ProGP356

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ProGP ID ProGP356
Validation Status Characterized
Organism Information
Organism NameBacteroides fragilis (strain ATCC 25285 / NCTC 9343)
Domain Bacteria
Classification Family: Bacteroidaceae
Order: "Bacteroidales"
Class: "Bacteroidia"
Division or phylum: "Bacteroidetes"
Taxonomic ID (NCBI) 272559
Genome Sequence(s)
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 NameftsQ (BF0252)
NCBI Gene ID 3289016
GenBank Gene Sequence 3289016
Protein Information
Protein NamePutative cell division protein
UniProtKB/SwissProt ID Q5LIJ9
NCBI RefSeq YP_209989.1
EMBL-CDSCAH06027.1
UniProtKB Sequence >tr|Q5LIJ9|Q5LIJ9_BACFN Putative cell division protein OS=Bacteroides fragilis (strain ATCC 25285 / NCTC 9343) GN=ftsQ PE=4 SV=1 MIKRILLTIVMLLLIAYLIAAVTVFNDKPAHQVCRDMELVIKDTLNAGFVTKNEVAAILQ KKGIYPVGKKMDRVHTKTLEKELDKHPLINEAQCYKTPNGKICVEVTQRVPILHIMSSNG ENYYLDNKGKMMPPDAKCVAHRAIVTGNVEKSFAMKDLYKFGVFLQNNPFWEAQIVQINV LPGKEIELVPRVGNHIIYLGKLEHFEDKLKRLKTFYEKGLNQVGWNKYSRISLEFGNQII CTKKKQ
Sequence length 246 AA
Subcellular LocationInner membrane
Function It is similar to FtsQ of E. coli and may be involved in cell division. Its orthologue in B. thetaiotaomicron is encoded by a candidate essential gene.
Glycosylation Status
Glycosylation Type O- (Thr) linked
Experimentally Validated Glycosite(s) in Full Length ProteinT44
Experimentally Validated Glycosite(s ) in Mature ProteinT44
Glycosite(s) Annotated Protein Sequence >tr|Q5LIJ9|Q5LIJ9_BACFN Putative cell division protein OS=Bacteroides fragilis (strain ATCC 25285 / NCTC 9343) GN=ftsQ PE=4 SV=1 MIKRILLTIVMLLLIAYLIAAVTVFNDKPAHQVCRDMELVIKDT*(44)LNAGFVTKNEVAAILQ KKGIYPVGKKMDRVHTKTLEKELDKHPLINEAQCYKTPNGKICVEVTQRVPILHIMSSNG ENYYLDNKGKMMPPDAKCVAHRAIVTGNVEKSFAMKDLYKFGVFLQNNPFWEAQIVQINV LPGKEIELVPRVGNHIIYLGKLEHFEDKLKRLKTFYEKGLNQVGWNKYSRISLEFGNQII CTKKKQ
Sequence Around Glycosites (21 AA) CRDMELVIKDTLNAGFVTKNE
Glycosite Sequence Logo
Technique(s) used for Glycosylation DetectionMass shift detected on 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 NamePutative fucosyl transferase
Predicted Accessory Gene(s)BF4298-4306 region lfg (locus of fragilis glycosylation).
Additional CommentGlycosylation 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 Identification2011
Year of Identification Month Wise2011.2.4
Year of Validation 2011
ReferenceFletcher, C.M., Coyne, M.J. and Comstock, L.E. (201Theoretical and experimental characterization of the scope of protein O-glycosylation in Bacteroides fragilis. J Biol Chem, 286, 3219-3226. [PubMed: 21115495]
Author Fletcher, C.M., Coyne, M.J. and Comstock, L.E.
Research GroupChanning Laboratory, Brigham and Womens Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA.
Corresponding Author Comstock, L.E.
ContactChanning Laboratory, Brigham and Womens Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA.