ProGP357

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ProGP ID ProGP357
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 NameBF3195
NCBI Gene ID 3286585
GenBank Gene Sequence 3286585
Protein Information
Protein NamePutative exported protein
UniProtKB/SwissProt ID Q5LAI3
NCBI RefSeq YP_212808.1
EMBL-CDSCAH08890.1
UniProtKB Sequence >tr|Q5LAI3|Q5LAI3_BACFN Putative exported protein OS=Bacteroides fragilis (strain ATCC 25285 / NCTC 9343) GN=BF3195 PE=4 SV=1 MKKTILLAALGLISLSALAQDKPQEEGFVFTTVKENPITSIKNQNRSSTCWSFSSLGFLE SELLRTGKGEYDLSEMFVVHHTMVDRAVNYVRYHGDSSFSPGGSFYDIMFCMKNYGLVPQ DAMPGIMYGDSLPVHNELDATAGAYVNAIAKGNLKKLTPVWKKGLCAIYDTYLGQCPEKF TYKGKEYTPMTFAQSLGLNPDDYVSLTSYTHHPFYSQFAIEIQDNWRNGLSYNLPLDEFM AVMDNAVKNGYTFAWGSDVSEEGFTRDGIAVVPDAAKGAELTGSDMARWTGMTAADKRKE LTSKPLPEMKITQEMRQTAFDNWETTDDHGMIIYGIAKDQNGKEYFMVKNSWGTNNKYKG TWYASKAFVAYKTMNILVHKDALPKDIAKKLGIK
Sequence length 394 AA
Subcellular LocationPeriplasm
Function Putative aminopeptidase.
Glycosylation Status
Glycosylation Type O (Ser) linked
Experimentally Validated Glycosite(s) in Full Length ProteinS131
Experimentally Validated Glycosite(s ) in Mature ProteinS131
Glycosite(s) Annotated Protein Sequence >tr|Q5LAI3|Q5LAI3_BACFN Putative exported protein OS=Bacteroides fragilis (strain ATCC 25285 / NCTC 9343) GN=BF3195 PE=4 SV=1 MKKTILLAALGLISLSALAQDKPQEEGFVFTTVKENPITSIKNQNRSSTCWSFSSLGFLE SELLRTGKGEYDLSEMFVVHHTMVDRAVNYVRYHGDSSFSPGGSFYDIMFCMKNYGLVPQ DAMPGIMYGDS*(131)LPVHNELDATAGAYVNAIAKGNLKKLTPVWKKGLCAIYDTYLGQCPEKF TYKGKEYTPMTFAQSLGLNPDDYVSLTSYTHHPFYSQFAIEIQDNWRNGLSYNLPLDEFM AVMDNAVKNGYTFAWGSDVSEEGFTRDGIAVVPDAAKGAELTGSDMARWTGMTAADKRKE LTSKPLPEMKITQEMRQTAFDNWETTDDHGMIIYGIAKDQNGKEYFMVKNSWGTNNKYKG TWYASKAFVAYKTMNILVHKDALPKDIAKKLGIK
Sequence Around Glycosites (21 AA) DAMPGIMYGDSLPVHNELDAT
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).
Literature
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.
Year of Identification2011
Year of Identification Month Wise2011.2.4
Year of Validation 2011
Reference1) 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. J Biol Chem, 286, 3219-3226. [PubMed: 21115495]
Author Fletcher, C.M., Coyne, M.J. and Comstock, L.E.
Research GroupChanning Laboratory, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA.
Corresponding Author Comstock, L.E.
ContactChanning Laboratory, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA.