ProGP312 (Hypothetical protein)
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| ProGP ID | ProGP312 (Hypothetical protein) |
| Validation Status | Characterized |
| Organism Information | |
| Organism Name | Bacteroides 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 Name | BF0522 |
| NCBI Gene ID | 3286009 |
| GenBank Gene Sequence | NC_003228.3 |
| Protein Information | |
| Protein Name | Hypothetical protein |
| UniProtKB/SwissProt ID | Q5LHV3 |
| NCBI RefSeq | WP_005784472.1 |
| EMBL-CDS | CAH06277.1 |
| UniProtKB Sequence | >tr|Q5LHV3|Q5LHV3_BACFN Putative uncharacterized protein OS=Bacteroides fragilis (strain ATCC 25285 / NCTC 9343) GN=BF0522 PE=4 SV=1 MKRLIPILLAVFAFAACEKDPDMDKLDNDYLVYTNYDKKADFKQFSTYYIPDSVLVIGDK KDPEYWKGEAAEAIINAYKENLNSKGFTYTDNKDAADLGIQVSYVQSTYYFTDYGQPEWW WNYPGYWDAPYWGNWGGWYYPYVVNYSITTNSFLTEIMNLKAPEGEKQKLPVLWSSFLSG PASYSGKVNQTLVVRAINQSFAQSPYLTNK |
| Sequence length | 210 AA |
| Subcellular Location | Outer membrane (facing surface) |
| Function | It is suggested to be involved in the response to oxidative stress as it was found upregulated 6.1-fold on exposure of B. fragilis to air. |
| Glycosylation Status | |
| Glycosylation Type | O- (Ser) linked |
| Experimentally Validated Glycosite(s) in Full Length Protein | S53 |
| Experimentally Validated Glycosite(s ) in Mature Protein | S53 |
| Glycosite(s) Annotated Protein Sequence | >tr|Q5LHV3|Q5LHV3_BACFN Putative uncharacterized protein OS=Bacteroides fragilis (strain ATCC 25285 / NCTC 9343) GN=BF0522 PE=4 SV=1 MKRLIPILLAVFAFAACEKDPDMDKLDNDYLVYTNYDKKADFKQFSTYYIPDS*(53)VLVIGDK KDPEYWKGEAAEAIINAYKENLNSKGFTYTDNKDAADLGIQVSYVQSTYYFTDYGQPEWW WNYPGYWDAPYWGNWGGWYYPYVVNYSITTNSFLTEIMNLKAPEGEKQKLPVLWSSFLSG PASYSGKVNQTLVVRAINQSFAQSPYLTNK |
| Sequence Around Glycosites (21 AA) | KQFSTYYIPDSVLVIGDKKDP |
| Technique(s) used for Glycosylation Detection | Mass shift detected on SDS-polyacrylamide gel and Western blot (using wild-type and mutant B. fragilis cells for expression, and anti-His tag antibody detection) |
| Technique(s) used for Glycosylated Residue(s) Detection | Site-directed mutagenesis |
| Protein Glycosylation- Implication | Protein glycosylation is central to the physiology of B. fragilis and is necessary for the organism to competitively colonize the mammalian intestine. Deletion of the lfg (protein glycosylation machinery) region results in a substantial growth deficiency in vitro and a complete inability to compete with wild-type bacteria in the mouse intestine. |
| Glycan Information | |
| Glycan Annotation | Exogenous fucose. |
| Technique(s) used for Glycan Identification | Lectin (AAL)binding |
| Protein Glycosylation linked (PGL) gene(s) | |
| OST Gene Name | Putative fucosyl transferase |
| Predicted Accessory Gene(s) | BF4298-4306 region lfg (locus of fragilis glycosylation). |
| Additional Comment | 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 of 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 were not tolerated at third position of sequon in BF2494. Ile, Leu, and Val were 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 Identification | 2009 |
| Year of Identification Month Wise | 2009.4.17 |
| Year of Validation | 2011 |
| Reference | Fletcher, 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 |
| Contact | Channing Laboratory, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA. |
| Reference | Fletcher, C.M., Coyne, M.J., Villa, O.F., Chatzidaki-Livanis, M. and Comstock, L.E., 2009. A general O-glycosylation system important to the physiology of a major human intestinal symbiont. Cell, 137(2), pp.321-331. |
| Corresponding Author | Laurie E. Comstock |
| Contact | Channing Laboratory, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA. |