ProGP207 (Glycopeptidolipid (GPL))
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ProGP ID | ProGP207 (Glycopeptidolipid (GPL)) |
Validation Status | Uncharacterized |
Organism Information | |
Organism Name | Mycobacterium smegmatis |
Domain | Bacteria |
Classification | Phylum : Actinobacteria Class : Actinomycetia Orders : Corynebacteriales Family : Mycobacteriaceae Genus : Mycobacterium Species : smegmatis |
Taxonomic ID (NCBI) | 1772 |
Genome Information | |
GenBank | DQ066883.1 |
EMBL | DQ066883 |
Protein Information | |
Protein Name | Glycopeptidolipid (GPL) |
UniProtKB Sequence | N-acylated tripeptide-amino alcohol (D-Phe-D-allo-Thr?D-Ala-L-alaninol) |
Subcellular Location | Surface |
Function | Role in both sliding motility and biofilm formation. |
Glycosylation Status | |
Glycosylation Type | O- (Thr) linked |
Technique(s) used for Glycosylation Detection | MALDI-TOF MS (matrix assisted laser desorption/ionization time of flight mass spectrometry) analysis |
Glycan Information | |
Glycan Annotation | C-terminal L-alaninol is glycosylated by an O-methylated rhamnosyl residue (Rha) and the D-allo-Thr is linked to a 6-deoxytalose (6-dTal). |
Literature | |
Year of Identification | 2001 |
Year of Identification Month Wise | 2001.9 |
Reference | Recht, J. and Kolter, R., 2001. Glycopeptidolipid acetylation affects sliding motility and biofilm formation in Mycobacterium smegmatis. Journal of bacteriology, 183(19), pp.5718-5724. |
Corresponding Author | Roberto Kolter |
Contact | Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115, USA. |