ProGP241 (FlaA)
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ProGP ID | ProGP241 (FlaA) |
Validation Status | Characterized |
Organism Information | |
Organism Name | Methanococcus voltae PS |
Domain | Archaea |
Classification | Phylum : Euryarchaeota Class : Methanococci Orders : Methanococcales Family : Methanococcaceae Genus : Methanococcus Species : voltae Strain : PS |
Taxonomic ID (NCBI) | 2188 |
Genome Information | |
GenBank | M72148 |
EMBL | M72148 |
Gene Information | |
Gene Name | flaA |
Protein Information | |
Protein Name | FlaA |
UniProtKB/SwissProt ID | P27802 |
EMBL-CDS | AAA73073.1 |
UniProtKB Sequence | >sp|P27802|FLAA_METVO Flagellin A OS=Methanococcus voltae GN=flaA PE=1 SV=1 MKVKEFMNNKKGATGVGTLIVFIAMVLVAAVAASVLINTSGFLQQKASSTGTESTEQVST GLKMFQTSGKLNEPIIDRLTIYVTPSPGSKPVDLKNTKLLMNRWTFQPPPVSYSSTYFEN NNKQIFDVTGSKAWNNGAILPEYNFGVIVIQDDDGSCTAESPVIGKGDMAVITINCTNLD LAPRTRLNGYLQSEIGFKTQFTYILPNAYDKTEDVVILQ |
Sequence length | 219 AA |
Subcellular Location | Surface |
Function | Flagellin structural protein |
Glycosylation Status | |
Glycosylation Type | N- (Asn) linked |
Experimentally Validated Glycosite(s) in Full Length Protein | (Propeptide: 1-12) N175 |
Experimentally Validated Glycosite(s ) in Mature Protein | N163 |
Glycosite(s) Annotated Protein Sequence | >sp|P27802|FLAA_METVO Flagellin A OS=Methanococcus voltae GN=flaA PE=1 SV=1 MKVKEFMNNKKGATGVGTLIVFIAMVLVAAVAASVLINTSGFLQQKASSTGTESTEQVST GLKMFQTSGKLNEPIIDRLTIYVTPSPGSKPVDLKNTKLLMNRWTFQPPPVSYSSTYFEN NNKQIFDVTGSKAWNNGAILPEYNFGVIVIQDDDGSCTAESPVIGKGDMAVITIN*(175)CTNLD LAPRTRLNGYLQSEIGFKTQFTYILPNAYDKTEDVVILQ |
Sequence Around Glycosites (21 AA) | GKGDMAVITINCTNLDLAPRT |
Technique(s) used for Glycosylation Detection | Mass shift detected on SDS-polyacrylamide gel and glycan identification by nano-LC-MS/MS |
Technique(s) used for Glycosylated Residue(s) Detection | Nano-LC-MS/MS (nano-liquid chromatography-electrospray tandem mass spectrometry) |
Protein Glycosylation- Implication | The glycans on flagellin proteins are involved in the flagella assembly process. |
Glycan Information | |
Glycan Annotation | Linkage:β-GlcNAc-Asn. Trisaccharide (779 Da) composed ofβ-Manp NAcA6Thr-(1- 4)-β-Glcp NAc3NAcA-(1-3)-β-Glcp NAc. The sugars are mannuronic acid with the attached threonine, diacetylated glucuronic acid, N-acetylglucosamine. In a second version of this strain (M. voltae PS*), the glycan is modified with one additional residue (either 220 or 262 Da) linked to the terminal modified mannuronic acid. |
BCSDB ID | 10182 |
GlyTouCan | G47369PB |
Technique(s) used for Glycan Identification | NanoLC-MS/MS analysis and NMR spectroscopy-COSY (correlated spectroscopy), TOCSY (total correlation spectroscopy), NOESY (nuclear Overhauser effect spectroscopy) spectra, and 1H-13C HMBC (heteronuclear multiple bond coherence) spectra. |
Protein Glycosylation linked (PGL) gene(s) | |
OST Gene Name | AglB |
OST ProGT ID | ProGT16 |
Characterized Accessory Gene(s) | AglH, AglC, AglK, AglA glycosyltransferases are involved in the biosynthesis of the glycan. AglH is a GlcNAc-1-phosphate transferase transfering first sugar to dolichol pyrophosphate. AglC and AglK add the second sugar residue and AglA adds the third sugar to the glycan. Characterized by gene deletion studies |
Accessory Gene(s)Progt ID | ProGT16.1, ProGT16.2, Pro |
Additional Comment | Post translational modification was detected in the year 1999. It was confirmed as glycosylation (by identifying the glycans) in 2005. |
Literature | |
Year of Identification | 2005 |
Year of Identification Month Wise | 2005.4.29 |
Year of Validation | 2005 |
Reference | Chaban, B., Logan, S.M., Kelly, J.F. and Jarrell, K.F., 2009. AglC and AglK are involved in biosynthesis and attachment of diacetylated glucuronic acid to the N-glycan in Methanococcus voltae. Journal of Bacteriology, 191(1), pp.187-195. |
Corresponding Author | KEN F. JARRELL |
Contact | Department of Microbiology and Immunology, Queen's University, Kingston, Ontario, Canada K7L 3N6. |
Reference | Shams-Eldin, H., Chaban, B., Niehus, S., Schwarz, R.T. and Jarrell, K.F., 2008. Identification of the archaeal alg7 gene homolog (encoding N-acetylglucosamine-1-phosphate transferase) of the N-linked glycosylation system by cross-domain complementation in Saccharomyces cerevisiae. Journal of Bacteriology, 190(6), pp.2217-2220. |
Corresponding Author | KEN F. JARRELL |
Contact | Department of Microbiology and Immunology, Queen's University, Kingston, Ontario, Canada K7L 3N6. |
Reference | Chaban, B., Voisin, S., Kelly, J., Logan, S.M. and Jarrell, K.F., 2006. Identification of genes involved in the biosynthesis and attachment of Methanococcus voltae N‐linked glycans: insight into N‐linked glycosylation pathways in Archaea. Molecular microbiology, 61(1), pp.259-268. |
Corresponding Author | KEN F. JARRELL |
Contact | Department of Microbiology and Immunology, Queen's University, Kingston, Ontario, Canada K7L 3N6. |
Reference | Voisin, S., Houliston, R.S., Kelly, J., Brisson, J.R., Watson, D., Bardy, S.L., Jarrell, K.F. and Logan, S.M., 2005. Identification and characterization of the unique N-linked glycan common to the flagellins and S-layer glycoprotein of Methanococcus voltae. Journal of Biological Chemistry, 280(17), pp.16586-16593. |
Corresponding Author | Susan M Logan |
Contact | Institute for Biological Sciences, National Research Council of Canada, Ottawa, Ontario K1A 0R6, Canada. |
Reference | Bayley, D.P. and Jarrell, K.F., 1999. Overexpression of Methanococcus voltae flagellin subunits in Escherichia coli and Pseudomonas aeruginosa: a source of archaeal preflagellin. Journal of bacteriology, 181(14), pp.4146-4153. |
Corresponding Author | KEN F. JARRELL |
Contact | Department of Microbiology and Immunology, Queen's University, Kingston, Ontario, Canada K7L 3N6. |