ProGP216 (BclA (collagen-like protein))

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ProGP ID ProGP216 (BclA (collagen-like protein))
Validation Status Uncharacterized
Organism Information
Organism NameBacillus anthracis str. Ames (Sterne 7702)
Domain Bacteria
Classification Phylum : Firmicutes
Class : Bacilli
Orders : Bacillales
Family : Bacillaceae
Genus : Bacillus
Species : anthracis
Taxonomic ID (NCBI) 1392
Genome Information
GenBank AE016879.1
EMBL AE016879
Organism Additional Information Bacillus anthracis is a Gram-positive bacterium that forms spores, the causal agent of anthrax. This lethal infection involves both toxaemia and septicaemia.
Gene Information
Gene NamebclA (BA_1222)
NCBI Gene ID 1084744
GenBank Gene Sequence NC_003997.3
Protein Information
Protein NameBclA (collagen-like protein)
UniProtKB/SwissProt ID Q81JD7
NCBI RefSeq WP_000069710.1
Sequence length 382 AA
Subcellular LocationSurface
Function It is the major glycoprotein of exosporium and also the immunodominant protein of the spore surface. Exosporium is a loose fitting layer enclosing the spore. BclA forms the filaments of the external hair-like nap of the exosporium.
Protein Structure
Glycosylation Status
Technique(s) used for Glycosylation DetectionECL Glycoprotein detection kit and chemical deglycosylation using trifluoromethanesulfonic acid (TFMS).
Glycan Information
Glycan Annotation The protein is extensively O-glycosylated with a 715-Da Tetrasaccharide and a 324-Da disaccharide. The Tetrasaccharide contains three rhamnose residues and an unusual terminal sugar, 2-O-methyl-4- (3-hydroxy-3-methylbutanamido)-4,6-dideoxy-D-glucopyranose, named anthrose (Ant). The Tetrasaccharide has the structure:β-Ant-(1→3)-α-L-Rhap-(1→3)-α-L-Rhap-(1→2)-L-Rhap. Oligosaccharide is attached to the BclA through a GalNAc linker. In its absence, GlcNAc can serve as a substitute linker.
BCSDB ID 23688
GlyTouCan G04931OZ
Protein Glycosylation linked (PGL) gene(s)
Additional CommentOwing to its absence in related strains of bacteria, anthrose has been regarded as a potential biomarker for anthrax detection.
A hydrophilic collagen-like region (CLR) from 41?250 residue consists of 70 triplet repeats (GXX) including 54 GPT triplets. The CLR is the prominent feature of BclA. BclA has got a high glycine and proline content like that of mammalian collagen.
Year of Identification2002
Year of Identification Month Wise2002.7
ReferenceOberli, M.A., Tamborrini, M., Tsai, Y.H., Werz, D.B., Horlacher, T., Adibekian, A., Gauss, D., Möller, H.M., Pluschke, G. and Seeberger, P.H., 2010. Molecular analysis of Carbohydrate− Antibody interactions: case study using a Bacillus anthracis Tetrasaccharide. Journal of the American Chemical Society, 132(30), pp.10239-10241.
Corresponding Author Peter H. Seeberger
ContactDepartment of Biomolecular Systems, Max-Planck Institute for Colloids and Interfaces, 14476 Potsdam, Germany.
ReferenceTamborrini, M., Holzer, M., Seeberger, P.H., Schürch, N. and Pluschke, G., 2010. Anthrax spore detection by a luminex assay based on monoclonal antibodies that recognize anthrose-containing oligosaccharides. Clinical and Vaccine Immunology, 17(9), pp.1446-1451.
Corresponding Author Marco Tamborrini
ContactSwiss Tropical and Public Health Institute, Socinstr. 57, CH 4002 Basel, Switzerland
ReferenceDong, S., Chesnokova, O.N., Turnbough Jr, C.L. and Pritchard, D.G., 2009. Identification of the UDP-N-acetylglucosamine 4-epimerase involved in exosporium protein glycosylation in Bacillus anthracis. Journal of bacteriology, 191(22), pp.7094-7101.
Corresponding Author David G Pritchard
ContactDepartment of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, Birmingham, AL 35294-2170, USA.
ReferenceSaksena, R., Adamo, R. and Kováč, P., 2006. Synthesis of the tetrasaccharide side chain of the major glycoprotein of the Bacillus anthracis exosporium. Bioorganic & medicinal chemistry letters, 16(3), pp.615-617.
Corresponding Author Pavol Ková?
ContactNational Institute of Diabetes and Digestive and Kidney Disease/LMC, National Institutes of Health, Bethesda, MD 20892-0815, USA.