ProGP205 (Flagellin A (FlaA))

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ProGP ID ProGP205 (Flagellin A (FlaA))
Validation Status Characterized
Organism Information
Organism NameCampylobacter jejuni 11168
Domain Bacteria
Classification Phylum : Proteobacteria
Class : Epsiolonproteobacteria
Orders : Campylobacterales
Family : Campylobacteraceae
Genus : Campylobacter
Species : jejuni
Subspecies : jejuni
Strain : 1168
Taxonomic ID (NCBI) 192222
Genome Information
GenBank AL111168.1
EMBL AL111168
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 NameflaA (Cj1339c)
NCBI Gene ID 905631
GenBank Gene Sequence NC_002163.1
Protein Information
Protein NameFlagellin A (FlaA)
UniProtKB/SwissProt ID P56963
NCBI RefSeq YP_002344727.1
EMBL-CDSCAL35451.1
UniProtKB Sequence >sp|P56963|FLA1_CAMJE Flagellin A OS=Campylobacter jejuni GN=flaA PE=3 SV=2 MGFRINTNVAALNAKANADLNSKSLDASLSRLSSGLRINSAADDASGMAIADSLRSQANT LGQAISNGNDALGILQTADKAMDEQLKILDTIKTKATQAAQDGQSLKTRTMLQADINRLM EELDNIANTTSFNGKQLLSGNFINQEFQIGASSNQTVKATIGATQSSKIGLTRFETGGRI STSGEVQFTLKNYNGIDDFQFQKVVISTSVGTGLGALADEINKNADKTGVRATFTVETRG IAAVRAGATSDTFAINGVKIGKVDYKDGDANGALVAAINSVKDTTGVEASIDANGQLLLT SREGRGIKIDGNIGGGAFINADMKENYGRLSLVKNDGKDILISGSNLSSAGFGATQFISQ ASVSLRESKGQIDANIADAMGFGSANKGVVLGGYSSVSAYMSSAGSGFSSGSGYSVGSGK NYSTGFANAIAISAASQLSTVYNVSAGSGFSSGSTLSQFATMKTTAFGVKDETAGVTTLK GAMAVMDIAETAITNLDQIRADIGSVQNQVTSTINNITVTQVNVKAAESQIRDVDFAAES ANYSKANILAQSGSYAMAQANSVQQNVLRLLQ
Sequence length 572 AA
Subcellular LocationSurface
Function It is the subunit protein forming the flagellar filaments. Implicated in TLR-5-mediated interaction with the innate immune system.
Glycosylation Status
Glycosylation Type O- (Ser/Thr) linked
Experimentally Validated Glycosite(s) in Full Length ProteinS181, S207, and either T464 or T465 or both.
Experimentally Validated Glycosite(s ) in Mature ProteinS181, 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 MGFRINTNVAALNAKANADLNSKSLDASLSRLSSGLRINSAADDASGMAIADSLRSQANT LGQAISNGNDALGILQTADKAMDEQLKILDTIKTKATQAAQDGQSLKTRTMLQADINRLM EELDNIANTTSFNGKQLLSGNFINQEFQIGASSNQTVKATIGATQSSKIGLTRFETGGRI S*(181)TSGEVQFTLKNYNGIDDFQFQKVVIS*(207)TSVGTGLGALADEINKNADKTGVRATFTVETRG IAAVRAGATSDTFAINGVKIGKVDYKDGDANGALVAAINSVKDTTGVEASIDANGQLLLT SREGRGIKIDGNIGGGAFINADMKENYGRLSLVKNDGKDILISGSNLSSAGFGATQFISQ ASVSLRESKGQIDANIADAMGFGSANKGVVLGGYSSVSAYMSSAGSGFSSGSGYSVGSGK NYSTGFANAIAISAASQLSTVYNVSAGSGFSSGSTLSQFATMKT*(464)T*(465)AFGVKDETAGVTTLK GAMAVMDIAETAITNLDQIRADIGSVQNQVTSTINNITVTQVNVKAAESQIRDVDFAAES ANYSKANILAQSGSYAMAQANSVQQNVLRLLQ
Sequence Around Glycosites (21 AA) LTRFETGGRISTSGEVQFTLK
DDFQFQKVVISTSVGTGLGAL
STLSQFATMKTTAFGVKDETA
TLSQFATMKTTAFGVKDETAG
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Technique(s) used for Glycosylation DetectionESMS (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 23773 24087
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.
Additional CommentSequon 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. 4).
Literature
Year of Identification2001
Year of Identification Month Wise2001.9.14
Year of Validation 2011
ReferenceZampronio, 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. Journal of proteome research, 10(3), pp.1238-1245.
Corresponding Author Helen J. Cooper
ContactSchool of Biosciences, College of Life and Environmental Sciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, U.K.
ReferenceMaita, N., Nyirenda, J., Igura, M., Kamishikiryo, J. and Kohda, D., 2010. Comparative Structural Biology of Eubacterial and Archaeal Oligosaccharyltransferases 2. Journal of Biological Chemistry, 285(7), pp.4941-4950.
Corresponding Author Daisuke Kohda
ContactDivision of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Maidashi 3-1-1, Higashi-ku, Fukuoka 812-8582, Japan.
ReferenceLogan, 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. The FEBS Journal, 276(4), pp.1014-1023.
Corresponding Author Evelyn C. Soo
ContactNRC-Institute for Biological Sciences, Ottawa, Canada.
ReferenceThibault, P., Logan, S.M., Kelly, J.F., Brisson, J.R., Ewing, C.P. and Guerry, P., 2001. Identification of the carbohydrate moieties and glycosylation motifs in Campylobacter jejuni flagellin. Journal of Biological Chemistry, 276(37), pp.34862-34870.
Corresponding Author Susan M Logan
ContactInstitute for Biological Sciences, National Research Council of Canada, Ottawa, Ontario K1A 0R6, Canada.
ReferenceLinton, 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. Molecular microbiology, 35(5), pp.1120-1134.
Corresponding Author Brendan W. Wren
ContactDepartment of Infectious and Tropical Diseases,London School of Hygiene and Tropical Medicine, LondonWC1E 7HT, UK