ProGP225 (Flagellin)

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ProGP ID ProGP225 (Flagellin)
Validation Status Characterized
Organism Information
Organism NamePseudomonas syringae pv. glycinea race 4
Domain Bacteria
Classification Phylum : Proteobacteria
Class : gammaproteobacteria
Orders : Pseudomondales
Family : Pseudomonadaceae
Genus : Pseudomonas
Species : savastanoi
Taxonomic ID (NCBI) 318
Genome Information
GenBank AB061232
EMBL AB061232
Organism Additional Information This Gram-negative bacterium is phytopathogenic.
Gene Information
Gene NamefliC
Protein Information
Protein NameFlagellin
UniProtKB/SwissProt ID Q76M64
EMBL-CDSBAD06420.1
UniProtKB Sequence >tr|Q76M64|Q76M64_PSESG Flagellin OS=Pseudomonas syringae pv. glycinea GN=fliC PE=4 SV=1 MALTVNTNAASLNVQKNLGRASDALSTSMTRLSSGLKINSAKDDAAGLQIATKITSQIRG QTMAIKNANDGMSLAQTAEGALQESTNILQRMRELAVQSRNDSNSSTDRDALNKEFTAMS SELTRIAQSTNLNGKNLLDGSASTMTFQVGSNSGASNQITLTLSASFDANTLGVGSAVTI AGSDSTTAETNFSAAIAAIDSALQTINSTRADLGAAQNRLTSTISNLQNINENASAALGR VQDTDFAAETAQLTKQQTLQQASTSVLAQANQLPSAVLKLLQ
Sequence length 282 AA
Subcellular LocationSurface
Function Flagellin, the major component of the flagella filament functions as one of the pathogen-associated molecular patterns (PAMPs). It is able to induce hypersensitive cell death in its non-host tobacco plants.
Glycosylation Status
Glycosylation Type O- (Ser) linked
Experimentally Validated Glycosite(s) in Full Length ProteinS143, S164, S176, S183, S193, S201
Experimentally Validated Glycosite(s ) in Mature ProteinS143, S164, S176, S183, S193, S201
Glycosite(s) Annotated Protein Sequence >tr|Q76M64|Q76M64_PSESG Flagellin OS=Pseudomonas syringae pv. glycinea GN=fliC PE=4 SV=1 MALTVNTNAASLNVQKNLGRASDALSTSMTRLSSGLKINSAKDDAAGLQIATKITSQIRG QTMAIKNANDGMSLAQTAEGALQESTNILQRMRELAVQSRNDSNSSTDRDALNKEFTAMS SELTRIAQSTNLNGKNLLDGSAS*(143)TMTFQVGSNSGASNQITLTLS*(164)ASFDANTLGVGS*(176)AVTI AGS*(183)DSTTAETNFS*(193)AAIAAIDS*(201)ALQTINSTRADLGAAQNRLTSTISNLQNINENASAALGR VQDTDFAAETAQLTKQQTLQQASTSVLAQANQLPSAVLKLLQ
Sequence Around Glycosites (21 AA) NGKNLLDGSASTMTFQVGSNS
GASNQITLTLSASFDANTLGV
SFDANTLGVGSAVTIAGSDST
GVGSAVTIAGSDSTTAETNFS
SDSTTAETNFSAAIAAIDSAL
NFSAAIAAIDSALQTINSTRA
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Technique(s) used for Glycosylation DetectionRapid migration on SDS-PAGE after chemical deglycosylation with TFMS, glycoprotein staining using GelCode-glycoprotein staining kit.
Technique(s) used for Glycosylated Residue(s) Detection Site-directed mutagenesis and MALDI-TOF MS (matrix assisted laser desorption/ionization time of flight mass spectrometry) analysis
Protein Glycosylation- Implication The flagellin glycan structures have a role to play in the virulence and host specificity of P. syringae. Glycosylation is important for the HR-inducing (hypersensitive reaction, a rapid and strong plant defence response) ability of the flagellin in plants.
Glycan Information
Glycan Annotation Linkage: Rha-Ser.
S201 carries a unique trisaccharide consisting of two rhamnosyl (Rha) residues and one modified 4-amino-4,6-dideoxyglucosyl (Qui4N; named as viosamine) residue, ß-D-Quip4N(3-hydroxy-1-oxobutyl)2Me-(1→3)-α-L-Rhap-(1→2)-α-L-Rhap. The trisaccharide is present as the major glycan on each Ser residue. The glycans contain both L-Rha and D-Rha at a molar ratio of about 4:1.
Heterogeneity due to the addition of one or two units of mass value 147 is also observed.
BCSDB ID 21440
GlyTouCan G82631IS
Technique(s) used for Glycan Identification Sugar composition analysis using an ABEE (p-aminobenzoic acid ethyl ester) labeling kit, MALDI-TOF MS (matrix-assisted laser desorption ionization?time-of-flight mass spectrometry), determination of D-Rha/L-Rha ratios using gas chromatography (GC), and 1H-NMR analyses including 1H-1H correlation spectra [DQF-COSY (double quantum filtered correlation spectroscopy), TOCSY (total correlation spectroscopy), and NOESY (nuclear Overhauser and exchange spectroscopy)] and 1H-13C correlation spectra [HSQC (heteronuclear single-quantum coherence) and HMBC (heteronuclear multiple bond connectivity)].
Protein Glycosylation linked (PGL) gene(s)
Characterized Accessory Gene(s)Orf1 and Orf2 are putative glycosyltransferases encoded in the flagellin glycosylation island.
Literature
Year of Identification2003
Year of Identification Month Wise2003.3.1
Year of Validation 2006
ReferenceTakeuchi, K., Ono, H., Yoshida, M., Ishii, T., Katoh, E., Taguchi, F., Miki, R., Murata, K., Kaku, H. and Ichinose, Y., 2007. Flagellin glycans from two pathovars of Pseudomonas syringae contain rhamnose in D and L configurations in different ratios and modified 4-amino-4, 6-dideoxyglucose. Journal of bacteriology, 189(19), pp.6945-6956.
Corresponding Author Kasumi Takeuchi
ContactNational Institute of Agrobiological Sciences, Kannondai 2-1-2, Tsukuba, Ibaraki 305-8602, Japan.
ReferenceTaguchi, F., Takeuchi, K., Katoh, E., Murata, K., Suzuki, T., Marutani, M., Kawasaki, T., Eguchi, M., Katoh, S., Kaku, H. and Yasuda, C., 2006. Identification of glycosylation genes and glycosylated amino acids of flagellin in Pseudomonas syringae pv. tabaci. Cellular microbiology, 8(6), pp.923-938.
Corresponding Author Yuki Ichinose
ContactLaboratory of Plant Pathology & Genetic Engineering, Faculty of Agriculture, Okayama University, Tsushima-naka 1-1-1, Okayama, 700-8530 Japan.
ReferenceTaguchi, F., Shimizu, R., Inagaki, Y., Toyoda, K., Shiraishi, T. and Ichinose, Y., 2003. Post-translational modification of flagellin determines the specificity of HR induction. Plant and cell physiology, 44(3), pp.342-349.
Corresponding Author Yuki Ichinose
ContactLaboratory of Plant Pathology & Genetic Engineering, Faculty of Agriculture, Okayama University, Tsushima-naka 1-1-1, Okayama, 700-8530 Japan.