ProGP243

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ProGP ID ProGP243
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)
GenBank M59200
EMBL M59200
Gene Information
Gene Namesla
Protein Information
Protein NameS-layer protein
UniProtKB/SwissProt ID Q50833
EMBL-CDSAAA93515.1
UniProtKB Sequence >sp|Q50833|CSG_METVO S-layer protein (Fragment) OS=Methanococcus voltae GN=sla PE=1 SV=2 KKIGAIAAGSAMVASALATGVFAVEKIGDVEGFKVIDNGEPTADIVVGSTAAAADVVSAA NVAAKVGSMMFKEGEAASGSAKLTVKASAESDDANLKSLLTNGTNDFTELDAGKEAFVVA AADSDYSDALINATTGFANIADNVLYDQAKLAAAVSLGDLSTLSVVKDIDPSDWYADKNK AADVATKDYYDQDGDAVEMLMATVASNDDGKSLTVDEDGVLYASIAYDDDNEDFQRATQV LKEGNRLPFLGEEYALVKLDTDDDIVYLGKEVFDGVLKEGDTYNIGDGYELKVVAILKSG DEYKISLQLMKDGKVVAEKFDKVSATSALKMIYTPGNIGIVVNEAWENVGQDYGYGSTLI TKDVIALELGEEYIPDWEVVTIEKDTTTDNTKDSKMTLSDDKITKDNTYGIGLQYVGDEE DNFKSGKAIKIAKYAELELDDEDKEDTKLNLFFSMDETKEATLAAGQKVTVLNSDITLSE VMADAKAPVAFKAPLAVLDTEVSLDAANKKLILVGGPVANALTKELADAGKIEMTVESPA TLAVVAGAANGNDVLVVAGGDRAATAEAANALIEML
Sequence length 576 AA
Subcellular LocationSurface
Function In Archaea, which do not possess other cell wall components, the S-layer has to maintain the cell integrity and stabilize as well as to protect the cell against mechanical and osmotic stresses or extreme pH conditions. It is also predicted that the S-layer has to maintain or even determine the cell shape.
Glycosylation Status
Glycosylation Type N- (Asn) linked
Experimentally Validated Glycosite(s) in Full Length Protein(Signal peptide: 1-23) N102, also N132 in a second version of this strain (M. voltae PS*).
Experimentally Validated Glycosite(s ) in Mature ProteinN79, also N109 in a second version of this strain (M. voltae PS*).
Glycosite(s) Annotated Protein Sequence >sp|Q50833|CSG_METVO S-layer protein (Fragment) OS=Methanococcus voltae GN=sla PE=1 SV=2 KKIGAIAAGSAMVASALATGVFAVEKIGDVEGFKVIDNGEPTADIVVGSTAAAADVVSAA NVAAKVGSMMFKEGEAASGSAKLTVKASAESDDANLKSLLTN*(102)GTNDFTELDAGKEAFVVA AADSDYSDALINATTGFANIADNVLYDQAKLAAAVSLGDLSTLSVVKDIDPSDWYADKNK AADVATKDYYDQDGDAVEMLMATVASNDDGKSLTVDEDGVLYASIAYDDDNEDFQRATQV LKEGNRLPFLGEEYALVKLDTDDDIVYLGKEVFDGVLKEGDTYNIGDGYELKVVAILKSG DEYKISLQLMKDGKVVAEKFDKVSATSALKMIYTPGNIGIVVNEAWENVGQDYGYGSTLI TKDVIALELGEEYIPDWEVVTIEKDTTTDNTKDSKMTLSDDKITKDNTYGIGLQYVGDEE DNFKSGKAIKIAKYAELELDDEDKEDTKLNLFFSMDETKEATLAAGQKVTVLNSDITLSE VMADAKAPVAFKAPLAVLDTEVSLDAANKKLILVGGPVANALTKELADAGKIEMTVESPA TLAVVAGAANGNDVLVVAGGDRAATAEAANALIEML
Sequence Around Glycosites (21 AA) DDANLKSLLTNGTNDFTELDA
ADSDYSDALINATTGFANIAD
Glycosite Sequence Logo
Technique(s) used for Glycosylation DetectionGlycan (779 Da) 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 Mutations that ultimately alter the structure of the S-layer protein could affect the protein interaction and disrupt the structural integrity of the cell. As a result, such mutants could suffer serious cell stability problems. It is this effect on the S-layer that likely explains why the agl mutants are so unstable.
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
Year of Identification2005
Year of Identification Month Wise2005.4.29
Year of Validation 2005
ReferenceChaban, 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, Queens University, Kingston, Ontario, K7L 3N6, Canada.
Corresponding Author Jarrell, K.F.
ContactDepartment of Microbiology and Immunology, Queens University, Kingston, Ontario, K7L 3N6, Canada.
ReferenceShams-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]
AuthorShams-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 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 Chaban, B., Voisin, S., Kelly, J., Logan, S.M. Jarrell, K.F.
Research GroupDepartment of Microbiology and Immunology, Queens University, Kingston, Ontario, K7L 3N6, Canada.
Corresponding Author Jarrell, K.F.
ContactDepartment of Microbiology and Immunology, Queens University, Kingston, Ontario, K7L 3N6, Canada.
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