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ProGlyProt ID
AC108
Organism Information
Organism Name
Haloferax (Halobacterium) volcanii DS2
Domain
Archaea
Classification
Family: Halobacteriaceae
Order: Halobacteriales
Class: Halobacteria or Halomebacteria
Division or phylum: "Euryarchaeota"
Taxonomic ID (NCBI)
 
 
Genome Sequence(s)
GenBank
EMBL
 
 
Gene Information
Gene Name
csg
NCBI Gene ID
GenBank Gene Sequence
 
 
Protein Information
Protein Name
S-lyer glycoprotein
UniProtKB/SwissProt ID
NCBI RefSeq
EMBL-CDS
UniProtKB Sequence
>sp|P25062|CSG_HALVO Cell surface glycoprotein OS=Halobacterium volcanii GN=csg
PE=1 SV=1 MTKLKDQTRAILLATLMVTSVFAGAIAFTGSAAAERGNLDADSESFNKTIQSGDRVFLGE EISTD
AGLGASNPLLTGTAGNSEGVSLDLSSPIPQTTENQPLGTYDVDGSGSATTPNVTL LAPRITDSEILTSSGGDVTG
SAISSSDAGNLYVNADYNYESAEKVEVTVEDPSGTDITNE VLSGTDTFVDDGSIGSTSSTGGGVGIDMSDQDAGE
YTIILEGAEDLDFGDATETMTLTIS SQDEIGIELDSESVTQGTDVQYTVTNGIDGNEHVVAMDLSDLQNDATTEQ
AKEVFRNIGD TSEVGIANSSATNTSGSSTGPTVETADIAYAVVEIDGASAVGGIETQYLDDSEVDLEVYD AGVS
ATAAVGQDATNDITLTIEEGGTTLSSPTGQYVVGSEVDINGTATSSDSVAIYVRDD GDWQLLEIGGDNEISVDSD
DTFEEEDIALSGLSGDGSSILSLTGTYRIGVIDASDADVGG DGSVDDSLTTSEFTSGVSSSNSIRVTDQALTGQF
TTINGQVAPVETGTVDINGTASGANS VLVIFVDERGNVNYQEVSVDSDGTYDEDDITVGLTQGRVTAHILSVGRD
SAIGDGSLPSG PSNGATLNDLTGYLDTLDQNNNNGEQINELIASETVDETASDDLIVTETFRLAESSTSID SIY
PDAAEAAGINPVATGETMVIAGSTNLKPDDNTISIEVTNEDGTSVALEDTDEWNNDG QWMVEIDTTDFETGTFTV
EADDGDNTDTVNVEVVSEREDTTTSSDNATDTTTTTDGPTET TTTAEPTETTEEPTEETTTSSNTPGFGIAVALV
ALVGAALLALRREN
Sequence length
827 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, (O, Thr-linked residues not known)
Experimentally Validated Glycosite(s) in Full Length Protein
(Signal peptide: 1-34) N47, N117, N308, N313, N532
Experimentally Validated Glycosite(s ) in Mature Protein
N13, N83, N274, N279, N498
Glycosite(s) Annotated Protein Sequence
>sp|P25062|CSG_HALVO Cell surface glycoprotein OS=Halobacterium volcanii GN=csg
PE=1 SV=1 MTKLKDQTRAILLATLMVTSVFAGAIAFTGSAAAERGNLDADSESFN*(47)KTIQSGDRVFL
GE EISTDAGLGASNPLLTGTAGNSEGVSLDLSSPIPQTTENQPLGTYDVDGSGSATTPN*(117)VTL LA
PRITDSEILTSSGGDVTGSAISSSDAGNLYVNADYNYESAEKVEVTVEDPSGTDITNE VLSGTDTFVDDGSIGS
TSSTGGGVGIDMSDQDAGEYTIILEGAEDLDFGDATETMTLTIS SQDEIGIELDSESVTQGTDVQYTVTNGIDG
NEHVVAMDLSDLQNDATTEQAKEVFRNIGD TSEVGIAN*(308)SSATN*(313)TSGSSTGPTVETADI
AYAVVEIDGASAVGGIETQYLDDSEVDLEVYD AGVSATAAVGQDATNDITLTIEEGGTTLSSPTGQYVVGSEVD
INGTATSSDSVAIYVRDD GDWQLLEIGGDNEISVDSDDTFEEEDIALSGLSGDGSSILSLTGTYRIGVIDASDA
DVGG DGSVDDSLTTSEFTSGVSSSNSIRVTDQALTGQFTTINGQVAPVETGTVDIN*(532)GTASGANS
VLVIFVDERGNVNYQEVSVDSDGTYDEDDITVGLTQGRVTAHILSVGRDSAIGDGSLPSG PSNGATLNDLTGYL
DTLDQNNNNGEQINELIASETVDETASDDLIVTETFRLAESSTSID SIYPDAAEAAGINPVATGETMVIAGSTN
LKPDDNTISIEVTNEDGTSVALEDTDEWNNDG QWMVEIDTTDFETGTFTVEADDGDNTDTVNVEVVSEREDTTT
SSDNATDTTTTTDGPTET TTTAEPTETTEEPTEETTTSSNTPGFGIAVALVALVGAALLALRREN
Sequence Around Glycosites (21 AA)
GNLDADSESFNKTIQSGDRVF
VDGSGSATTPNVTLLAPRITD
IGDTSEVGIANSSATNTSGSS
EVGIANSSATNTSGSSTGPTV
APVETGTVDINGTASGANSVL
Glycosite Sequence Logo
Glycosite Sequence Logo
Technique(s) used for Glycosylation Detection
Deglycosylation with anhydrous hydrogen fluoride.
Technique(s) used for Glycosylated Residue(s) Detection
Nano-LC-ES-MS/MS (nano-liquid chromatography-electrospray tandem mass spectrometry)
Protein Glycosylation- Implication
N-glycosylation endows H. volcanii with an ability to maintain an intact and stable cell envelope (correct S-layer architecture and stable association of the S-layer glycoprotein within the S-layer) in hypersaline surroundings, ensuring survival in this extreme environment.
 
