ProGP1160 (BCAL2640)

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ProGP ID ProGP1160 (BCAL2640)
Validation Status Uncharacterized
Organism Information
Organism NameBurkholderia cenocepacia
Domain Bacteria
Classification Phylum : Proteobacteria
Class : Betaproteobacteria
Orders : Burkholderiales
Family : Burkholderiaceae
Genus : Burkholderia
Species : cenocepacia
Taxonomic ID (NCBI) 216591
Genome Information
GenBank AM747720.1
EMBL AM747720
Organism Additional Information It is the causative agent of human tuberculosis. The pathogenesis is influenced by its lipoglycans and glycolipids (having a wide range of immunomodulatory activities), and a variety of its virulence factors and antigens.
Gene Information
Gene NamepglL
Protein Information
Protein NameBCAL2640
UniProtKB/SwissProt ID B4E8D4
NCBI RefSeq CAR52942.1
UniProtKB Sequence >CAR52942.1 putative exported protein [Burkholderia cenocepacia J2315] MATHGRLRAMRAALAALVVWTAGLAGLAGAGVAHAEVAAADPIDVAMRQCLARRDRSSPAGQIQCMGEAQQQWQTVMDGAYQRLLKDAPADAKRGWQDSQRRWLTWRKDEVLLLKAVYDTTRGTAYAMSSADLQLQPVRDRALALRGAADRYAPPPAAVPVAATSGAQGGAAAAAAPAGTKPANAPREPAVRRVRPCVQDAACEHALFDLNRYYQKLRRKMPAHSAGTLVRAQRAWVAFRDATAPLVGEDGRVDLIGARIATMKRLSETAGNR
Function Enhances growth under many different carbon sources as well as oxidative and osmotic stress
Glycosylation Status
Glycosylation Type O- (Ser/Thr) linked
Experimentally Validated Glycosite(s ) in Mature Protein>CAR52942.1 putative exported protein [Burkholderia cenocepacia J2315] MATHGRLRAMRAALAALVVWTAGLAGLAGAGVAHAEVAAADPIDVAMRQCLARRDRSSPAGQIQCMGEAQQQWQTVMDGAYQRLLKDAPADAKRGWQDSQRRWLTWRKDEVLLLKAVYDTTRGTAYAMSSADLQLQPVRDRALALRGAADRYAPPPAAVPVAATSGAQGGAAAAAAPAGTKPANAPREPAVRRVRPCVQDAACEHALFDLNRYYQKLRRKMPAHSAGTLVRAQRAWVAFRDATAPLVGEDGRVDLIGARIATMKRLSETAGNR
Technique(s) used for Glycosylation DetectionNMR spectrometry
Protein Glycosylation- Implication Loss of O-glycosylation is associated with growth defects under many different carbon sources as well as oxidative and osmotic stress
Glycan Information
Glycan Structureβ-Gal-(1→3)-α-GalNAc-(1→3)-β-GalNAc-(1→)
Technique(s) used for Glycan Identification NMR spectrometry and LC-MS based analyses
Literature
Year of Identification2019
ReferenceMohamed, Y.F., Scott, N.E., Molinaro, A., Creuzenet, C., Ortega, X., Lertmemongkolchai, G., Tunney, M.M., Green, H., Jones, A.M., DeShazer, D. and Currie, B.J., 2019. A general protein O-glycosylation machinery conserved in Burkholderia species improves bacterial fitness and elicits glycan immunogenicity in humans. Journal of Biological Chemistry, 294(36), pp.13248-13268.
Corresponding Author Miguel A. Valvano
ContactWellcome-Wolfson Institute of Experimental Medicine, Queen's University Belfast, Belfast BT97BL, United Kingdom Department of Microbiology and Immunology, University of Western Ontario, London, Ontario N6A 5C1, Canada