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ProGlyProt ID
BC171
Organism Information
Organism Name
Pseudomonas syringae pv. glycinea race 4
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.
 
 
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 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 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|Q76M64|Q76M64_PSESG Flagellin OS=Pseudomonas syringae pv. glycinea GN=fliC P
E=4 SV=1 MALTVNTNAASLNVQKNLGRASDALSTSMTRLSSGLKINSAKDDAAGLQIATKITSQIRG QTMA
IKNANDGMSLAQTAEGALQESTNILQRMRELAVQSRNDSNSSTDRDALNKEFTAMS SELTRIAQSTNLNGKNLL
DGSAS*(143)TMTFQVGSNSGASNQITLTLS*(164)ASFDANTLGVGS*(176)AVTI AGS*(18
3)
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
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
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)
Orf1 and Orf2 are putative glycosyltransferases encoded in the flagellin glycosylation island.
 
 
Literature
Reference(s)
1) 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]
2) 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]
3) 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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