 
Glycan Information
Glycan Annotation
Linkage: βGlc-Asn, Gal-Thr.
N glycosylated with a pentasaccharide (2 hexoses, 2 hexuronic acids and a methyl ester of hexuronic acid). Pentasaccharide sequence is: hexose (Hex)-X-hexuronic acid (HexA)-HexA-Hex-peptide, where X is a 190 Da moiety, likely to be either dimethylated hexose or the methyl ester of hexuronic acid. Relatively minor amount of the completed pentasaccharide as compared to the level of tetrasaccharide as well as di- and trisaccharide-bearing species were detected during experiments.
Glucosyl-(1→2)-galactose disaccharides linked to clustered threonine residues at 4-6 positions adjacent to the membrane anchor at the C terminus but precise position of O glycosylated residue is not known.
 
 
Protein Glycosylation linked (PGL) gene(s)
OST Gene Name
aglB
OST NCBI Gene ID
OST GenBank Gene Sequence
OST Protein Name
AglB
OST UniProtKB/ SwissProt ID
OST NCBI RefSeq
OST EMBL-CDS
OST UniProtKB Sequence
>tr|D4GYH4|D4GYH4_HALVD Oligosaccharyltransferase AglB OS=Haloferax volcanii (st
rain ATCC 29605 / DSM 3757 / IFO 14742 / NCIMB 2012 / DS2) GN=aglB PE=4 SV=1
MSDEQTKYSPSIAELARDWYHIPVLSTIILVMLWIRLRSYDAFIREGTVFFSGNDAWYHL RQVEYTVRNWPATM
PFDPWTEFPFGRTAGQFGTIYDQLVATAALVVGLGSPSSDLVAKSL LVAPAVFGALTVIPTYLIGKRLGGRLGGL
FGAVILMLLPGTFLQRGLVGFADHNIVEPFF MGFAVLAIMIALTVADREKPVWELVAARDLDALREPLKWSVLAG
VATAIYMWSWPPGILL VGIFGLFLVLKMASDYVRGRSPEHTAFVGAISMTVTGLLMFIPIEEPGFGVTDFGFLQP
L FSLGVALGAVFLAALARWWESNDVDERYYPAVVGGTMLVGIVLFSLVLPSVFDSIARNFL RTVGFSAGAATRT
ISEAQPFLAANVLQSNGQTAVGRIMSEYGFTFFTGALAAVWLVAKPL VKGGNSRKIGYAVGSLALIGVLFLIPAL
PAGIGSALGVEPSLVSLTIVTALIVGAVMQAD YESERLFVLVWAAIITSAAFTQVRFNYYLAVVVAVMNAYLLRE
ALGIDFVGLANVERFDD ISYGQVAAVVIAVLLILTPVLIIPIQLGNGGVSQTAMQASQTGPGTVTQWDGSLTWMQ
NN TPAEGEFGGESNRMEYYGTYEYTDDFDYPDGAYGVMSWWDYGHWITVLGERIPNANPFQG GATEAANYLLAE
DEQQAESVLTSMGDDGEGDQTRYVMVDWQMASTDAKFSAPTVFYDESN ISRSDFYNPMFRLQEQGEQTTVAAASS
LKDQRYYESLMVRLYAYHGSAREASPIVVDWEE RTSADGSTTFRVTPSDGQAVRTFDNMSAAEEYVANDPTSQIG
GIGTFPEERVSALEHYRL VKSSNSSALRSGSYQRSLISEGNTYGLQPQALVPNNPAWVKTFERVPGATVDGSGAP
ANT TVTARVQMRDLTTGTNFTYTQQAQTDADGEFTMTLPYSTTGYDEYGPDNGYTNVSVRAAG GYAFTGPTSVT
GNSTIVSYQAENVAVDEGLVNGAEDGTVQVTLERNEQELDLPGDSSSED SSSEDGTSDGSQTNESASTSTSASVD
ASAVSAAA
OST EC Number (BRENDA)
Characterized Accessory Gene(s)
AglD, AglE, AglI, AglG and AglJ are glycosyltransferases involved in the pentasaccharide assembly. AglJ adds the first sugar of the glycan and AglD adds the last one. All except AglD are encoded in the agl gene island or cluster. aglB is also present in this island.
Characterized by a combination of gene deletion, mass spectroscopy and biochemical characterization.
PGL Additional Links
 
