ProGP243 (Synthetic Glycopeptide)

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ProGP ID ProGP243 (Synthetic Glycopeptide)
Validation Status Characterized
Organism Information
Organism NameCampylobacter jejuni NCTC 11168
Domain Bacteria
Classification Phylum : Proteobacteria
Class : Epsilonproteobacteria
Orders : Campylobacterales
Family : Campylobacteraceae
Genus : Campylobacter
Species : jejuni
Strain : NCTC 11168
Taxonomic ID (NCBI) 197
Genome Information
GenBank AL111168.1
EMBL AL111168
Organism Additional Information Campylobacter jejuni is a microaerophilic, Gram-negative, human pathogen that is the major cause of bacterial food-borne diarrhoea (gastroenteritis). It is most frequently responsible for a form of post-infection neuromuscular paralysis known as Guillain Barre' syndrome. It also leads to an immunoproliferative small intestine disease that is a rare malignant lymphoma of the intestine. Motility is essential for pathogenicity.
Protein Information
Protein NameSynthetic Glycopeptide
UniProtKB Sequence KDFNVSKA
Sequence length 5 AA
Function NA
Glycosylation Status
Glycosylation Type N- (Asn) linked
Experimentally Validated Glycosite(s) in Full Length ProteinN4
Experimentally Validated Glycosite(s ) in Mature ProteinN4
Glycosite(s) Annotated Protein Sequence KDFN*(4)VSKA
Technique(s) used for Glycosylation DetectionIn vitro chemo enzymatic glycosylation,HPLC analysis of glycopeptides with reference to known glycopeptide HPLC profiles
Technique(s) used for Glycosylated Residue(s) Detection Not applicable
Protein Glycosylation- Implication Not applicable
Glycan Information
Glycan Annotation GalNAc-α1,3-bacillosamine.
BCSDB ID 20059
GlyTouCan G82182GL
Technique(s) used for Glycan Identification NanoLC-MS/MS analysis and NMR spectroscopy-COSY (correlated spectroscopy), TOCSY (total correlation spectroscopy), NOESY (nuclear Overhauser effect spectroscopy) spectra, and 1H-13C HMBC (heteronuclear multiple bond coherence) spectra.
Protein Glycosylation linked (PGL) gene(s)
OST Gene NamePglB
Additional CommentEngineered glycopeptide.
In vitro characterization of the oligosaccharyl transferase activity of PglB protein from membrane fraction of Campylobacter jejuni using a synthetic disaccharide glycan donor (GalNAc-β-1,3-bacillosamine-pyrophosphate-undecaprenyl) and a peptide acceptor substrate (KDFNVSKA).
Year of Identification2005
Year of Identification Month Wise2005.4.29
Year of Validation 2005
ReferenceGlover, K.J., Weerapana, E., Numao, S. and Imperiali, B., 2005. Chemoenzymatic synthesis of glycopeptides with PglB, a bacterial oligosaccharyl transferase from Campylobacter jejuni. Chemistry & biology, 12(12), pp.1311-1316.
Corresponding Author Barbara Imperiali
ContactDepartment of Chemistry and Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, USA.