ProGP3

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ProGP ID ProGP3
Validation Status Characterized
Organism Information
Organism NameHalobacterium salinarum (halobium) R1M1/NRC-1
Domain Archaea
Classification Family: Halobacteriaceae
Order: Halobacteriales
Class: Halobacteria or Halomebacteria
Division or phylum: "Euryarchaeota"
Taxonomic ID (NCBI) 64091
Genome Sequence(s)
GenBank AE004437.1
EMBL AE004437
Gene Information
Gene Namecsg (VNG_2679G)
NCBI Gene ID 1449008
GenBank Gene Sequence 1449008
Protein Information
Protein NameS layer glycoprotein
UniProtKB/SwissProt ID P0DME1
NCBI RefSeq WP_012289536.1
EMBL-CDSAE004437.1
UniProtKB Sequence >sp|P0DME1|CSG_HALSA Cell surface glycoprotein OS=Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) GN=csg PE=3 SV=1 MTDTTGKLRAVLLTALMVGSVIGAGVAFTGGAAAANASDLNDYQRFNENTNYTYSTASED GKTEGSVASGATIFQGEEDVTFRKLDNEKEVSPATLSRTGGSDEGVPLQMPIPEDQSTGS YDSNGPDNDEADFGVTVQSPSVTMLEVRNNADNDVTGGVLNTQQDESSIAVDYNYYAAED LELTVEDEDGLDVTDEILAADQSGGAYEDGTGNNGPNTLRFDIDPNNVDAGDYTVSVEGV EDLDFGDATESASVTISSSNKASLNLAEDEVVQGANLKYTIENSPEGNYHAVTIDSSDFR DSSSGADAAKVMRSVGDTVDTGLVVDNDSTTEIVDDYENTSISDVDYAYAIVEIDDGNGV GSIETQYLDDSSADIDLYPASDTEDAPDYVNSNEELTNGSALDGVSTDDDTDFDVTQGDI TLDNPTGAYVVGSEVDINGTANEGTDDVVLYARDNNDFELVTVDGEKSIEVDSDDTFEEE DITLSDGDKGGDDILGLPGTYRLGIIAKSDAVNSSGGVKDNIDTSDFNQGVSSTSSIRVT DTELTASFETYNGQVADDDNQIDVEGTAPGKDNVAAIIIGSRGKVKFQSISVDSDDTFDE EDIDISELRQGSASAHILSSGRDGKFGEDTANSISDLEDEVGNYTSGSPTGDQIRDRILS NTVDDTASDDLIVTQQFRLVDGLTTIEATEGGEAGGSLTVMGTTNRKADDNTITVELLQG DASIEINSTDEWNSDGQWSVDVPLSNVEPGNYTVEADDGDNTDRQNVEIVEELEEPDQTT VDQPENNQTMTTTMTETTTETTTEMTTTQENTTENGSEGTSDGESGGSIPGFGVGVALVA VLGAALLALRQN
Sequence length 852 AA
Subcellular LocationSurface
Function In Archaea, which do not possess other cell wall components, the S-layer has been implicated in the maintaineance of 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) N36, N339, N398, N438, N513, N643, N727, N751, N787, N811, N815 (N36, N513 and N643 were confirmed glycosylated directly by glycopeptide sequence analysis , the reference no. 2 mentions that ten sulfated saccharides are N-linked to the protein imlplying that most or all sites are glycosylated.)
