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Information on EC 2.4.99.19 - undecaprenyl-diphosphooligosaccharide-protein glycotransferase and Organism(s) Campylobacter jejuni and UniProt Accession Q5HTX9

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IUBMB Comments
A bacterial enzyme that has been isolated from Campylobacter jejuni and Campylobacter lari . It forms a glycoprotein by the transfer of a glucosyl-N-acetylgalactosaminyl-N,N'-diacetylbacillosamine (GalNAc2(Glc)GalNAc3diNAcBac) polysaccharide and related oligosaccharides to the side-chain of an L-asparagine residue in the sequence -Asp/Glu-Xaa-Asn-Xaa'-Ser/Thr- (Xaa and Xaa' not Pro) in nascent polypeptide chains. Requires Mn2+ or Mg2+. Occurs on the external face of the plasma membrane. The polyprenol involved is normally tritrans,heptacis-undecaprenol but a decaprenol is used by some species.
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Campylobacter jejuni
UNIPROT: Q5HTX9
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Word Map
The taxonomic range for the selected organisms is: Campylobacter jejuni
The enzyme appears in selected viruses and cellular organisms
Synonyms
pglb2, n-oligosaccharyltransferase, bacterial oligosaccharyltransferase, bacterial ost, pglb protein, oligosacharyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oligosaccharyltransferase
-
bacterial oligosaccharyltransferase
-
-
bacterial OST
-
-
N-oligosaccharyltransferase
-
-
oligosaccharyl transferase
-
-
oligosaccharyltransferase
-
-
oligosacharyltransferase
-
-
PglB oligosaccharyltransferase
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
tritrans,heptacis-undecaprenyl-diphosphooligosaccharide:protein-L-asparagine N-beta-D-oligosaccharidotransferase
A bacterial enzyme that has been isolated from Campylobacter jejuni [1] and Campylobacter lari [2]. It forms a glycoprotein by the transfer of a glucosyl-N-acetylgalactosaminyl-N,N'-diacetylbacillosamine (GalNAc2(Glc)GalNAc3diNAcBac) polysaccharide and related oligosaccharides to the side-chain of an L-asparagine residue in the sequence -Asp/Glu-Xaa-Asn-Xaa'-Ser/Thr- (Xaa and Xaa' not Pro) in nascent polypeptide chains. Requires Mn2+ or Mg2+. Occurs on the external face of the plasma membrane. The polyprenol involved is normally tritrans,heptacis-undecaprenol but a decaprenol is used by some species.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(bacillosamine1) undecaprenyl diphosphate + Ac-D-F-N-V-TNH(CH2CH2O)2CH2CH2NH-BODIPY
?
show the reaction diagram
-
-
-
-
?
(GalNAc2-bacillosamine1) undecaprenyl diphosphate + Ac-D-F-N-V-TNH(CH2CH2O)2CH2CH2NH-BODIPY
?
show the reaction diagram
-
-
-
-
?
(Glc1GalNAc5-bacillosamine1) undecaprenyl diphosphate + Ac-D-F-N-V-TNH(CH2CH2O)2CH2CH2NH-BODIPY
?
show the reaction diagram
-
-
-
-
?
Lys-Asp-Phe-Asn-Val-Ser-Lys-Ala + N-acetyl-alpha-D-galactosaminyl-diphospho-tritrans,heptacis-undecaprenol
tritrans,heptacis-undecaprenyl diphosphate + Lys-Asp-Phe-N4-[N-acetyl-beta-D-galactosaminyl]-Asn-Val-Ser-Lys-Ala
show the reaction diagram
-
a chemically synthesized sugar donor with synthesized peptide acceptor
-
-
?
N-acetyl-D-galactosaminyl-alpha-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol + KDFNVSKA
tritrans,heptacis-undecaprenyl diphosphate + Lys-Asp-Phe-N4-[N-acetyl-D-galactosaminyl-alpha-(1->3)-N,N'-diacetyl-beta-D-bacillosaminyl]-Asn-Val-Ser-Lys-Ala
show the reaction diagram
-
oligosaccharyl transferase activity of PglB in vitro with synthetic disaccharide glycan donor and peptide acceptor substrate
-
-
?
