ProGP315 (Putative outer membrane protein)
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| ProGP ID | ProGP315 (Putative outer membrane 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 | BF0447 |
| GenBank Gene Sequence | NC_003228.3 |
| Protein Information | |
| Protein Name | Putative outer membrane protein |
| UniProtKB/SwissProt ID | Q5LI20 |
| NCBI RefSeq | WP_005784365.1 |
| EMBL-CDS | CAH06208.1 |
| UniProtKB Sequence | >tr|Q5LI20|Q5LI20_BACFN Putative outer membrane protein OS=Bacteroides fragilis (strain ATCC 25285 / NCTC 9343) GN=BF0447 PE=4 SV=1 MLKKIALLMMLILPMGVFAQNLKFGHINAMEIVSAMPEYTKAQSELQALNKQLGQDLQRS QEEFSKKYQEFMQQKDSLPAVIAERRQKELEDMMQRQEQFQAKAQQDMEKANNDLMAPVY KKLDDAIKAVGAAEGVIYIFDMARTPIPYVNEAQSINLTPKVKTQLGIK |
| Sequence length | 169 AA |
| Subcellular Location | Periplasm |
| Function | It is similar to E. coli chaperone Skp and is predicted to be involved in a chaperone system. |
| Glycosylation Status | |
| Glycosylation Type | O- (Ser) linked |
| Experimentally Validated Glycosite(s) in Full Length Protein | S77 |
| Experimentally Validated Glycosite(s ) in Mature Protein | S77 |
| Glycosite(s) Annotated Protein Sequence | >tr|Q5LI20|Q5LI20_BACFN Putative outer membrane protein OS=Bacteroides fragilis (strain ATCC 25285 / NCTC 9343) GN=BF0447 PE=4 SV=1 MLKKIALLMMLILPMGVFAQNLKFGHINAMEIVSAMPEYTKAQSELQALNKQLGQDLQRS QEEFSKKYQEFMQQKDS*(77)LPAVIAERRQKELEDMMQRQEQFQAKAQQDMEKANNDLMAPVY KKLDDAIKAVGAAEGVIYIFDMARTPIPYVNEAQSINLTPKVKTQLGIK |
| Sequence Around Glycosites (21 AA) | KYQEFMQQKDSLPAVIAERRQ |
| Technique(s) used for Glycosylation Detection | Mass shift detected on SDS-polyacrylamide gel, AAL (Aleuria aurantia lectin) reactivity, Pro-Q Emerald Glycostaining and reactivity towards anti-glycan antiserum. |
| 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. |