ProGP71 (S-layer glycoprotein)

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ProGP ID ProGP71 (S-layer glycoprotein)
Validation Status Characterized
Organism Information
Organism NameHaloferax volcanii DS2
Domain Archaea
Classification Family: Halobacteriaceae
Order: Halobacteriales
Class: Halobacteria or Halomebacteria
Division or phylum: "Euryarchaeota"
Taxonomic ID (NCBI) 2246
Genome Information
GenBank M62816
EMBL M62816
Gene Information
Gene Namecsg
NCBI Gene ID 8924493
GenBank Gene Sequence NC_013967
Protein Information
Protein NameS-layer glycoprotein
UniProtKB/SwissProt ID P25062
NCBI RefSeq YP_003536097.1
EMBL-CDSAAA72996.1
UniProtKB Sequence >sp|P25062|CSG_HALVO Cell surface glycoprotein OS=Halobacterium volcanii GN=csg PE=1 SV=1 MTKLKDQTRAILLATLMVTSVFAGAIAFTGSAAAERGNLDADSESFNKTIQSGDRVFLGE EISTDAGLGASNPLLTGTAGNSEGVSLDLSSPIPQTTENQPLGTYDVDGSGSATTPNVTL LAPRITDSEILTSSGGDVTGSAISSSDAGNLYVNADYNYESAEKVEVTVEDPSGTDITNE VLSGTDTFVDDGSIGSTSSTGGGVGIDMSDQDAGEYTIILEGAEDLDFGDATETMTLTIS SQDEIGIELDSESVTQGTDVQYTVTNGIDGNEHVVAMDLSDLQNDATTEQAKEVFRNIGD TSEVGIANSSATNTSGSSTGPTVETADIAYAVVEIDGASAVGGIETQYLDDSEVDLEVYD AGVSATAAVGQDATNDITLTIEEGGTTLSSPTGQYVVGSEVDINGTATSSDSVAIYVRDD GDWQLLEIGGDNEISVDSDDTFEEEDIALSGLSGDGSSILSLTGTYRIGVIDASDADVGG DGSVDDSLTTSEFTSGVSSSNSIRVTDQALTGQFTTINGQVAPVETGTVDINGTASGANS VLVIFVDERGNVNYQEVSVDSDGTYDEDDITVGLTQGRVTAHILSVGRDSAIGDGSLPSG PSNGATLNDLTGYLDTLDQNNNNGEQINELIASETVDETASDDLIVTETFRLAESSTSID SIYPDAAEAAGINPVATGETMVIAGSTNLKPDDNTISIEVTNEDGTSVALEDTDEWNNDG QWMVEIDTTDFETGTFTVEADDGDNTDTVNVEVVSEREDTTTSSDNATDTTTTTDGPTET TTTAEPTETTEEPTEETTTSSNTPGFGIAVALVALVGAALLALRREN
Sequence length 827 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, (O- (Thr) linked residues not known)
Experimentally Validated Glycosite(s) in Full Length Protein(Signal peptide: 1-34) N47, N117, N308, N313, N532 and N766
Experimentally Validated Glycosite(s ) in Mature ProteinN13, N83, N274, N279, N498 and N732
Glycosite(s) Annotated Protein Sequence >sp|P25062|CSG_HALVO Cell surface glycoprotein OS=Halobacterium volcanii GN=csg PE=1 SV=1 MTKLKDQTRAILLATLMVTSVFAGAIAFTGSAAAERGNLDADSESFN*(47)KTIQSGDRVFLGE EISTDAGLGASNPLLTGTAGNSEGVSLDLSSPIPQTTENQPLGTYDVDGSGSATTPN*(117)VTL LAPRITDSEILTSSGGDVTGSAISSSDAGNLYVNADYNYESAEKVEVTVEDPSGTDITNE VLSGTDTFVDDGSIGSTSSTGGGVGIDMSDQDAGEYTIILEGAEDLDFGDATETMTLTIS SQDEIGIELDSESVTQGTDVQYTVTNGIDGNEHVVAMDLSDLQNDATTEQAKEVFRNIGD TSEVGIAN*(308)SSATN*(313)TSGSSTGPTVETADIAYAVVEIDGASAVGGIETQYLDDSEVDLEVYD AGVSATAAVGQDATNDITLTIEEGGTTLSSPTGQYVVGSEVDINGTATSSDSVAIYVRDD GDWQLLEIGGDNEISVDSDDTFEEEDIALSGLSGDGSSILSLTGTYRIGVIDASDADVGG DGSVDDSLTTSEFTSGVSSSNSIRVTDQALTGQFTTINGQVAPVETGTVDIN*(532)GTASGANS VLVIFVDERGNVNYQEVSVDSDGTYDEDDITVGLTQGRVTAHILSVGRDSAIGDGSLPSG PSNGATLNDLTGYLDTLDQNNNNGEQINELIASETVDETASDDLIVTETFRLAESSTSID SIYPDAAEAAGINPVATGETMVIAGSTNLKPDDNTISIEVTNEDGTSVALEDTDEWNNDG QWMVEIDTTDFETGTFTVEADDGDNTDTVNVEVVSEREDTTTSSDN*(766)ATDTTTTTDGPTET TTTAEPTETTEEPTEETTTSSNTPGFGIAVALVALVGAALLALRREN
Sequence Around Glycosites (21 AA) GNLDADSESFNKTIQSGDRVF
VDGSGSATTPNVTLLAPRITD
IGDTSEVGIANSSATNTSGSS
EVGIANSSATNTSGSSTGPTV
APVETGTVDINGTASGANSVL
EREDTTTSSDNATDTTTTTDG
ProGP Web Logo
Technique(s) used for Glycosylation DetectionDeglycosylation 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 Sulfoquinovose-hexose-based glycan, N-linked via a chitobiose core.
