ProGlyProt IDBC115
Organism Information
Organism NameCampylobacter coli VC 167
DomainBacteria
ClassificationFamily: Campylobacteraceae
Order: Campylobacterales
Class: Epsilonproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI)195
Genome Sequence (s)
EMBLM64670
Gene Information
Gene NameflaA
NCBI Gene ID
Protein Information
Protein NameFlagellin A
UniProtKB/SwissProt IDP27053
NCBI RefSeq
EMBL-CDSAAA23022.1
UniProtKB Sequence>sp|P27053|FLAA_CAMCO Flagellin A OS=Campylobacter coli GN=flaA PE=3 SV=3 MGFRINTNVAALNAKANSDLNSRALDQSLSRLSSGLRINSAADDASGMAIADSLRSQANT LGQAISNGNDALGILQTADKAMDEQLKILDTIKTKATQAAQDGQSLKTRTMLQADINRLM EELDNIANTTSFNGKQLLSGGFTNQEFQIGSSSNQTIKASIGATQSSKIGVTRFETGSQS FSSGTVGLTIKNYNGIEDFKFDSVVISTSVGTGLGALAEEINRNADKTGIRATFDVKSVG AYAIKAGNTSQDFAINGVVIGKVDYSDGDENGSLISAINAVKDTTGVQASKDENGKLVLT SADGRGIKITGSIGVGAGILHTENYGRLSLVKNDGRDINISGTGLSAIGMGATDMISQSS VSLRESKGQISAANADAMGFNAYNGGGAKQIIFASSIAGFMSQAGSGFSAGSGFSVGSGK NYSAILSASIQIVSSARSISSTYVVSTGSGFSAGSGNSQFAALRISTVSAHDETAGVTTL KGAMAVMDIAETAITNLDQIRADIGSVQNQITSTINNITVTQVNVKSAESQIRDVDFASE SANYSKANILAQSGSYAMAQANSSQQNVLRLLQ
Sequence length573 AA
Subcellular LocationSecreted
FunctionIt is the subunit protein which is polymerized into the flagellar filaments. Motility mediated by flagella is essential for virulence.
Protein Structure
PDB ID
Glycosylation Status
Glycosylation TypeO (Ser) linked
Experimentally Validated Glycosite(s) in Full Length Protein(Initiator Met removed) S207, S395, S396, S402, S409, S415, S423, S427, S434, S438, S440, S446, S452
Experimentally Validated Glycosite(s ) in Mature ProteinS206, S394, S395, S401, S408, S414, S422, S426, S433, S437, S439, S445, S451
Glycosite(s) Annotated Protein Sequence>sp|P27053|FLAA_CAMCO Flagellin A OS=Campylobacter coli GN=flaA PE=3 SV=3 MGFRINTNVAALNAKANSDLNSRALDQSLSRLSSGLRINSAADDASGMAIADSLRSQANT LGQAISNGNDALGILQTADKAMDEQLKILDTIKTKATQAAQDGQSLKTRTMLQADINRLM EELDNIANTTSFNGKQLLSGGFTNQEFQIGSSSNQTIKASIGATQSSKIGVTRFETGSQS FSSGTVGLTIKNYNGIEDFKFDSVVIS*(207)TSVGTGLGALAEEINRNADKTGIRATFDVKSVG AYAIKAGNTSQDFAINGVVIGKVDYSDGDENGSLISAINAVKDTTGVQASKDENGKLVLT SADGRGIKITGSIGVGAGILHTENYGRLSLVKNDGRDINISGTGLSAIGMGATDMISQSS VSLRESKGQISAANADAMGFNAYNGGGAKQIIFAS*(395)S*(396)IAGFMS*(402)QAGSGFS*(409)AGSGFS*(415)VGSGK NYS*(423)AILS*(427)ASIQIVS*(434)SARS*(438)IS*(440)STYVVS*(446)TGSGFS*(452)AGSGNSQFAALRISTVSAHDETAGVTTL KGAMAVMDIAETAITNLDQIRADIGSVQNQITSTINNITVTQVNVKSAESQIRDVDFASE SANYSKANILAQSGSYAMAQANSSQQNVLRLLQ
Sequence Around Glycosites (21 AA)EDFKFDSVVISTSVGTGLGAL
GGGAKQIIFASSIAGFMSQAG
GGAKQIIFASSIAGFMSQAGS
IFASSIAGFMSQAGSGFSAGS
GFMSQAGSGFSAGSGFSVGSG
GSGFSAGSGFSVGSGKNYSAI
GFSVGSGKNYSAILSASIQIV
GSGKNYSAILSASIQIVSSAR
AILSASIQIVSSARSISSTYV
ASIQIVSSARSISSTYVVSTG
IQIVSSARSISSTYVVSTGSG
ARSISSTYVVSTGSGFSAGSG
TYVVSTGSGFSAGSGNSQFAA
Glycosite Sequence Logoseqlogo
Glycosite Sequence Logo
Technique(s) used for Glycosylation DetectionBiotin-hydrazide labeling after periodate oxidation, sialic acid-specific lectin LFA (limax flavus agglutinin)-binding, mass excess (approx. 6 kDa) detected by intact mass analysis using ESMS (electrospray mass spectrometry)
Technique(s) used for Glycosylated Residue(s) DetectionEdman sequencing
Protein Glycosylation- ImplicationSone level of glycosylation is necessary for filament assembly. Modification with either Pse5Ac7Ac or PseAm is sufficient for filament assembly.Modification with pseudaminic acid and derivatives is essential for targeting and/or secretion of flagellin. Glycosylation may be required for interaction of the subunits with the flagellin chaperone, FliS, with other components of the flagellar structure or in subunit interactions.
Glycan Information
Glycan AnnotationMore Pse5Ac7Ac (5,7-diacetamido-3,5,7,9-tetradeoxy-L-glycero-L-manno-nonulosonic acid) in this case than from 81-176. Acetamidino and N-methylacetimidoyl derivatives of legionaminic acid, 315 Da Leg5Am7Ac (5-acetamidino-7-acetamido-3,5,7,9,-tetradeoxy-D-glycero-D-galacto-nonulosonic acid) and Leg5AmNMe7Ac (5-E/Z-N-(N-methylacetimidoyl)-7-acetamidino-3,5,7,9-tetradeoxy-D-glycero-D-galacto-nonulosonic), are also present. Leg5Ac7Ac (Leg) is legionaminic acid and Pse5Ac7Ac (Pse) is pseudaminic acid.
Technique(s) used for Glycan IdentificationHomo- and heteronuclear correlated two-dimensional 1H NMR, 13C HSQC (heteronuclear single quantum coherence), HMBC (heteronuclear multiple bond coherence), COSY (correlated spectroscopy), TOCSY (total correlation spectroscopy), and NOESY (nuclear Overhauser effect spectroscopy).
Protein Glycosylation linked (PGL) gene(s)
OST Gene Name
OST NCBI Gene ID
OST GenBank Gene Sequence
OST Protein Name
OST UniProtKB/ SwissProt ID
OST NCBI RefSeq
OST EMBL-CDS
OST UniProtKB Sequence
OST EC Number (BRENDA)
OST Genome Context
Characterized Accessory Gene(s)Products of ptmA-H genes are involved in the biosynthesis of Leg and Pse sugars that modify the flagellin.
PGL Additional LinksCAZy
Literatures
Reference(s)1) 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. [PMID: 19154343]
2) McNally, D.J., Aubry, A.J., Hui, J.P., Khieu, N.H., Whitfield, D., Ewing, C.P., Guerry, P., Brisson, J.R., Logan, S.M. and Soo, E.C. (2007) Targeted metabolomics analysis of Campylobacter coli VC167 reveal
Additional CommentsIt is the first report of legionaminic acid in Campylobacter sp. and the first report of legionaminic acid derivatives as modifications on a protein.
Sequon feature: Consensus sequon does not appear to be related to the site of glycosylation. However, it has been suggested that the local hydrophobicity upstream of Ser/Thr residues partially influences the site of glycosylation.
It is the first report of eubacterial flagellin glycosylation. The modified residues were identified in 1989
Year of Identification1996
Year of Validation1989