ProGP298 (FliC (Flagellin subunit))

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ProGP ID ProGP298 (FliC (Flagellin subunit))
Validation Status Characterized
Organism Information
Organism NameClostridium difficile strain 630
Domain Bacteria
Classification Phylum : Firmicutes
Class : Clostridia
Orders : Eubacteriales
Family : Peptostreptococcaceae
Genus : Clostridium
Species : difficile
Strain : strain 630
Taxonomic ID (NCBI) 272563
Genome Information
GenBank AM180355.1
EMBL AM180355
Organism Additional Information Clostridium difficile is a gram-positive, anaerobic, spore-forming bacterium that produces TcdA and TcdB toxins causing severe tissue damage. It ia an opportunistic pathogen that is the major cause of antibiotic-associated diarrhoea and pseudomembranous colitis in humans. C. dificile infection can also result in abdominal pain, inflammation, and ulceration of the lining of the intestinal wall.
Gene Information
Gene NamefliC (CD0239)
NCBI Gene ID 4916757
GenBank Gene Sequence NC_009089.1
Protein Information
Protein NameFliC (Flagellin subunit)
UniProtKB/SwissProt ID Q18CX7
NCBI RefSeq WP_011860690.1
EMBL-CDSCAJ67060.1
UniProtKB Sequence >tr|Q18CX7|Q18CX7_CLOD6 Flagellin subunit OS=Clostridium difficile (strain 630) GN=fliC PE=4 SV=1 MRVNTNVSALIANNQMGRNVNGQSKSMEKLSSGVRIKRAADDAAGLAISEKMRAQIKGLD QAGRNVQDGISVVQTAEGSLEETGNILQRMRTLSLQSANEINNTEEREKIADELTQLKDE IERISSSTEFNGKKLLDGTSSTIRLQVGASYGTNVSGTSNNNNEIKIQLVNTASIMASAG ITTASIGSMKAGGTTGTDAAKTMVSSLDAALKSLNSSRAKLGAQQNRLESTQNNLNNTLE NVTAAESRIRDTDVASEMVNLSKMNILVQASQSMLAQANQQPQGVLQLLG
Sequence length 290 AA
Subcellular LocationSurface
Function Forms the filaments of bacterial flagella.
Glycosylation Status
Glycosylation Type O- (Ser/Thr) linked
Experimentally Validated Glycosite(s) in Full Length ProteinS141, S174, T183, S188, S205
Experimentally Validated Glycosite(s ) in Mature ProteinS141, S174, T183, S188, S205
Glycosite(s) Annotated Protein Sequence >tr|Q18CX7|Q18CX7_CLOD6 Flagellin subunit OS=Clostridium difficile (strain 630) GN=fliC PE=4 SV=1 MRVNTNVSALIANNQMGRNVNGQSKSMEKLSSGVRIKRAADDAAGLAISEKMRAQIKGLD QAGRNVQDGISVVQTAEGSLEETGNILQRMRTLSLQSANEINNTEEREKIADELTQLKDE IERISSSTEFNGKKLLDGTSS*(141)TIRLQVGASYGTNVSGTSNNNNEIKIQLVNTAS*(174) IMASAG ITT*(183)ASIGS*(188)MKAGGTTGTDAAKTMVS*(205)SLDAALKSLNSSRAKLGAQQNRLESTQNNLNNTLE NVTAAESRIRDTDVASEMVNLSKMNILVQASQSMLAQANQQPQGVLQLLG
Sequence Around Glycosites (21 AA) NGKKLLDGTSSTIRLQVGASY
EIKIQLVNTASIMASAGITTA
ASIMASAGITTASIGSMKAGG
SAGITTASIGSMKAGGTTGTD
TGTDAAKTMVSSLDAALKSLN
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Technique(s) used for Glycosylation DetectionIntact mass analysis with QTOF2-MS (hybrid quadrupole time of flight mass spectrometry)
Technique(s) used for Glycosylated Residue(s) Detection Electron transfer dissociation (ETD) MS
Protein Glycosylation- Implication Glycosylation of the flagellin protein is required for proper assembly and consequent motility.
Glycan Information
Glycan Annotation (398-Da glycan) O-linked HexNAc residue, to which a methylated aspartic acid is linked via a phosphate bond. Flagellins from a number of C. difficile isolates from more recent outbreaks are modified in O linkage with a heterogeneous glycan containing up to five monosaccharide residues with masses of 204 (HexNAc), 146 (deoxyhexose), 160 (methylated deoxyhexose), and 192 (heptose). HexNAc is GlcNAc.
Technique(s) used for Glycan Identification MS/MS (tandem mass spectrometry), nESI-feCID-MS/MS (nano-electrospray ionization-front-end collision-induced dissociation MS/MS) analyses
Protein Glycosylation linked (PGL) gene(s)
OST ProGT IDProGT32
Characterized Accessory Gene(s)CD0240 glycosyltransferase. Its insertional mutagenesis abolished the flagellar filament production at the cell surface.
Literature
Year of Identification2009
Year of Identification Month Wise2009.3.17
Year of Validation 2009
ReferenceTwine, S.M., Reid, C.W., Aubry, A., McMullin, D.R., Fulton, K.M., Austin, J. and Logan, S.M., 2009. Motility and flagellar glycosylation in Clostridium difficile. Journal of bacteriology, 191(22), pp.7050-7062.
Corresponding Author Susan M. Logan
ContactNRC-Institute for Biological Sciences, Ottawa, Canada.
ReferenceHensbergen, P.J., de Ru, A.H., Friggen, A.H., Corver, J., Smits, W.K. and van Veelen, P.A., 2022. New insights into the type A glycan modification of Clostridioides difficile flagellar protein flagellin C by phosphoproteomics analysis. Journal of Biological Chemistry, 298(3).
Corresponding Author Paul J. Hensbergen
ContactCenter for Proteomics and Metabolomics, and 2Department of Medical Microbiology, Leiden University Medical Center, Leiden, The Netherlands