 
Literature
Reference(s)
1) Kaminski, L., Abu-Qarn, M., Guan, Z., Naparstek, S., Ventura, V.V., Raetz, C.R., Hitchen, P.G., Dell, A. and Eichler, J. (2010) AglJ adds the first sugar of the N-linked pentasaccharide decorating the Haloferax volcanii S-layer glycoprotein. J Bacteriol, 192, 5572-5579. [PubMed: 20802039]
2) Kaminski, L. and Eichler, J. (2010) Identification of residues important for the activity of Haloferax volcanii AglD, a component of the archaeal N-glycosylation pathway. Archaea, 2010, 315108. [PubMed: 20585355]
3) Magidovich, H., Yurist-Doutsch, S., Konrad, Z., Ventura, V.V., Dell, A., Hitchen, P.G. and Eichler, J. (2010) AglP is a S-adenosyl-L-methionine-dependent methyltransferase that participates in the N-glycosylation pathway of Haloferax volcanii. Mol Microbiol, 76, 190-199. [PubMed: 20149102]
4) Yurist-Doutsch, S., Magidovich, H., Ventura, V.V., Hitchen, P.G., Dell, A. and Eichler, J. (2010) N-glycosylation in Archaea: on the coordinated actions of Haloferax volcanii AglF and AglM. Mol Microbiol, 75, 1047-1058. [PubMed: 20487296]
5) Yurist-Doutsch, S. and Eichler, J. (2009) Manual annotation, transcriptional analysis, and protein expression studies reveal novel genes in the agl cluster responsible for N glycosylation in the halophilic archaeon Haloferax volcanii. J Bacteriol, 191, 3068-3075. [PubMed: 19251857]
6) Abu-Qarn, M., Giordano, A., Battaglia, F., Trauner, A., Hitchen, P.G., Morris, H.R., Dell, A. and Eichler, J. (2008) Identification of AglE, a second glycosyltransferase involved in N glycosylation of the Haloferax volcanii S-layer glycoprotein. J Bacteriol, 190, 3140-3146. [PubMed: 18310347]
7) Plavner, N. and Eichler, J. (2008) Defining the topology of the N-glycosylation pathway in the halophilic archaeon Haloferax volcanii. J Bacteriol, 190, 8045-8052. [PubMed: 18931126]
8) Yurist-Doutsch, S., Abu-Qarn, M., Battaglia, F., Morris, H.R., Hitchen, P.G., Dell, A. and Eichler, J. (2008) AglF, aglG and aglI, novel members of a gene island involved in the N-glycosylation of the Haloferax volcanii S-layer glycoprotein. Mol Microbiol, 69, 1234-1245. [PubMed: 18631242]
9) Abu-Qarn, M., Yurist-Doutsch, S., Giordano, A., Trauner, A., Morris, H.R., Hitchen, P., Medalia, O., Dell, A. and Eichler, J. (2007) Haloferax volcanii AglB and AglD are involved in N-glycosylation of the S-layer glycoprotein and proper assembly of the surface layer. J Mol Biol, 374, 1224-1236. [PubMed: 17996897]
10) Abu-Qarn, M. and Eichler, J. (2006) Protein N-glycosylation in Archaea: defining Haloferax volcanii genes involved in S-layer glycoprotein glycosylation. Mol Microbiol, 61, 511-525. [PubMed: 16762024]
11) Eichler, J. (2000) Novel glycoproteins of the halophilic archaeon Haloferax volcanii. Arch Microbiol, 173, 445-448. [PubMed: 10896226]
12) Mengele, R. and Sumper, M. (1992) Drastic differences in glycosylation of related S-layer glycoproteins from moderate and extreme halophiles. J Biol Chem, 267, 8182-8185. [PubMed: 1569073]
13) Sumper, M., Berg, E., Mengele, R. and Strobel, I. (1990) Primary structure and glycosylation of the S-layer protein of Haloferax volcanii. J Bacteriol, 172, 7111-7118. [PubMed: 2123862]
Additional Comments
Based on analogy to H. salinarum and presence of similar glycans, the S layer protein in H. volcanii that exhibits a cluster of threonine residues (yet uncharacterized) at C terminus of the protein nearby hydrophobic membrane anchor has been speculated to be glycosylated with glucosyl-(1-2)-galactose disaccharides. The probable glycosylated cluster sequence has been attributed to act as a spacer between membrane anchor and extracellular domain akin to periplasmic space in Gram-negative bacteria.
Year of Identification
1990
Year of Validation
1992
 
 
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