ProGP313

Home -> ProGPdb -> Search ProGP -> Display data

ProGP ID ProGP313
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 NameBF0994
NCBI Gene ID 3287312
GenBank Gene Sequence 3287312
Protein Information
Protein NameHypothetical protein
UniProtKB/SwissProt ID Q5LGK6
NCBI RefSeq YP_210682.1
EMBL-CDSCAH06733.1
UniProtKB Sequence >tr|Q5LGK6|Q5LGK6_BACFN Putative uncharacterized protein OS=Bacteroides fragilis (strain ATCC 25285 / NCTC 9343) GN=BF0994 PE=4 SV=1 MATLQNIRSKGPLLVIVIGLALFAFIAGDAWKVLQPHQSHDVGEVNGETLSAQDYQNMVE EYTEVIKFSSGMSSLNDEQTNQVKDEVWRSYVNNKLIEKEAKKLGITVSKAEIQSIINEG VNPLLQQTPFRNPQTGAFDKDMLKKFLADYSKMDKTKMPSQYVEYYEGMHKLWSFVEKTL IQSRLAEKYQALVTKALFSNPVEAQDAFDARVNQSDVLLAAVPYSSIVDSTITVKESELK DLYNKKKEQFKQYVETRNIKYIDVQVIASAEDRAAIQQEVTDYTNQLATANGDYTTFIRS TGSEYPYVDLYYTKKAFPSDVVARMDSASIGQVYGPYYNAGDNTINSFKVLSKVAAADSV QFRQIQVYTEDAAKTKALADSIYTAIKGGADFTALAKKYGQTGESNWISSANYENAQVDG DNLKFISTINNLGVNELSNVALGQGNIILQVTDKKAVKDKYKVAVIKRAVEFSKETYNKA YNEFSQFIAANPTVDKVAANAEESGYKLLERNDLYSSEHGIGGIRGTKEALKWAFAAKPG EVSGLYECGESDRMLVVGLVSVIEEGYRPLAQVQDQLRAEIIRDKKAEKIMADMKAANAT TIAQYTSMANAVSDSVKHVTFAAPAYVAALRSSEPLVGAYASVSDINKLSAPIKGNGGVF VLQVYAKDKLNETFDAQSEEATLENMHARLASRFMNDLYLKGDVKDKRYLFF
Sequence length 712 AA
Subcellular LocationPeriplasm
Function Predicted to function as a proline cis-trans isomerase (parvulin family) involved in a chaperone system.
Glycosylation Status
Glycosylation Type O (Ser) linked
Experimentally Validated Glycosite(s) in Full Length ProteinS230, S327, S615
Experimentally Validated Glycosite(s ) in Mature ProteinS230, S327, S615
Glycosite(s) Annotated Protein Sequence >tr|Q5LGK6|Q5LGK6_BACFN Putative uncharacterized protein OS=Bacteroides fragilis (strain ATCC 25285 / NCTC 9343) GN=BF0994 PE=4 SV=1 MATLQNIRSKGPLLVIVIGLALFAFIAGDAWKVLQPHQSHDVGEVNGETLSAQDYQNMVE EYTEVIKFSSGMSSLNDEQTNQVKDEVWRSYVNNKLIEKEAKKLGITVSKAEIQSIINEG VNPLLQQTPFRNPQTGAFDKDMLKKFLADYSKMDKTKMPSQYVEYYEGMHKLWSFVEKTL IQSRLAEKYQALVTKALFSNPVEAQDAFDARVNQSDVLLAAVPYSSIVDS*(230)TITVKESELK DLYNKKKEQFKQYVETRNIKYIDVQVIASAEDRAAIQQEVTDYTNQLATANGDYTTFIRS TGSEYPYVDLYYTKKAFPSDVVARMDS*(327)ASIGQVYGPYYNAGDNTINSFKVLSKVAAADSV QFRQIQVYTEDAAKTKALADSIYTAIKGGADFTALAKKYGQTGESNWISSANYENAQVDG DNLKFISTINNLGVNELSNVALGQGNIILQVTDKKAVKDKYKVAVIKRAVEFSKETYNKA YNEFSQFIAANPTVDKVAANAEESGYKLLERNDLYSSEHGIGGIRGTKEALKWAFAAKPG EVSGLYECGESDRMLVVGLVSVIEEGYRPLAQVQDQLRAEIIRDKKAEKIMADMKAANAT TIAQYTSMANAVSDS*(615)VKHVTFAAPAYVAALRSSEPLVGAYASVSDINKLSAPIKGNGGVF VLQVYAKDKLNETFDAQSEEATLENMHARLASRFMNDLYLKGDVKDKRYLFF
Sequence Around Glycosites (21 AA) AAVPYSSIVDSTITVKESELK
FPSDVVARMDSASIGQVYGPY
YTSMANAVSDSVKHVTFAAPA
Glycosite Sequence Logo
Technique(s) used for Glycosylation DetectionMass 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 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 Identification2009
Year of Identification Month Wise2009.4.17
Year of Validation 2011
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, 321-331. [PubMed: 19379697]
Author Fletcher, C.M., Coyne, M.J., Villa, O.F., Chatzidaki-Livanis, M. Comstock, L.E.
Research GroupChanning Laboratory, Brigham & Women's Hospital, Harvard Medical School, 181 Longwood Avenue, Boston, MA 02115, USA.
Corresponding Author Comstock, L.E.
ContactChanning Laboratory, Brigham & Women's Hospital, Harvard Medical School, 181 Longwood Avenue, Boston, MA 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, 321-331. [PubMed: 19379697]
Author Fletcher, C.M., Coyne, M.J., Villa, O.F., Chatzidaki-Livanis, M. and Comstock, L.E.
Research GroupChanning Laboratory, Brigham & Women's Hospital, Harvard Medical School, 181 Longwood Avenue, Boston, MA 02115, USA.
Corresponding Author Comstock, L.E.
ContactChanning Laboratory, Brigham & Women's Hospital, Harvard Medical School, 181 Longwood Avenue, Boston, MA 02115, USA.
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.