ProGP242

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ProGP ID ProGP242
Validation Status Characterized
Organism Information
Organism NameMethanococcus voltae PS
Domain Archaea
Classification Family: Methanococcaceae
Order: Methanococcales
Class: Methanococci or Methanothermea
Division or phylum: "Euryarchaeota"
Taxonomic ID (NCBI) 2188
Genome Sequence(s)
EMBL M72148
Gene Information
Gene NameflaA
Protein Information
Protein NameFlaA
UniProtKB/SwissProt ID P27802
EMBL-CDSAAA73073.1
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 LocationSurface associated
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 ProteinN163
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
Glycosite Sequence Logo
Technique(s) used for Glycosylation DetectionMass 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 of β-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 ID10182
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 NameAglB
OST ProGT IDProGT14
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 IDProGT14.1-ProGT14.4
Literature
Additional CommentPost translational modification was detected in the year 1999. It was confirmed as glycosylation (by identifying the glycans) in 2005.
Year of Identification2005
Year of Identification Month Wise2005.4.29
Year of Validation 2005
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. J Bacteriol, 190, 2217-2220. [PubMed: 18178736]
Author Shams-Eldin, H., Chaban, B., Niehus, S., Schwarz, R.T. Jarrell, K.F.
Research GroupInstitute for Virology, AG Parasitologie BMFZ, Philipps-University Marburg, Hans-Meerwein-Str. 2, 35043 Marburg, Germany.
Corresponding Author Jarrell, K.F.
ContactInstitute for Virology, AG Parasitologie BMFZ, Philipps-University Marburg, Hans-Meerwein-Str. 2, 35043 Marburg, Germany.
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. J Bacteriol, 190, 2217-2220. [PubMed: 18178736]
Author Shams-Eldin, H., Chaban, B., Niehus, S., Schwarz, R.T. and Jarrell, K.F
Research GroupInstitute for Virology, AG Parasitologie BMFZ, Philipps-University Marburg, Hans-Meerwein-Str. 2, 35043 Marburg, Germany.
Corresponding Author Jarrell, K.F.
ContactInstitute for Virology, AG Parasitologie BMFZ, Philipps-University Marburg, Hans-Meerwein-Str. 2, 35043 Marburg, Germany.
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. J Biol Chem, 280, 16586-16593. [PubMed: 15723834]
Author Voisin, S., Houliston, R.S., Kelly, J., Brisson, J.R., Watson, D., Bardy, S.L., Jarrell, K.F. Logan, S.M.
Research GroupInstitute for Biological Sciences, National Research Council, Ottawa, Ontario K1A OR6, Canada
Corresponding Author Logan, S.M.
ContactInstitute for Biological Sciences, National Research Council, Ottawa, Ontario K1A OR6, Canada
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. Mol Microbiol, 61, 259-268. [PubMed: 16824110]
Author Jarrell, K.F.
Research GroupDepartment of Microbiology and Immunology, Queen's University, Kingston, Ontario, K7L 3N6, Canada.
Corresponding Author Chaban, B., Voisin, S., Kelly, J., Logan, S.M. Jarrell, K.F.
ContactDepartment of Microbiology and Immunology, Queen's University, Kingston, Ontario, K7L 3N6, Canada.
Reference1) 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. J Bacteriol, 191, 187-195. [PubMed: 18978056]
AuthorChaban, B., Logan, S.M., Kelly, J.F. and Jarrell, K.F.
Research GroupDepartment of Microbiology and Immunology, Queen's University, Kingston, Ontario, K7L 3N6, Canada.
Corresponding Author Jarrell, K.F.
ContactDepartment of Microbiology and Immunology, Queen's University, Kingston, Ontario, K7L 3N6, 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. J Bacteriol, 181, 4146-4153. [PubMed: 10400569]
Author Bayley, D.P. Jarrell, K.F.
Research GroupDepartment of Microbiology and Immunology, Queen's University, Kingston, Ontario, Canada K7L 3N6.
Corresponding Author Jarrell, K.F.
ContactDepartment of Microbiology and Immunology, Queen's University, Kingston, Ontario, Canada K7L 3N6.