ProGP351 (BF0810)

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ProGP ID ProGP351 (BF0810)
Validation Status Characterized
Organism Information
Organism NameBacteroides fragilis (strain ATCC 25285 / NCTC 9343)
Domain Bacteria
Classification Phylum : Bacteroidetes
Class : Bacteroidia
Orders : Bacteroidales
Family : Bacteroidaceae
Genus : Bacteroides
Species : fragilis
Strain : strain ATCC 25285 / NCTC 9343
Taxonomic ID (NCBI) 272559
Genome Information
GenBank CR626927.1
EMBL CR626927
Organism Additional Information The Bacteroides constitute the major population of human intestinal microbiota. They are beneficial to the humans in terms of metabolism, development, and immunity. They play roles in recycling of bile acids, provision of short-chain fatty acids to the host and angiogenesis.
Gene Information
Gene NameBF0810
GenBank Gene Sequence NC_003228.3
Protein Information
Protein NameBF0810
UniProtKB/SwissProt ID Q5LH32
NCBI RefSeq WP_005785086.1
EMBL-CDSCAH06554.1
UniProtKB Sequence >tr|Q5LH32|Q5LH32_BACFN Putative alpha-L-fucosidase OS=Bacteroides fragilis (strain ATCC 25285 / NCTC 9343) GN=BF0810 PE=4 SV=1 MKNNRLIITLIALFLLGFGLKAQTASTEETAAQKEKRMEWFAQAKLGIFIHWGIYAVNGV SESWSFFNNYLPYEEYMAQEKGFTASAYNPQEWVKLIKESGARYTVITTKHHDGVALWDT KAGDLSTVKSTPAGRDLIAPFVKEVRKQGLKLGFYYSLLDWSHPDYPNKTRTEVRYKNDP DRWAKFVKFNFGQLSELNKTWKPDLYWFDGDWEQTAEAWDSKGIINLLRSTNPNVIVNSR IQGYGDYATPEQGVPVVRPADKYWELCMTMNDSWGYQHADTNYKTPFMLLRTFVDCLSMG GNLLLDIGPKEDGTIPAEQIAVLKEFGRWTKKHKEAIYETRAGIPCEHFQGYTTLNKAGD ILYLYLPYKPNGPIEVKGLVNKVNRVWVVGNGAMLPYKVYNKNYWSEVPGNLYIDIPERV QDEQITVIAVLLDGPIKLYRGVGQVIESN
Sequence length 449 AA
Function Putative alpha-L-fucosidase.
Glycosylation Status
Glycosylation Type O- (Thr) linked
Experimentally Validated Glycosite(s) in Full Length ProteinT84, T281 (Engineered glycosylation site DTA was created at two positions F83D and N282A)
Experimentally Validated Glycosite(s ) in Mature ProteinT84, T281 (Engineered glycosylation site DTA was created at two positions F83D and N282A)
Glycosite(s) Annotated Protein Sequence >tr|Q5LH32|Q5LH32_BACFN Putative alpha-L-fucosidase OS=Bacteroides fragilis (strain ATCC 25285 / NCTC 9343) GN=BF0810 PE=4 SV=1 MKNNRLIITLIALFLLGFGLKAQTASTEETAAQKEKRMEWFAQAKLGIFIHWGIYAVNGV SESWSFFNNYLPYEEYMAQEKGDT*(84)ASAYNPQEWVKLIKESGARYTVITTKHHDGVALWDT KAGDLSTVKSTPAGRDLIAPFVKEVRKQGLKLGFYYSLLDWSHPDYPNKTRTEVRYKNDP DRWAKFVKFNFGQLSELNKTWKPDLYWFDGDWEQTAEAWDSKGIINLLRSTNPNVIVNSR IQGYGDYATPEQGVPVVRPADKYWELCMTMNDSWGYQHADT*(281)AYKTPFMLLRTFVDCLSMG GNLLLDIGPKEDGTIPAEQIAVLKEFGRWTKKHKEAIYETRAGIPCEHFQGYTTLNKAGD ILYLYLPYKPNGPIEVKGLVNKVNRVWVVGNGAMLPYKVYNKNYWSEVPGNLYIDIPERV QDEQITVIAVLLDGPIKLYRGVGQVIESN
Sequence Around Glycosites (21 AA) EEYMAQEKGFTASAYNPQEWV
NDSWGYQHADTNYKTPFMLLR
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Technique(s) used for Glycosylation DetectionCoomassie staining, Pro-Q Emerald glycostaining, and reactivity with anti-glycan serum
Technique(s) used for Glycosylated Residue(s) Detection Known residues are mutated to create glycosylation motif/sequon
Glycan Information
Glycan Annotation Exogenous fucose.
Technique(s) used for Glycan Identification Lectin (AAL)binding
Protein Glycosylation linked (PGL) gene(s)
Additional CommentEngineered glycoprotein.
An example of engineered glycoprotein from a native protein.
Glycosylation sequon features: the sequon has an aspartate (D) preceding the glycosylated T or S which is followed by an amino acid with one or more methyl groups (alanine, isoleucine, or leucine; (D)(S/T)(A/I/L/V/M/T). Moreover, none of the 17 unglycosylated S and T residues examined in BF2494 (excluding two in the signal peptide) have a preceding D, although seven are followed by A, I, or L and one by V. Non methylated amino acids are not tolerated at third position of sequon in BF2494. Ile, Leu, and Val are found most frequently whereas Met is rarest at third position (reflecting the otherwise low number of Mets in proteins compared with the other five amino acids at the third position of the motif). The methyl group-containing amino acid at the third position being unreactive may play a role only in recognition of the site, whereas Asp residue may play a catalytic role.
Literature
Year of Identification2011
Year of Identification Month Wise2011.2.4
Year of Validation 2011
ReferenceFletcher, C.M., Coyne, M.J. and Comstock, L.E., 2011. Theoretical and experimental characterization of the scope of protein O-glycosylation in Bacteroides fragilis. Journal of Biological Chemistry, 286(5), pp.3219-3226.
Corresponding Author Laurie E. Comstock
ContactChanning Laboratory, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA.