| ProGlyProt ID | BC115 | | Organism Information | | Organism Name | Campylobacter coli VC 167 | | Domain | Bacteria | | Classification | Family: Campylobacteraceae
Order: Campylobacterales
Class: Epsilonproteobacteria
Division or phylum: "Proteobacteria" | | Taxonomic ID (NCBI) | 195 | | Genome Sequence (s) | | EMBL | M64670 | | Gene Information | | Gene Name | flaA | | NCBI Gene ID | | | Protein Information | | Protein Name | Flagellin A | | UniProtKB/SwissProt ID | P27053 | | NCBI RefSeq | | | EMBL-CDS | AAA23022.1 | | 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 length | 573 AA | | Subcellular Location | Secreted | | Function | It 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 Type | O (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 Protein | S206, 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 Logo | seqlogo | | Glycosite Sequence Logo |  | | Technique(s) used for Glycosylation Detection | Biotin-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) Detection | Edman sequencing | | Protein Glycosylation- Implication | Sone 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 Annotation | More 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 Identification | Homo- 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 Links | CAZy | | 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 Comments | It 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 Identification | 1996 | | Year of Validation | 1989 |
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