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ProGlyProt ID
BC172
Organism Information
Organism Name
Pseudomonas syringae pv. tabaci 6605
Domain
Bacteria
Classification
Family: Pseudomonadaceae
Order: Pseudomonadales
Class: Gammaproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI)
 
 
Genome Sequence(s)
EMBL
Organism Additional Information
This Gram-negative bacterium is phytopathogenic causing wildfire disease in tobacco plants. In this host tobacco infection, flagella play an important role.
 
 
Gene Information
Gene Name
fliC
 
 
Protein Information
Protein Name
Flagellin
UniProtKB/SwissProt ID
EMBL-CDS
UniProtKB Sequence
Sequence length
282 AA
Subcellular Location
Surface
Function
Flagellin, the major component of the flagella filament functions as one of the pathogen-associated molecular patterns (PAMPs). It is a major HR (hypersensitive reaction) elicitor in this pathogen but does not remarkably induce hypersensitive cell death in its host tobacco plants.
 
 
Protein Structure
Homology Model
Homology Model File
 
 
Glycosylation Status
Glycosylation Type
O (Ser) linked
Experimentally Validated Glycosite(s) in Full Length Protein
S143, S164, S176, S183, S193, S201
Experimentally Validated Glycosite(s ) in Mature Protein
S143, S164, S176, S183, S193, S201
Glycosite(s) Annotated Protein Sequence
>tr|Q6I809|Q6I809_PSESZ Flagellin OS=Pseudomonas syringae pv. tabaci GN=fliC PE=
4 SV=1 MALTVNTNVASLNVQKNLGRASDALSTSMTRLSSGLKINSAKDDAAGLQIATKITSQIRG QTMAIK
NANDGMSLAQTAEGALQESTNILQRMRELAVQSRNDSNSSTDRDALNKEFTAMS SELTRIAQSTNLNGKNLLDG
SAS*(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
Glycosite Sequence Logo
Technique(s) used for Glycosylation Detection
Rapid 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
Glycosylation, especially at positions S176 and S183, is required for smooth motility and bacterial virulence. Glycosylation is one of the important process in bacterial HR-inducing (hypersensitive reaction, a rapid and strong plant defence response) activity. Glycosylation may also serve to mask elicitor function of flagellin molecule in order to avoid plant recognition. Glycosylation of sites that are most surface-exposed plays a role in the swarming motility of the P. syringae pv. tabaci 6605.
 
 
Glycan Information
Glycan Annotation
Linkage: α-L-Rha-Ser.
Tetrasaccharide, 4,6-dideoxy-4-(3-hydroxybutanamido)-2-O-methyl-Glcp-(1→3)-α-L-Rhap-(1→2)-α-L-Rhap-(1→2)-α-L-Rha-(1→, as well as a trisaccharide, 4,6-dideoxy-4-(3-hydroxybutanamido)-2-O-methyl-Glcp-(1→3)-α-L-Rhap-(1→2)-α-L-Rha-(1→. Rhamnose (Rha) is exclusively of the L form. 4,6-dideoxy-4-(3-hydroxy-3-methylbutanamido)-2-O-methylglucopyranose is named as viosamine. Therefore, in the glycans, modified viosamine is present.
The ratios of a trisaccharide and a tetrasaccharide on LC by fluorescence detection were about 5:1, indicating that about five serine residues (including S201) were glycosylated with a trisaccharide. The major component of each glycan is similar to that at S201.
Microheterogeneity in glycosylation is observed.
BCSDB ID
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 coherence)].
 
 
Protein Glycosylation linked (PGL) gene(s)
Characterized Accessory Gene(s)
FGT1 and FGT2 are two glycosyltransferases which are encoded in the flagellin glycosylation island. Non-glycosylated and partially glycosylated flagellins were respectively produced by fgt1 and fgt2 mutants.
 
 
Literature
Reference(s)
1) Taguchi, F., Yamamoto, M., Ohnishi-Kameyama, M., Iwaki, M., Yoshida, M., Ishii, T., Konishi, T. and Ichinose, Y. (2010) Defects in flagellin glycosylation affect the virulence of Pseudomonas syringae pv. tabaci 6605. Microbiology, 156, 72-80. [PubMed: 19815579]
2) Konishi, T., Taguchi, F., Iwaki, M., Ohnishi-Kameyama, M., Yamamoto, M., Maeda, I., Nishida, Y., Ichinose, Y., Yoshida, M. and Ishii, T. (2009) Structural characterization of an O-linked tetrasaccharide from Pseudomonas syringae pv. tabaci flagellin. Carbohydr Res, 344, 2250-2254. [PubMed: 19766989]
3) 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]
4) 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]
5) 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]
Year of Identification
2003
Year of Validation
2006
 
 
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