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ProGlyProt ID
BC123
Organism Information
Organism Name
Campylobacter jejuni 11168
Domain
Bacteria
Classification
Family: Campylobacteraceae
Order: Campylobacterales
Class: Epsilonproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI)
 
 
Genome Sequence(s)
GenBank
EMBL
Organism Additional Information
Campylobacter jejuni is a microaerophilic, Gram-negative, human pathogen that is the major cause of bacterial food-borne diarrhoea (gastroenteritis). It is most frequently responsible for a form of post-infection neuromuscular paralysis known as Guillain Barre' syndrome. It also leads to an immunoproliferative small intestine disease that is a rare malignant lymphoma of the intestine. Motility is essential for pathogenicity.
 
 
Gene Information
Gene Name
flaA (Cj1339c)
NCBI Gene ID
GenBank Gene Sequence
 
 
Protein Information
Protein Name
Flagellin A (FlaA)
UniProtKB/SwissProt ID
NCBI RefSeq
EMBL-CDS
UniProtKB Sequence
Sequence length
572 AA
Subcellular Location
Surface
Function
It is the subunit protein forming the flagellar filaments. Implicated in TLR-5-mediated interaction with the innate immune system.
 
 
Protein Structure
Homology Model
Homology Model File
 
 
Glycosylation Status
Glycosylation Type
O (Ser/Thr) linked
Experimentally Validated Glycosite(s) in Full Length Protein
S181, S207, and either T464 or T465 or both.
Experimentally Validated Glycosite(s ) in Mature Protein
S181, S207, and either T464 or T465 or both.
Glycosite(s) Annotated Protein Sequence
>sp|P56963|FLA1_CAMJE Flagellin A OS=Campylobacter jejuni GN=flaA PE=3 SV=2 MGF
RINTNVAALNAKANADLNSKSLDASLSRLSSGLRINSAADDASGMAIADSLRSQANT LGQAISNGNDALGILQT
ADKAMDEQLKILDTIKTKATQAAQDGQSLKTRTMLQADINRLM EELDNIANTTSFNGKQLLSGNFINQEFQIGA
SSNQTVKATIGATQSSKIGLTRFETGGRI S*(181)TSGEVQFTLKNYNGIDDFQFQKVVIS*(207)TS
VGTGLGALADEINKNADKTGVRATFTVETRG IAAVRAGATSDTFAINGVKIGKVDYKDGDANGALVAAINSVKD
TTGVEASIDANGQLLLT SREGRGIKIDGNIGGGAFINADMKENYGRLSLVKNDGKDILISGSNLSSAGFGATQF
ISQ ASVSLRESKGQIDANIADAMGFGSANKGVVLGGYSSVSAYMSSAGSGFSSGSGYSVGSGK NYSTGFANA
IAISAASQLSTVYNVSAGSGFSSGSTLSQFATMKT*(464)T*(465)AFGVKDETAGVTTLK GAMAVMDIA
ETAITNLDQIRADIGSVQNQVTSTINNITVTQVNVKAAESQIRDVDFAAES ANYSKANILAQSGSYAMAQANSV
QQNVLRLLQ
Sequence Around Glycosites (21 AA)
LTRFETGGRISTSGEVQFTLK
DDFQFQKVVISTSVGTGLGAL
STLSQFATMKTTAFGVKDETA
TLSQFATMKTTAFGVKDETAG
Glycosite Sequence Logo
Glycosite Sequence Logo
Technique(s) used for Glycosylation Detection
ESMS (electrospray mass spectrometry) giving broad heterogeneous molecular mass envelopes with a few discrete glycoform peaks
Technique(s) used for Glycosylated Residue(s) Detection
Liquid chromatography electron capture dissociation (ECD) tandem mass spectrometry (MS/MS). Also β-elimination reactions.
Protein Glycosylation- Implication
Glycosylation is required for flagellar filament assembly.
 
 
Glycan Information
Glycan Annotation
Two novel glycans - dimethylglyceric acid derivatives of pseudaminic acid (Pse5Ac7Ac) and 7-acetamidino pseudaminic acid are found. Ser181 and Ser207 were glycosylated by both glycans. Thr464 or Thr465 (or both, but exclusively) have been shown to be glycosylated by first glycan. Pse5Ac7Ac is also written as Pse5NAc7NAc (Pse).
BCSDB ID
Technique(s) used for Glycan Identification
MS/MS (tandem mass spectrometry), precursor ion scanning, and 1H, 13C NMR spectroscopy- HMBC (heteronuclear multiple bond correlation), COSY (correlation spectroscopy)
 
 
Protein Glycosylation linked (PGL) gene(s)
Characterized Accessory Gene(s)
Information currently not available with us.
PGL Additional Links
 
 
Literature
Reference(s)
1) Zampronio, C.G., Blackwell, G., Penn, C.W. and Cooper, H.J. (2011) Novel Glycosylation Sites Localized in Campylobacter jejuni Flagellin FlaA by Liquid Chromatography Electron Capture Dissociation Tandem Mass Spectrometry. J Proteome Res, 10, 1238-1245. [PubMed: 21158479]
2) Maita, N., Nyirenda, J., Igura, M., Kamishikiryo, J. and Kohda, D. (2010) Comparative structural biology of eubacterial and archaeal oligosaccharyltransferases. J Biol Chem, 285, 4941-4950. [PubMed: 20007322]
3) Logan, S.M., Hui, J.P., Vinogradov, E., Aubry, A.J., Melanson, J.E., Kelly, J.F., Nothaft, H. and Soo, E.C. (2009) Identification of novel carbohydrate modifications on Campylobacter jejuni 11168 flagellin using metabolomics-based approaches. FEBS J, 276, 1014-1023. [PubMed: 19154343]
4) Thibault, P., Logan, S.M., Kelly, J.F., Brisson, J.R., Ewing, C.P., Trust, T.J. and Guerry, P. (2001) Identification of the carbohydrate moieties and glycosylation motifs in Campylobacter jejuni flagellin. J Biol Chem, 276, 34862-34870. [PubMed: 11461915]
5) Linton, D., Karlyshev, A.V., Hitchen, P.G., Morris, H.R., Dell, A., Gregson, N.A. and Wren, B.W. (2000) Multiple N-acetyl neuraminic acid synthetase (neuB) genes in Campylobacter jejuni: identification and characterization of the gene involved in sialylation of lipo-oligosaccharide. Mol Microbiol, 35, 1120-1134. [PubMed: 10712693]
Additional Comments
Sequon feature: Both S181 and S207 are located within the motif IS*TS pointing towards a probable consensus glycosylation sequence in FlaA.
Some enzymes (e.g., neuB2 gene product) have been implicated in the post translational modification of the flagellin protein (Ref. no. 5).
Year of Identification
2001
Year of Validation
2011
 
 
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