ProGP683 (Flagellin)

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ProGP ID ProGP683 (Flagellin)
Validation Status Characterized
Organism Information
Organism NameSelenomonas sputigena
Domain Bacteria
Classification Family: Selenomonadaceae
Order: Selenomonadales
Class: Negativicutes
Phylum: Firmicutes
Taxonomic ID (NCBI) 546271
Genome Information
GenBank CP002637
EMBL CP002637
Gene Information
Gene NameSelsp_0329
GenBank Gene Sequence NZ_GG698598.1
Protein Information
Protein NameFlagellin
UniProtKB/SwissProt ID C9LY14
NCBI RefSeq WP_006193737.1
EMBL-CDSAEB99302.1
UniProtKB Sequence >tr|C9LY14|C9LY14_SELS3 Flagellin OS=Selenomonas sputigena (strain ATCC 35185 / DSM 20758 / VPI D19B-28) OX=546271 GN=Selsp_0329 PE=3 SV=1 MALVVKNNMMAVNTLNTLNKNQSALSTSLKQVSSGMKINGAVDDASGYAISERMRVQIRS LDQDNQNTQNGNSMMKVAEGAVSSTVDILKTLKEKVINAANDTNTDDDRLTIQKELNQSI DQINDNANITFNGKYLVDGTHNQKVTATTTTFTNQSMSTATVATSAMTGLLDRTGRNLNI HSQDTITVSYVNQGKTETTSFKVSTQTFSEVIKRLSGTGIVGGMATDVGATSVIGTNVAG DTVYTASGESAISLYAAGTGVGKSVGGITFSITDTQGNINKSANAVLDAFSETVRAQDNS QDNSMNFQIGTRANQAIRVGMTDMRAQALGLQGSDGSTLNISTRDKANAAINVLDNAISK ALDQQTTIGAVQSRLNYTSQNLTTASENVQASESTIRDADMAKAMTNYTKNNVLMQAAQA MLAQANQSSSGVLSLLQ
Sequence length 437 AA
Subcellular LocationFlagellum
Function Flagellin is the subunit of bacterial flagella
Glycosylation Status
Glycosylation Type O- (Ser/Thr) linked
Experimentally Validated Glycosite(s) in Full Length ProteinT149, S182, T199, T259, and S334
Glycosite(s) Annotated Protein Sequence >tr|C9LY14|C9LY14_SELS3 Flagellin OS=Selenomonas sputigena (strain ATCC 35185 / DSM 20758 / VPI D19B-28) OX=546271 GN=Selsp_0329 PE=3 SV=1 MALVVKNNMMAVNTLNTLNKNQSALSTSLKQVSSGMKINGAVDDASGYAISERMRVQIRSLDQDNQNTQNGNSMMKVAEGAVSSTVDILKTLKEKVINAANDTNTDDDRLTIQKELNQSIDQINDNANITFNGKYLVDGTHNQKVTATT*(149)TTFTNQSMSTATVATSAMTGLLDRTGRNLNIHS*(182) QDTITVSYVNQGKTETT*(199)SFKVSTQTFSEVIKRLSGTGIVGGMATDVGATSVIGTNVAGDTVYTASGESAISLYAAGT*(259)GVGKSVGGITFSITDTQGNINKSANAVLDAFSETVRAQDNSQDNSMNFQIGTRANQAIRVGMTDMRAQALGLQGS*(334)DGSTLNISTRDKANAAINVLDNAISKALDQQTTIGAVQSRLNYTSQNLTTASENVQASESTIRDADMAKAMTNYTKNNVLMQAAQAMLAQANQSSSGVLSLLQ
Sequence Around Glycosites (21 AA) GTHNQKVTATT*TTFTNQSMST
DRTGRNLNIHS*QDTITVSYVN
SYVNQGKTETT*SFKVSTQTFS
ESAISLYAAGT*GVGKSVGGIT
MRAQALGLQGS*DGSTLNISTR
Technique(s) used for Glycosylation DetectionWestern-Immunoblotting, and Monosaccharide Analysis by Reversed Phase (RP)-HPLC
Technique(s) used for Glycosylated Residue(s) Detection nanoLC-ESI-MSMS.
Protein Glycosylation- Implication The O-glycans present in the proteins’ N-terminal region' of Flagellin protein could potentially affect recognition of flagellin monomers by TLR5 (an innate immune receptor Toll-like receptor 5).
Glycan Information
Glycan Annotation Six different O-glycans in the range from tri- to pentasaccharides that consisted mostly of deoxyhexose (dHex) and N-acetylhexosamine (HexNAc) residues. Monosaccharide analyses identified these sugars as rhamnose (Rha) and GlcNAc. The GlcNAc residue in the Rha3GlcNAc tetrasaccharide identify in its reduced state, indicates that the glycan which is attached to the protein is GlcNAc.
Literature
Year of Identification2018
Year of Validation 2018
ReferenceRath CB, Schirmeister F, Figl R, Seeberger PH, Schäffer C and Kolarich D (2018) Flagellin Glycoproteomics of the Periodontitis Associated Pathogen Selenomonas sputigena Reveals Previously Not Described O-glycans and Rhamnose Fragment Rearrangement Occurring on the Glycopeptides. Mol Cell Proteomics, 17(4):721-736. [PubMed: 29339411]
AuthorRath CB, Schirmeister F, Figl R, Seeberger PH, Schäffer C and Kolarich D
Research Group1 Department of NanoBiotechnology, NanoGlycobiology unit, University of Natural Resources and Life Sciences Vienna, 1190 Vienna, Austria. 2 Department of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, 14424 Potsdam, Germany. 3 Department of Biology, Chemistry, Pharmacy, Institute of Chemistry and Biochemistry, Freie Universität Berlin, 14195 Berlin, Germany. 4 Department of Chemistry, Division of Biochemistry, Universität für Bodenkultur Wien, 1190 Vienna, Austria. 5 From the Department of NanoBiotechnology, NanoGlycobiology unit, Universität für Bodenkultur Wien, 1190 Vienna, Austria. 6 Department of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, 14424 Potsdam, Germany. 7 Institute for Glycomics, Gold Coast Campus, Griffith University, Queensland, 4222, Australia.
Corresponding Author Kolarich D
ContactDepartment of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, 14424 Potsdam, Germany