ProGP226

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ProGP ID ProGP226
Validation Status Characterized
Organism Information
Organism NamePseudomonas syringae pv. glycinea race 4
Domain Bacteria
Classification Family: Pseudomonadaceae
Order: Pseudomonadales
Class: Gammaproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI) 318
Genome Sequence(s)
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
Glycosite Sequence Logo
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 ID21440
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)].
Literature
Year of Identification2003
Year of Identification Month Wise2003.3.1
Year of Validation 2006
Reference Taguchi, F., Takeuchi, K., Katoh, E., Murata, K., Suzuki, T., Marutani, M., Kawasaki, T., Eguchi, M., Katoh, S., Kaku, H. et al. (2006) Identification of glycosylation genes and glycosylated amino acids of flagellin in Pseudomonas syringae pv. tabaci. Cell Microbiol, 8, 923-938. [PubMed: 16681835]
Author Taguchi, F., Takeuchi, K., Katoh, E., Murata, K., Suzuki, T., Marutani, M., Kawasaki, T., Eguchi, M., Katoh, S., Kaku, H. et al. (2006) Identification of glycosylation genes glycosylated amino acids of flagellin in Pseudomonas syringae pv. tabaci. Cell Microbiol, 8, 923-938. [PubMed: 16681835]
Research GroupThe Graduate School of Natural Science and Technology, Okayama University, Tsushima-naka 1-1-1, Okayama 700-8530, Japan
Corresponding Author glycosylated amino acids of flagellin in Pseudomonas syringae pv. tabaci. Cell Microbiol, 8, 923-938. [PubMed: 16681835]
ContactThe Graduate School of Natural Science and Technology, Okayama University, Tsushima-naka 1-1-1, Okayama 700-8530, Japan
Reference Taguchi, F., Takeuchi, K., Katoh, E., Murata, K., Suzuki, T., Marutani, M., Kawasaki, T., Eguchi, M., Katoh, S., Kaku, H. et al. (2006) Identification of glycosylation genes and glycosylated amino acids of flagellin in Pseudomonas syringae pv. tabaci. Cell Microbiol, 8, 923-938. [PubMed: 16681835]
Author Taguchi, F., Takeuchi, K., Katoh, E., Murata, K., Suzuki, T., Marutani, M., Kawasaki, T., Eguchi, M., Katoh, S., Kaku, H. glycosylated amino acids of flagellin in Pseudomonas syringae pv. tabaci. Cell Microbiol, 8, 923-938. [PubMed: 16681835]
Research GroupThe Graduate School of Natural Science and Technology, Okayama University, Tsushima-naka 1-1-1, Okayama 700-8530, Japan.
Corresponding Author glycosylated amino acids of flagellin in Pseudomonas syringae pv. tabaci. Cell Microbiol, 8, 923-938. [PubMed: 16681835]
ContactThe Graduate School of Natural Science and Technology, Okayama University, Tsushima-naka 1-1-1, Okayama 700-8530, Japan.
Reference1) Takeuchi, 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. J Bacteriol, 189, 6945-6956. [PubMed: 17644592]
AuthorTakeuchi, K., Ono, H., Yoshida, M., Ishii, T., Katoh, E., Taguchi, F., Miki, R., Murata, K., Kaku, H. and Ichinose, Y.
Research GroupNational Institute of Agrobiological Sciences, Kannondai 2-1-2, Tsukuba, Ibaraki 305-8602, Japan. kasumit@affrc.go.jp
Corresponding Author Ichinose, Y.
ContactNational Institute of Agrobiological Sciences, Kannondai 2-1-2, Tsukuba, Ibaraki 305-8602, Japan. kasumit@affrc.go.jp
Reference Taguchi, 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 Cell Physiol, 44, 342-349. [PubMed: 12668781]
Author Ichinose, Y.
Research GroupLaboratory of Plant Pathology & Genetic Engineering, Faculty of Agriculture, Okayama University, Tsushima-naka 1-1-1, Okayama, 700-8530 Japan.
Corresponding Author Taguchi, F., Shimizu, R., Inagaki, Y., Toyoda, K., Shiraishi, T. Ichinose, Y.
ContactLaboratory of Plant Pathology & Genetic Engineering, Faculty of Agriculture, Okayama University, Tsushima-naka 1-1-1, Okayama, 700-8530 Japan.