A trisaccharide corresponding to glucuronic acid (GlcA)-β1,4-GlcA-β1,4-glucose-β1-Asn, a tetrasaccharide corresponding to methyl-O-4-GlcA-β-1,4-galacturonic acid-α1,4-GlcA-β1,4-glucose-β1-Asn, and a pentasaccharide corresponding to hexose-1,2-[methyl-O-4-]GlcA-β-1,4-galacturonic acid-α1,4-GlcA-β1,4-glucose-β1-Asn.
The hexose at the non-reducing end of the pentasaccharide is a mannose.
In high salt (3.4 M NaCl) conditions, N13 and N83 are modified by a pentasaccharide while dolicholphosphate is modified by a tetrasaccharide comprising the first four pentasaccharide residues.
Cells grown at low salinity (1.75 M NaCl) possess dolichol phosphate and N498 residue (in S-layer glycoprotein) modified by a distinct tetrasaccharide comprising a sulfated hexose, two hexoses and a rhamnose.
A novel glycan, N-acetylglucosamine2-hexose2-(sulfoquinovose-hexose)6, is bound to Asn-732.
Technique(s) used for Glycan Identification LC-ESI-MS, MALDI-TOF MS, Nano-LC-MS/MS and NMR
Protein Glycosylation linked (PGL) gene(s)
OST Gene NameAglB
OST ProGT IDProGT15 (AglB)
Literature
ReferenceKandiba L, Lin CW, Aebi M, Eichler J, Guerardel Y. (2016) Structural characterization of the N-linked pentasaccharide decorating glycoproteins of the halophilic archaeon Haloferax volcanii. Glycobiology, 26(7), 745-756. [PubMed: 26863921]
AuthorKandiba L, Lin CW, Aebi M, Eichler J, Guerardel Y.
Research Group1 Department of Life Sciences, Ben Gurion University of the Negev, PO Box 653, Beersheva 84105, Israel. 2 Institute of Microbiology, ETH Zurich, CH-8093 Zurich, Switzerland. 3 Université de Lille, CNRS, UMR 8576-UGSF-Unité de Glycobiologie Structurale et Fonctionnelle, F 59000 Lille, France.
Corresponding Author Eichler J, Guerardel Y.
ContactDepartment of Life Sciences, Ben Gurion University of the Negev, PO Box 653, Beersheva 84105, Israel.
ReferenceParente J, Casabuono A, Ferrari MC, Paggi RA, De Castro RE, Couto AS, Giménez MI. (2014) A rhomboid protease gene deletion affects a novel oligosaccharide N-linked to the S-layer glycoprotein of Haloferax volcanii. J Biol Chem., 289(16), 11304-17. [PubMed: 24596091]
AuthorParente J, Casabuono A, Ferrari MC, Paggi RA, De Castro RE, Couto AS, Giménez MI.
Research GroupFrom the ‡Centro de Investigación en Hidratos de Carbono, Departamento de Química Orgánica, Facultad de Ciencias, Exactas y Naturales, Universidad de Buenos Aires, Pabellón II, Ciudad Universitaria, Buenos Aires, Argentina and the §Instituto de Investigaciones Biológicas, Universidad Nacional de Mar del Plata-Consejo Nacional de Investigaciones Científicas y Técnicas, Funes 3250 4to nivel, 7600 Mar del Plata, Provincia de Buenos Aires, Argentina 3 To whom correspondence should be addressed. Tel.: 54-223-475-3030; Fax: 54-223-472-4143; E-mail: ra.ude.pdm@nemigim.
Corresponding Author Giménez MI.
ContactTo whom correspondence should be addressed. Tel.: 54-223-475-3030; Fax: 54-223-472-4143; E-mail: ra.ude.pdm@nemigim.
ReferenceGuan Z, Naparstek S, Calo D, Eichler J. (2012) Protein glycosylation as an adaptive response in Archaea: growth at different salt concentrations leads to alterations in Haloferax volcanii S-layer glycoprotein N-glycosylation. Environ Microbiol., 14(3), 743-53. [PubMed: 22029420]
AuthorGuan Z, Naparstek S, Calo D, Eichler J.
Research Group1Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA 2Department of Life Sciences, Ben Gurion University, Beersheva 84105, Israel *For correspondence. li.ca.ugb@relhciej; Tel. (+972) 8646 1343; Fax (+972) 8647 9175
Corresponding Author Eichler J.
