalent
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evolution
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proteins with PGT activity occur as monofunctional glycosyltransferases (MGTs) and as bifunctional penicillin-binding proteins (PBPs) designated as class A PBPs
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evolution
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proteins with PGT activity occur as monofunctional glycosyltransferases (MGTs) and as bifunctional penicillin-binding proteins (PBPs) designated as class A PBPs. Both forms contain a single transmembrane span at the N-terminus followed by the glycosyltransferase domain. In the class A PBPs, the C-terminus contains the transpeptidase domain. Bacterial species typically have multiple forms of these enzymes. Staphylococcus aureus has a single class A PBP (PBP2) and 2 MGT proteins (SgtA, SgtB/MGT)
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malfunction
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inhibition of the enzyme blocks peptidoglycan synthesis and leads to bacterial lysis and death
malfunction
an Staphylococcus aureus sgtB transposon mutant, with the monofunctional peptidoglycan glycosyltransferase SgtB inactivated, display a 4fold increase in the MIC of oxacillin, suggesting that alterations in the peptidoglycan structure can help bacteria compensate for the lack of lipoteichoic acid (LTA). Muropeptide analysis of peptidoglycans isolated from a wild-type strain and sgtB mutant strain does not reveal any sizable alterations in the peptidoglycan structure. In contrast, the peptidoglycan isolated from an LTA-negative ltaS mutant strain shows a significant reduction in the fraction of highly cross-linked peptidoglycan, which is partially rescued in the sgtB ltaS double mutant suppressor strain. Introduction of SgtB or MazE in the respective suppressor strain results in growth arrest. Increased resistance of the sgtB mutant to oxacillin. The increase in peptidoglycan cross-linking potentially strengthens the cell wall to better sustain the high internal turgor pressure and might be at least partly responsible for the observed growth improvement
malfunction
DELTAmltG mutants in unencapsulated strains accumulate inactivation mutations of class A PBP1a. The reduction of cell width and size of DELTApbp1a mutants compared to those of wild-type parent cells. Mutations in pbp1a suppress the DELTAmltG mutations
malfunction
mutations that inactivate the pneumococcal YceG-domain protein, Spd_1346 (renamed MltG), remove the requirement for PBP2b. DELTAmltG mutants in unencapsulated strains accumulate inactivation mutations of class A PBP1a, which possesses TP and transglycosylase (TG) activities
malfunction
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DELTAmltG mutants in unencapsulated strains accumulate inactivation mutations of class A PBP1a. The reduction of cell width and size of DELTApbp1a mutants compared to those of wild-type parent cells. Mutations in pbp1a suppress the DELTAmltG mutations
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malfunction
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mutations that inactivate the pneumococcal YceG-domain protein, Spd_1346 (renamed MltG), remove the requirement for PBP2b. DELTAmltG mutants in unencapsulated strains accumulate inactivation mutations of class A PBP1a, which possesses TP and transglycosylase (TG) activities
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metabolism
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the enzyme also functions as an activity enhancer of SpoIIP which generates its substrate
metabolism
the pneumococcal YceG-domain protein MltG releases anchored peptidoglycan (PG) glycan strands synthesized by PBP1a for crosslinking by a PBP2b:RodA complex in peripheral PG synthesis
metabolism
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the pneumococcal YceG-domain protein MltG releases anchored peptidoglycan (PG) glycan strands synthesized by PBP1a for crosslinking by a PBP2b:RodA complex in peripheral PG synthesis
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physiological function
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isoform PBP3 is required for localization of MurG to division site
physiological function
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MtgA localizes at the division site of Escherichia coli cells that are deficient in PBP1b and produce a thermosensitive PBP1a and is able to interact with three constituents of the divisome, PBP3, FtsW, and FtsN in peptidoglycan assembly during the cell cycle
physiological function
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pbp-1C gene regulates in vitro growth and cell morphology, whereas pbp-1A, pbp-1B, and pbp-2 genes are essential for viability of Brucella melitensis
physiological function
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PGT catalyzes the polymerization of lipid II to form the bacterial cell wall
physiological function
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bifunctional penicillin-binding proteins (PBPs) proceed and catalyze the transglycosylation and transpeptidation. Bifunctional PBPs have both glycosyltransferase and transpeptidase catalytic sites that are located at N-terminus and C-terminus, respectively. In transglycosylation step, the glycosyltransferase polymerizes disaccharide phospholipid lipid II into polysaccharide strands. These oligosaccharide strands are cross-linked by transpeptidase to form peptidoglycans in the next transpeptidation step
physiological function
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bifunctional penicillin-binding proteins (PBPs) proceed and catalyze the transglycosylation and transpeptidation. Bifunctional PBPs have both glycosyltransferase and transpeptidase catalytic sites that are located at N-terminus and C-terminus, respectively. In transglycosylation step, the glycosyltransferase polymerizes disaccharide phospholipid lipid II into polysaccharide strands. These oligosaccharide strands are cross-linked by transpeptidase to form peptidoglycans in the next transpeptidation step
physiological function
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synthesis of bacterial cell wall requires the concerted action of peptidoglycan glycosyltransferases (PGT, also known as peptidoglycan transglycosylases) and transpeptidases. The PGT enzymes transfer the disaccharide-peptide from the lipid II substrate onto the growing glycan chain allowing TP enzymes to crosslink peptides from adjacent chains. The lipid II substrate is anchored into the cell membrane through an undecaprenyl (C55) tail. Each round of catalysis results in the extension of the peptidoglycan chain by two saccharides and in the release of undecaprenyl diphosphate (C55PP)
physiological function
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synthesis of bacterial cell wall requires the concerted action of peptidoglycan glycosyltransferases (PGT, also known as peptidoglycan transglycosylases) and transpeptidases. The PGT enzymes transfer the disaccharide-peptide from the lipid II substrate onto the growing glycan chain allowing TP enzymes to crosslink peptides from adjacent chains. The lipid II substrate is anchored into the cell membrane through an undecaprenyl (C55) tail. Each round of catalysis results in the extension of the peptidoglycan chain by two saccharides and in the release of undecaprenyl diphosphate (C55PP)
physiological function
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the enzyme catalyze the polymerization of lipid II to form linear glycan chains, which, after cross linking by the transpeptidases, form the net-like peptidoglycan macromolecule, which encases bacteria and protects them from rupture under their high cytoplasmic pressure
physiological function
the enzyme is involved in synthesis of peptidoglycan, a key cell wall component in nearly all bacteria, protecting the cell from bursting by its internal turgor and maintaining cell shape. Peptidoglycan consists of glycan strands connected by short peptides and forms a continuous, mesh-like structure around the cytoplasmic membrane, called the sacculus. In Gram-negative species, such as Escherichia coli, the sacculus is made of a mainly single layer of peptidoglycan with a thickness of 3-6 nm. The glycan strands are made of alternating N-acetylglucosamine (GlcNAc) and N-acetylmuramic acid (MurNAc) residues linked by beta-1,4 glyosidic bonds. The peptides contain L- and D-amino acids and are linked to MurNAc residues. The sequence is L-Ala-D-iGlu-m-Dap-D-Ala-D-Ala (m-Dap, meso-diaminopimelic acid). During cell growth and division, the surface of the sacculus is enlarged by the incorporation of new peptidoglycan material. In this process, the precursor lipid II (undecaprenyl-diphosphoryl-MurNAc(pentapeptide)-GlcNAc) is polymerized by the glycosyltransferase reaction of the GTase domain of enzyme PBP1B
physiological function
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the PGT enzymes transfer the disaccharide-peptide from the lipid II substrate onto the growing glycan chain allowing transpeptidase enzymes to crosslink peptides from adjacent chains. The lipid II substrate is anchored into the cell membrane through an undecaprenyl (C55) tail. The enzymatic reaction is thought to occur at the surface of the membrane
physiological function
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the PGT enzymes transfer the disaccharide-peptide from the lipid II substrate onto the growing glycan chain allowing transpeptidase enzymes to crosslink peptides from adjacent chains. The lipid II substrate is anchored into the cell membrane through an undecaprenyl (C55) tail. The enzymatic reaction is thought to occur at the surface of the membrane
physiological function
