| ProGlyProt ID | BU117 |
| Organism Information |
| Organism Name | Bacillus thuringiensis |
| Domain | Bacteria |
| Classification | Family: Bacillaceae
Order: Bacillales
Class: Bacilli (or Firmibacteria)
Division or phylum: "Firmicutes" |
| Taxonomic ID (NCBI) | |
| Genome Sequence (s) |
| GeneBank | |
| EMBL | |
| Gene Information |
| Gene Name | exsJ |
| NCBI Gene ID | |
| Protein Information |
| Protein Name | 72-kDa glycoprotein (ExsJ) |
| UniProtKB/SwissProt ID | |
| NCBI RefSeq | |
| EMBL-CDS | |
| UniProtKB Sequence | |
| Sequence length | |
| Subcellular Location | Surface (Exosporium and/or the spore coat) |
| Function | 72-kDa ExsJ glycoprotein forms a multimer of 205-kDa mass. They are found in sporangia. |
| Glycosylation Status |
| Glycosylation Type | Information currently not available with us. |
| Technique(s) used for Glycosylation Detection | Deglycosylation with trifluoromethanesulfonic acid (TFMS) |
| Literatures |
| Reference(s) | 1) Garcia-Patrone, M. and Tandecarz, J.S. (1995) A glycoprotein multimer from Bacillus thuringiensis sporangia: dissociation into subunits and sugar composition. Mol Cell Biochem, 145, 29-37. [PubMed: 7659076] |
| Year of Identification | 1995 |
