ProGP71

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ProGP ID ProGP71
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 Sequence(s)
GenBank CP001956.1
EMBL M62816
Gene Information
Gene Namecsg
NCBI Gene ID 8924493
GenBank Gene Sequence 8924493
Protein Information
Protein NameS-lyer 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
Experimentally Validated Glycosite(s ) in Mature ProteinN13, 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)KTIQSGDRVFLGE EISTDAGLGASNPLLTGTAGNSEGVSLDLSSPIPQTTENQPLGTYDVDGSGSATTPN*(117)VTL LAPRITDSEILTSSGGDVTGSAISSSDAGNLYVNADYNYESAEKVEVTVEDPSGTDITNE VLSGTDTFVDDGSIGSTSSTGGGVGIDMSDQDAGEYTIILEGAEDLDFGDATETMTLTIS SQDEIGIELDSESVTQGTDVQYTVTNGIDGNEHVVAMDLSDLQNDATTEQAKEVFRNIGD TSEVGIAN*(308)SSATN*(313)TSGSSTGPTVETADIAYAVVEIDGASAVGGIETQYLDDSEVDLEVYD AGVSATAAVGQDATNDITLTIEEGGTTLSSPTGQYVVGSEVDINGTATSSDSVAIYVRDD GDWQLLEIGGDNEISVDSDDTFEEEDIALSGLSGDGSSILSLTGTYRIGVIDASDADVGG DGSVDDSLTTSEFTSGVSSSNSIRVTDQALTGQFTTINGQVAPVETGTVDIN*(532)GTASGANS VLVIFVDERGNVNYQEVSVDSDGTYDEDDITVGLTQGRVTAHILSVGRDSAIGDGSLPSG PSNGATLNDLTGYLDTLDQNNNNGEQINELIASETVDETASDDLIVTETFRLAESSTSID SIYPDAAEAAGINPVATGETMVIAGSTNLKPDDNTISIEVTNEDGTSVALEDTDEWNNDG QWMVEIDTTDFETGTFTVEADDGDNTDTVNVEVVSEREDTTTSSDNATDTTTTTDGPTET TTTAEPTETTEEPTEETTTSSNTPGFGIAVALVALVGAALLALRREN
Sequence Around Glycosites (21 AA) GNLDADSESFNKTIQSGDRVF
VDGSGSATTPNVTLLAPRITD
IGDTSEVGIANSSATNTSGSS
EVGIANSSATNTSGSSTGPTV
APVETGTVDINGTASGANSVL
Glycosite Sequence 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. 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.
Protein Glycosylation linked (PGL) gene(s)
OST Gene NameAglB
OST ProGT IDProGT13
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
Accessory Gene(s)Progt IDProGT13.1 ProGT13.22
Literature
Additional CommentBased on analogy to H. salinarium and presence of similar glycans, the S layer protein in H. volcanni 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 Identification1990
Year of Identification Month Wise1990.12.25
Year of Validation 1992
Reference 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]
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.
Reference1) 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]
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.
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.
Reference 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]
Author Eichler, J.
Research GroupDepartment of Life Sciences, Ben Gurion University, Beersheva, Israel.
Corresponding Author Magidovich, H., Yurist-Doutsch, S., Konrad, Z., Ventura, V.V., Dell, A., Hitchen, P.G. Eichler, J.
ContactDepartment of Life Sciences, Ben Gurion University, Beersheva, 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. 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 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]
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.
Reference 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]
Author Kaminski, L. 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.
Reference 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]
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.
Reference 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]
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.