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ProGlyProt ID
BC112
Organism Information
Organism Name
Bacteroides fragilis (strain ATCC 25285 / NCTC 9343)
Domain
Bacteria
Classification
Family: Bacteroidaceae
Order: "Bacteroidales"
Class: "Bacteroidia"
Division or phylum: "Bacteroidetes"
Taxonomic ID (NCBI)
 
 
Genome Sequence(s)
GenBank
EMBL
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
BF2334
NCBI Gene ID
GenBank Gene Sequence
 
 
Protein Information
Protein Name
Putative exported protein
UniProtKB/SwissProt ID
NCBI RefSeq
EMBL-CDS
UniProtKB Sequence
Sequence length
245 AA
Subcellular Location
Periplasm
Function
Contains tetratricopeptide repeat (TPR) domains that mediate protein-protein interactions. It is suggested to be involved in the response to oxidative stress as it was found upregulated 3.9-fold on exposure of B. fragilis to air.
 
 
Protein Structure
Homology Model
Homology Model File
 
 
Glycosylation Status
Glycosylation Type
O (Ser) linked
Experimentally Validated Glycosite(s) in Full Length Protein
S59
Experimentally Validated Glycosite(s ) in Mature Protein
S59
Glycosite(s) Annotated Protein Sequence
>tr|Q5LCY3|Q5LCY3_BACFN Putative exported protein OS=Bacteroides fragilis (strai
n ATCC 25285 / NCTC 9343) GN=BF2334 PE=4 SV=1 MKKIILLLALCFTANNFFAQTTDPNQLKN
EGNDALNAKNYAVAFEKYSEYLKLTNNQDS*(59)V TAYNCGVCADNIKKYKEAADYFDIAIKKNYNLANAY
IGKSAAYRDMKNNQEYIATLTEGI KAVPGNATIEKLYAIYYLKEGQKFQQAGNIEKAEENYKHATDVTSKKWKT
DALYSLGVLF YNNGADVLRKATPLASSNKEKYASEKAKADAAFKKAVDYLGEAVTLSPNRTEIKQMQDQV KAMIK
Sequence Around Glycosites (21 AA)
EYLKLTNNQDSVTAYNCGVCA
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
wcfB
OST NCBI Gene ID
OST GenBank Gene Sequence
OST Protein Name
Putative fucosyl transferase
OST UniProtKB/ SwissProt ID
OST NCBI RefSeq
OST EMBL-CDS
OST UniProtKB Sequence
OST Genome Context
Predicted Accessory Gene(s)
BF4298-4306 region lfg (locus of fragilis glycosylation).
PGL Additional Links
 
 
Literature
Reference(s)
1) 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]
2) 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, 321-331. [PubMed: 19379697]
Additional Comments
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.
Year of Identification
2009
Year of Validation
2011
 
 
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