tritrans,heptacis-undecaprenyl diphospho-O1 antigen + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-O1 antigen
show the reaction diagram
-
from Shigella dysenteriae
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphospho-O11 antigen + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-O11 antigen
show the reaction diagram
-
from Pseudomonas aeruginosa
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphospho-O157 antigen + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-O157 antigen
show the reaction diagram
-
from Escherichia coli
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphospho-O16 antigen + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-O16 antigen
show the reaction diagram
-
from Escherichia coli
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphospho-O7 antigen + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-O7 antigen
show the reaction diagram
-
from Escherichia coli
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphospho-O9 antigen + [Acra]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [Acra]-L-asparagine-O9 antigen
show the reaction diagram
-
PglB transfers the O9a antigen, an ABC transporter-dependent O antigen, to AcrA in Escherichia coli strain CWG28, the K30 antigen is not transferred to AcrA
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
show the reaction diagram
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
show the reaction diagram
-
-
-
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
the physiological cation is Mn2+, but PglB is also active with Mg2+
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene pglB
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
bacterial PglB and archaeal AglB constitute a protein family of the catalytic subunit of OST, along with STT3 from eukaryotes, that has three types of OST catalytic centers, structure analysis and comparison, overview
evolution
malfunction
-
if the WWDYGY signature sequence is mutated to WAAYGY, PglB is no longer active in vivo
metabolism
physiological function
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
82000
-
x * 82000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 82000, SDS-PAGE
monomer
-
sequence and structure comparison with STT3 subunit of the eukaryotic OST complex
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified detagged and methylated wild-type and selenomethionine-labeled C-terminal globular domain of PglB, hanging drop vapour diffusion method, 500 nl of 10 mg/ml protein in 10 mM Tris-HCl, pH 8.0, is mixed in an 1:1 ratio with reservoir solution containing 0.1 M sodium cacodylate, pH 6.5, 18% PEG 8000, 0.2 M calcium acetate, 20°C, X-ray diffraction structure determination and analysis at 2.8 A resolution
PglB crystal structure analysis
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D152E
-
site-directed mutagenesis, D152 and E316 can both be mutated to their acidic counterparts (D152E and E316D) and still retain activity, albeit at a notably decreased level
D475A
-
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
D475E
-
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
D54A
-
site-directed mutagenesis, the increased Und-PP-Bac-GalNAc substrate concentration has little effect on the mutant activity
E316D
-
site-directed mutagenesis, D152 and E316 can both be mutated to their acidic counterparts (D152E and E316D) and still retain activity, albeit at a notably decreased level
E316Q
-
site-directed mutagenesis, inactive mutant
K478A
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged full-length PglB from Escherichia coli strain BL21(DE3) in the membrane fraction by ultracentrifugation, recombinant GST-tagged wild-type and selenomethionine-labeled C-terminal globular domain of PglB from Escherichia coli strain BL21(DE3)pLysS by glutathione affinity chromatography and cleavage of the tag by 3C protease, followed by to reductive methylation of the lysine residues, gel filtration, and anion exchange chromatography
recombinant His-tagged PglB from Escherichia coli strain C43(DE3) by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene pglB, expression of the GST-tagged C-terminal globular domain of PglB in Escherichia coli strain BL21(DE3)pLysS, expression of His-tagged full-length PglB in Escherichia coli strain BL21(DE3)
expressed in Escherichia coli BL21-Gold (DE3) cells
-
gene pglB, expressio of the enzyme and the modified substrates in Escherichia coli
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gene pglB, expression of the wild-type and mutant WAAYGY-PglB variant in Escherichia coli in membranes
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gene pglB, functional expression in Escherichia coli
-
gene pglB, functional expression in Escherichia coli strains E69, CWG28, or CWG44 using an arabinose-inducible promoter, coexpression of the Acra protein substrate
-
gene pglB, large-scale overexpression of His-tagged PglB in Escherichia coli strain C43(DE3)
-
gene pglB, sequence and structure comparison with STT3 subunit of the eukaryotic OTase complex of Saccharomyces cerevisiae
-
gene pglB, sequence comparisons and phylogenetic analysis, functional expression in Escherichia coli. All genes necessary for N-linked glycosylation in Campylobacter jejuni are located in a single locus
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
application for protein glycosylation in recombinant bacteria in the production of potent conjugate vaccines where polysaccharide antigens of pathogenic bacteria are covalently bound to immunogenic carrier proteins
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Glover, K.J.; Weerapana, E.; Numao, S.; Imperiali, B.
Chemoenzymatic synthesis of glycopeptides with PglB, a bacterial oligosaccharyl transferase from Campylobacter jejuni
Chem. Biol.
12
1311-1315
2005
Campylobacter jejuni
Manually annotated by BRENDA team
Chen, M.M.; Glover, K.J.; Imperiali, B.
