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ProGlyProt ID
AC116
Organism Information
Organism Name
Methanococcus voltae PS
Domain
Archaea
Classification
Family: Methanococcaceae
Order: Methanococcales
Class: Methanococci or Methanothermea
Division or phylum: "Euryarchaeota"
Taxonomic ID (NCBI)
 
 
Genome Sequence(s)
EMBL
 
 
Gene Information
Gene Name
sla
 
 
Protein Information
Protein Name
S-layer protein
UniProtKB/SwissProt ID
EMBL-CDS
UniProtKB Sequence
Sequence length
576 AA
Subcellular Location
Surface
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 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 Protein
N79, 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 P
E=1 SV=2 KKIGAIAAGSAMVASALATGVFAVEKIGDVEGFKVIDNGEPTADIVVGSTAAAADVVSAA NVAA
KVGSMMFKEGEAASGSAKLTVKASAESDDANLKSLLTN*(102)GTNDFTELDAGKEAFVVA AADSDYSDAL
INATTGFANIADNVLYDQAKLAAAVSLGDLSTLSVVKDIDPSDWYADKNK AADVATKDYYDQDGDAVEMLMATV
ASNDDGKSLTVDEDGVLYASIAYDDDNEDFQRATQV LKEGNRLPFLGEEYALVKLDTDDDIVYLGKEVFDGVLK
EGDTYNIGDGYELKVVAILKSG DEYKISLQLMKDGKVVAEKFDKVSATSALKMIYTPGNIGIVVNEAWENVGQD
YGYGSTLI TKDVIALELGEEYIPDWEVVTIEKDTTTDNTKDSKMTLSDDKITKDNTYGIGLQYVGDEE DNFK
SGKAIKIAKYAELELDDEDKEDTKLNLFFSMDETKEATLAAGQKVTVLNSDITLSE VMADAKAPVAFKAPLAVL
DTEVSLDAANKKLILVGGPVANALTKELADAGKIEMTVESPA TLAVVAGAANGNDVLVVAGGDRAATAEAANAL
IEML
Sequence Around Glycosites (21 AA)
DDANLKSLLTNGTNDFTELDA
ADSDYSDALINATTGFANIAD
Technique(s) used for Glycosylation Detection
Glycan (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 ID
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 Protein Name
AglB
OST UniProtKB/ SwissProt ID
OST EMBL-CDS
OST UniProtKB Sequence
>tr|Q2EMT4|Q2EMT4_METVO STT3 OS=Methanococcus voltae GN=MVO1749 PE=4 SV=1MTENNEK
VKNSDSANNQSSKNSKFNFNFEDKKVKCAKTILIIIFLAFLSFQMRAQTADMGFTTNEQYLDVFSDDNGRMYLTAL
DPYYYLRMSENYLENGHTGDTLKNIDGQQVPWDSYKYGPTGARATFNLLSVVTVWVYQVWHAMDSTVTLMNAAFWV
PAILSMFLITPIFFTVRRITSSDIGGAVAAILASLSPSIFVKTVAGFSDTPILEILPLLFIVWFIIEAIHYSKEKN
YKSLIYGLLATLMLALYPFMWSAWWYGYYIVIAFLVIYAIYKGISYNSIAKYTKSKNNNHKDKIESEKLEMLNILK
ISGLFIIGGAVLITALYGVSTTMNALQAPLNYLGLDEVSSQTGWPNVLTTVSELDTASLDEIISSSLGSIHLFAIG
LIGIFLSLFRKVLTPVKQISNGLAEKLDIKYALLLIIWFAVTFLAASKGVRFVALMVPPLSIGVGIFVGFIEQFIK
NNLDKKYEYVAYPTIAIIVLYALFTIYRADSADLVRMLLPSNYVPIAEGIMLASLAVLIIYKVAELIAESNKKLVM
NKIFMILLAIGLITPTIATIVPFYSVPTYNDGWGESLEWINTQTPNNSVVTCWWDNGHIYTWKTDRMVTFDGSSQN
TPRAYWVGRAFSTSNESLANGIFRMLASSGDKAYTTDSVLIKKTGSIKNTVDVLNEILPLTKSDAQKALKNSSYKF
TDTEVSEILDATHPKVTNPDYLITYNRMTSIASVWSYFGNWDFNLPAGTSRSEREAGSFQGLQTYATNINDTLIVR
SLIQQTAEYNIYTLIEVRNETLTGAMMAVTNDGQMQTQQLNMHKVKLMVNENGKSKMYNSLADPDGQLSLLIKVDK
NSIIGTDGSNNPVYSSSSWMATANLEDSVYSKLHFFDGEGLDTIKLEKESLDPTANGVQPGFKVFSVDYGNYSK
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.
PGL Additional Links
 
 
Literature
Reference(s)
1) 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]
2) 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]
3) 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]
4) 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]
Year of Identification
2005
Year of Validation
2005
 
 
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