peptidoglycan (PG) is composed of glycan chains of beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) sugars that are crosslinked by PG peptides. Pneumococcal PG provides the major scaffold for the covalent attachment of wall-teichoic acid (WTA), capsule and surface proteins linked by sortases, many of which are virulence factors. Class A PBP1a, which possesses TP and transglycosylase (TG) activities
physiological function
peptidoglycan (PG) is composed of glycan chains of beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) sugars that are crosslinked by PG peptides. Pneumococcal PG provides the major scaffold for the covalent attachment of wall-teichoic acid (WTA), capsule and surface proteins linked by sortases, many of which are virulence factors. In the pathogen Streptococcus pneumoniae (pneumococcus), side-wall (peripheral) peptidoglycan (PG) synthesis emanates from midcells and is catalyzed by the essential class B penicillin-binding protein PBP2b transpeptidase (TP). Class B PBP2x and PBP2b are essential for growth and required for septal and peripheral PG synthesis, respectively, in dividing Streptococcus pneumoniae cells. Pbp2b is essential in unencapsulated or encapsulated wild-type D39 strains
physiological function
peptidoglycan glycosyltransferase (PGT) transfers the disaccharide-peptide of lipid II to the growing glycan chain in bacterial cell wall synthesis
physiological function
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peptidoglycan glycosyltransferases (GTases) of family 51 are essential enzymes for the synthesis of the glycan chains of the bacterial cell wall. Enzyme MtgA converts lipid II substrate into glycan chains
physiological function
Staphylococcus aureus has a typical Gram-positive cell envelope, which consists of a cytoplasmic membrane surrounded by a thick peptidoglycan layer. The peptidoglycan layer is a dynamic macromolecular structure that undergoes constant cycles of polymerization and hydrolysis to allow bacteria to grow and to divide. It is composed of glycan chains made of alternating N-acetylglucosamine and N-acetylmuramic acid residues connected by peptide bridges. This mesh-like sacculus is able to protect the cell from environmental threats while withstanding the high internal osmotic pressure. The final steps of peptidoglycan synthesis are catalyzed by enzymes termed penicillin binding proteins (PBPs) and coordinated actions of these enzymes are crucial for cell survival. PBPs with glycosyltransferase and transpeptidase activities polymerize the glycan chains and form peptide cross-bridges, while monofunctional transpeptidases, e.g. the monofunctional peptidoglycan glycosyltransferase SgtB in Staphylococcus aureus, have only the former activity. Important function of lipoteichoic acid (LTA) in cell wall integrity through its necessity for proper peptidoglycan assembly
physiological function
the majority of bacteria surround their cytoplasmic membrane with a peptidoglycan sacculus, a continuous layer that is required to maintain cell shape and osmotic stability. The basic chemical structure of peptidoglycan is well known, glycan strands consisting of alternating N -acetylglucosamine (GlcNAc) and N-acetylmuramic acid (MurNAc) residues connected by short stem peptides protruding from MurNAc. Peptides of neighboring glycan strands may be connected (i.e. cross-linked) forming a net-like layer. Peptide cross-links are formed by DD-transpeptidases. DD-transpeptidases covalently bind beta-lactam antibiotics such as penicillin, and are hence named penicillin-binding proteins (PBPs). Most bacteria possess several peptidoglycan synthases capable of catalyzing the glycosyltransferase (GTase) and/or transpeptidase (TPase) reactions. The Gram negative model organism Escherichia coli has three enzymes capable of performing both reactions, so-called bifunctional synthases: PBP1A, PBP1B, and PBP1C, two monofunctional transpeptidases, PBP2 and PBP3, and the monofunctional glycosyltransferase MtgA. The main peptidoglycan synthesis activity in the cell is provided by the semi-redundant PBP1A and PBP1B in consort with the transpeptidases PBP2 and PBP3, latter have essential roles in cell elongation and division, respectively. PBP1C and MtgA are dispensable for growth
physiological function
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synthesis of bacterial cell wall requires the concerted action of peptidoglycan glycosyltransferases (PGT, also known as peptidoglycan transglycosylases) and transpeptidases. The PGT enzymes transfer the disaccharide-peptide from the lipid II substrate onto the growing glycan chain allowing TP enzymes to crosslink peptides from adjacent chains. The lipid II substrate is anchored into the cell membrane through an undecaprenyl (C55) tail. Each round of catalysis results in the extension of the peptidoglycan chain by two saccharides and in the release of undecaprenyl diphosphate (C55PP)
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physiological function