From peptide to protein: comparative analysis of the substrate specificity of N-linked glycosylation in C. jejuni
Biochemistry
46
5579-5585
2007
Campylobacter jejuni
Manually annotated by BRENDA team
Li, L.; Woodward, R.; Ding, Y.; Liu, X.W.; Yi, W.; Bhatt, V.S.; Chen, M.; Zhang, L.W.; Wang, P.G.
Overexpression and topology of bacterial oligosaccharyltransferase PglB
Biochem. Biophys. Res. Commun.
394
1069-1074
2010
Campylobacter jejuni
Manually annotated by BRENDA team
Jervis, A.J.; Langdon. R.; Hitchen, P.; Lawson, A.J.; Wood, A.; Fothergill, J.L.; Morris, H.R.; Dell, A.; Wren, B.; Linton, D.
Characterization of N-linked protein glycosylation in Helicobacter pullorum
J. Bacteriol.
192
5228-5236
2010
Campylobacter jejuni, Campylobacter jejuni NCTC 11168, Helicobacter pullorum, Helicobacter pullorum NCTC 12824
Manually annotated by BRENDA team
Maita, N.; Nyirenda, J.; Igura, M.; Kamishikiryo, J.; Kohda, D.
Comparative structural biology of eubacterial and archaeal oligosaccharyltransferases
J. Biol. Chem.
285
4941-4950
2010
Campylobacter jejuni (Q5HTX9), Campylobacter jejuni RM1221 (Q5HTX9)
Manually annotated by BRENDA team
Wacker, M.; Feldman, M.F.; Callewaert, N.; Kowarik, M.; Clarke, B.R.; Pohl, N.L.; Hernandez, M.; Vines, E.D.; Valvano, M.A.; Whitfield, C.; Aebi, M.
Substrate specificity of bacterial oligosaccharyltransferase suggests a common transfer mechanism for the bacterial and eukaryotic systems
Proc. Natl. Acad. Sci. USA
103
7088-7093
2006
Campylobacter jejuni
Manually annotated by BRENDA team
Jaffee, M.B.; Imperiali, B.
Exploiting topological constraints to reveal buried sequence motifs in the membrane-bound N-linked oligosaccharyl transferases
Biochemistry
50
7557-7567
2011
Campylobacter jejuni
Manually annotated by BRENDA team
Ihssen, J.; Kowarik, M.; Wiesli, L.; Reiss, R.; Wacker, M.; Thoeny-Meyer, L.
Structural insights from random mutagenesis of Campylobacter jejuni oligosaccharyltransferase PglB
BMC Biotechnol.
12
67
2012
Campylobacter jejuni
Manually annotated by BRENDA team
Ielmini, M.V.; Feldman, M.F.
Desulfovibrio desulfuricans PglB homolog possesses oligosaccharyltransferase activity with relaxed glycan specificity and distinct protein acceptor sequence requirements
Glycobiology
21
734-742
2011
Campylobacter jejuni, Desulfovibrio desulfuricans
Manually annotated by BRENDA team
Valderrama-Rincon, J.D.; Fisher, A.C.; Merritt, J.H.; Fan, Y.Y.; Reading, C.A.; Chhiba, K.; Heiss, C.; Azadi, P.; Aebi, M.; DeLisa, M.P.
An engineered eukaryotic protein glycosylation pathway in Escherichia coli
Nat. Chem. Biol.
8
434-436
2012
Campylobacter jejuni, Campylobacter lari
Manually annotated by BRENDA team
Lizak, C.; Gerber, S.; Numao, S.; Aebi, M.; Locher, K.
X-ray structure of a bacterial oligosaccharyltransferase
Nature
474
350-356
2011
Campylobacter jejuni, Campylobacter lari (B9KDD4), Campylobacter lari
Manually annotated by BRENDA team
Ishiwata, A.; Taguchi, Y.; Lee, Y.J.; Watanabe, T.; Kohda, D.; Ito, Y.
N-Glycosylation with synthetic undecaprenyl pyrophosphate-linked oligosaccharide to oligopeptides by PglB oligosaccharyltransferase from Campylobacter jejuni
ChemBioChem
16
731-737
2015
Campylobacter jejuni
Manually annotated by BRENDA team
Barre, Y.; Nothaft, H.; Thomas, C.; Liu, X.; Li, J.; Ng, K.K.S.; Szymanski, C.M.
A conserved DGGK motif is essential for the function of the PglB oligosaccharyltransferase from Campylobacter jejuni
Glycobiology
27
978-989
2017
Campylobacter jejuni
Manually annotated by BRENDA team