ContactDepartment of Life Sciences, Ben Gurion University, Beersheva 84105, Israel. Email: li.ca.ugb@relhciej; Tel. (+972) 8646 1343; Fax (+972) 8647 9175
ReferenceKaminski, 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]
Author Kaminski, L., Abu-Qarn, M., Guan, Z., Naparstek, S., Ventura, V.V., Raetz, C.R., Hitchen, P.G., Dell, A. and Eichler, J.
Research GroupDept. of Life Sciences, Ben Gurion University, Beersheva 84105, Israel.
Corresponding Author Eichler, J.
ContactDept. of Life Sciences, Ben Gurion University, Beersheva 84105, Israel.
ReferenceKaminski, 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]
Author Kaminski, L. and Eichler, J
Research GroupDepartment of Life Sciences, Ben Gurion University, Beersheva, Israel.
Corresponding Author Eichler, J.
ContactDepartment of Life Sciences, Ben Gurion University, Beersheva, Israel.
ReferenceMagidovich, 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]
Author Magidovich, H., Yurist-Doutsch, S., Konrad, Z., Ventura, V.V., Dell, A., Hitchen, P.G. Eichler, J.
Research GroupDepartment of Life Sciences, Ben Gurion University, Beersheva, Israel.
Corresponding Author Eichler, J.
ContactDepartment of Life Sciences, Ben Gurion University, Beersheva, Israel.
ReferenceYurist-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]
AuthorYurist-Doutsch, S., Magidovich, H., Ventura, V.V., Hitchen, P.G., Dell, A. and Eichler, J
Research GroupDepartment of Life Sciences, Ben Gurion University of the Negev, Beersheva 84105, Israel.
Corresponding Author Eichler, J.
ContactDepartment of Life Sciences, Ben Gurion University of the Negev, Beersheva 84105, Israel.
ReferenceYurist-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]
Author Yurist-Doutsch, S. Eichler, J.
Research GroupDept. of Life Sciences, Ben Gurion University, P.O. Box 653, Beersheva 84105, Israel
Corresponding Author Eichler, J.
ContactDept. of Life Sciences, Ben Gurion University, P.O. Box 653, Beersheva 84105, Israel
Reference 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]
Author Wieland, F., Heitzer, R. and Schaefer, W.
Research GroupDepartment of Life Sciences, Ben Gurion University, P.O. Box 653, Beersheva 84105, Israel.
Corresponding Author Eichler, J
ContactDepartment of Life Sciences, Ben Gurion University, P.O. Box 653, Beersheva 84105, Israel.
Reference 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]
Author Yurist-Doutsch, S., Abu-Qarn, M., Battaglia, F., Morris, H.R., Hitchen, P.G., Dell, A. and Eichler, J.
Research GroupDepartment of Life Sciences, Ben Gurion University, Beersheva 84105, Israel.
Corresponding Author Eichler, J.
ContactDepartment of Life Sciences, Ben Gurion University, Beersheva 84105, Israel.
ReferencePlavner, 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]
Author Plavner, N. and Eichler, J.
Research GroupDepartment of Life Sciences, Ben Gurion University, Beersheva 84105, Israel.
Corresponding Author Eichler, J.
ContactDepartment of Life Sciences, Ben Gurion University, Beersheva 84105, Israel.
ReferenceAbu-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]
Author Abu-Qarn, M., Yurist-Doutsch, S., Giordano, A., Trauner, A., Morris, H.R., Hitchen, P., Medalia, O., Dell, A. and Eichler, J.
Research GroupDepartment of Life Sciences, Ben Gurion University, Beersheva 84105, Israel.
Corresponding Author Eichler, J
ContactDepartment of Life Sciences, Ben Gurion University, Beersheva 84105, Israel.
ReferenceAbu-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]
AuthorAbu-Qarn, M. and Eichler, J.
Research GroupDepartment of Life Sciences, Ben Gurion University, Beersheva 84105, Israel.
Corresponding Author Eichler, J.
ContactDepartment of Life Sciences, Ben Gurion University, Beersheva 84105, Israel.
Reference Eichler, J. (2000) Novel glycoproteins of the halophilic archaeon Haloferax volcanii. Arch Microbiol, 173, 445-448. [PubMed: 10896226]
Author Eichler, J.
Research GroupDepartment of Life Sciences and The Doris and Bertie Black Center for Bioenergetics in Life Sciences, Ben Gurion University, Beersheva, Israel.
Corresponding Author Eichler, J.
ContactDepartment of Life Sciences and The Doris and Bertie Black Center for Bioenergetics in Life Sciences, Ben Gurion University, Beersheva, Israel.
Reference 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]
AuthorMengele, R. and Sumper, M.
Research GroupLehrstuhl Biochemie I, Universität Regensburg, Federal Republic of Germany.
Corresponding Author Sumper, M.
ContactLehrstuhl Biochemie I, Universität Regensburg, Federal Republic of Germany.