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the PGT enzymes transfer the disaccharide-peptide from the lipid II substrate onto the growing glycan chain allowing transpeptidase enzymes to crosslink peptides from adjacent chains. The lipid II substrate is anchored into the cell membrane through an undecaprenyl (C55) tail. The enzymatic reaction is thought to occur at the surface of the membrane
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physiological function
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peptidoglycan (PG) is composed of glycan chains of beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) sugars that are crosslinked by PG peptides. Pneumococcal PG provides the major scaffold for the covalent attachment of wall-teichoic acid (WTA), capsule and surface proteins linked by sortases, many of which are virulence factors. Class A PBP1a, which possesses TP and transglycosylase (TG) activities
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physiological function
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peptidoglycan (PG) is composed of glycan chains of beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) sugars that are crosslinked by PG peptides. Pneumococcal PG provides the major scaffold for the covalent attachment of wall-teichoic acid (WTA), capsule and surface proteins linked by sortases, many of which are virulence factors. In the pathogen Streptococcus pneumoniae (pneumococcus), side-wall (peripheral) peptidoglycan (PG) synthesis emanates from midcells and is catalyzed by the essential class B penicillin-binding protein PBP2b transpeptidase (TP). Class B PBP2x and PBP2b are essential for growth and required for septal and peripheral PG synthesis, respectively, in dividing Streptococcus pneumoniae cells. Pbp2b is essential in unencapsulated or encapsulated wild-type D39 strains
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physiological function
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synthesis of bacterial cell wall requires the concerted action of peptidoglycan glycosyltransferases (PGT, also known as peptidoglycan transglycosylases) and transpeptidases. The PGT enzymes transfer the disaccharide-peptide from the lipid II substrate onto the growing glycan chain allowing TP enzymes to crosslink peptides from adjacent chains. The lipid II substrate is anchored into the cell membrane through an undecaprenyl (C55) tail. Each round of catalysis results in the extension of the peptidoglycan chain by two saccharides and in the release of undecaprenyl diphosphate (C55PP)
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physiological function
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the PGT enzymes transfer the disaccharide-peptide from the lipid II substrate onto the growing glycan chain allowing transpeptidase enzymes to crosslink peptides from adjacent chains. The lipid II substrate is anchored into the cell membrane through an undecaprenyl (C55) tail. The enzymatic reaction is thought to occur at the surface of the membrane
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physiological function
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bifunctional penicillin-binding proteins (PBPs) proceed and catalyze the transglycosylation and transpeptidation. Bifunctional PBPs have both glycosyltransferase and transpeptidase catalytic sites that are located at N-terminus and C-terminus, respectively. In transglycosylation step, the glycosyltransferase polymerizes disaccharide phospholipid lipid II into polysaccharide strands. These oligosaccharide strands are cross-linked by transpeptidase to form peptidoglycans in the next transpeptidation step
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additional information
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the enzyme contain a conserved hydrophobic surface that mediates its interaction with the cytoplasmic membrane and renders the purified protein polydisperse. Quantitative binding study of the MtgA by surface plasmon resonance
additional information
domain architecture of PBP1a
additional information
domain architecture of PBP1a
additional information
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domain architecture of PBP1a
additional information
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overall fold and active site of wild-type and mutant GTases
additional information
the single MltG(Y488D) change suppresses the requirement for PBP2b, MreCD, RodZ and RodA
additional information
the single MltG(Y488D) change suppresses the requirement for PBP2b, MreCD, RodZ and RodA
additional information
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the single MltG(Y488D) change suppresses the requirement for PBP2b, MreCD, RodZ and RodA
additional information
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domain architecture of PBP1a
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additional information
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the single MltG(Y488D) change suppresses the requirement for PBP2b, MreCD, RodZ and RodA
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