Experimentally Validated Glycosite(s ) in Mature ProteinN2, N305, N364, N404, N479, N609, N693, N717, N753, N777, N781
Glycosite(s) Annotated Protein Sequence >sp|P0DME1|CSG_HALSA Cell surface glycoprotein OS=Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) GN=csg PE=3 SV=1 MTDTTGKLRAVLLTALMVGSVIGAGVAFTGGAAAAN*(36)ASDLNDYQRFNENTNYTYSTASED GKTEGSVASGATIFQGEEDVTFRKLDNEKEVSPATLSRTGGSDEGVPLQMPIPEDQSTGS YDSNGPDNDEADFGVTVQSPSVTMLEVRNNADNDVTGGVLNTQQDESSIAVDYNYYAAED LELTVEDEDGLDVTDEILAADQSGGAYEDGTGNNGPNTLRFDIDPNNVDAGDYTVSVEGV EDLDFGDATESASVTISSSNKASLNLAEDEVVQGANLKYTIENSPEGNYHAVTIDSSDFR DSSSGADAAKVMRSVGDTVDTGLVVDNDSTTEIVDDYEN*(339)TSISDVDYAYAIVEIDDGNGV GSIETQYLDDSSADIDLYPASDTEDAPDYVNSNEELTN*(398)GSALDGVSTDDDTDFDVTQGDI TLDNPTGAYVVGSEVDIN*(438)GTANEGTDDVVLYARDNNDFELVTVDGEKSIEVDSDDTFEEE DITLSDGDKGGDDILGLPGTYRLGIIAKSDAVN*(513)SSGGVKDNIDTSDFNQGVSSTSSIRVT DTELTASFETYNGQVADDDNQIDVEGTAPGKDNVAAIIIGSRGKVKFQSISVDSDDTFDE EDIDISELRQGSASAHILSSGRDGKFGEDTANSISDLEDEVGN*(643) YTSGSPTGDQIRDRILS NTVDDTASDDLIVTQQFRLVDGLTTIEATEGGEAGGSLTVMGTTNRKADDNTITVELLQG DASIEIN*(727)STDEWNSDGQWSVDVPLSNVEPGN*(751)YTVEADDGDNTDRQNVEIVEELEEPDQTT VDQPENN*(787)QTMTTTMTETTTETTTEMTTTQEN*(811)TTEN*(815)GSEGTSDGESGGSIPGFGVGVALVA VLGAALLALRQN
Sequence Around Glycosites (21 AA) VAFTGGAAAANASDLNDYQRF
STTEIVDDYENTSISDVDYAY
DYVNSNEELTNGSALDGVSTD
AYVVGSEVDINGTANEGTDDV
LGIIAKSDAVNSSGGVKDNID
SISDLEDEVGNYTSGSPTGDQ
LLQGDASIEINSTDEWNSDGQ
DVPLSNVEPGNYTVEADDGDN
DQTTVDQPENNQTMTTTMTET
TTTEMTTTQENTTENGSEGTS
MTTTQENTTENGSEGTSDGES
Glycosite Sequence Logo
Technique(s) used for Glycosylation DetectionPeriodate-arsenite-Schiff reagent staining and carbohydrate analysis using GC.
Technique(s) used for Glycosylated Residue(s) Detection Glycopeptide sequencing
Protein Glycosylation- Implication It is the pattern and the chemical nature of the N-linked saccharides which exhibits a drastic change at the transition from moderate to extreme halophily. This different pattern of glycosylation (sulfated glucuronic acids and a repeating unit saccharide) introduces at least 120 additional negative charges into the glycoprotein. The protruding highly negatively charged loops are required for stabilization in high salt concentrations. Thus, the sulfated repeating unit saccharide is required for stabilization of the rod shaped morphology.
Glycan Information
Glycan Annotation Linkages: βGalNAc- Asn, Glc-Asn, Gal-Thr.
Total carbohydrate content is approximately 10 to 12% of 200kDa S layer glycoprotein.
N glycosylated (at position N2) with GlcNAc-linked repeating (10-15 repeats) sulfated pentasaccharide and with sulphated oligosaccharides: (GlcA(OSO3-)-[β1→4GlcA(OSO3-)]2-β1→4Glc-Asn) at ten other poistions.
Abut 20 neutral di/ tri- saccharides α-D-Glc-(1→2)-Gal-(1→ or (uronic acid, glucose)-galactose are O-glycosidically attached to clustered threonine residues (14) adjacent to the TM domain at the C terminus but precise position of O glycosylated residues is not known.
Technique(s) used for Glycan Identification GC-MS (gas chromatography-mass spectrometry) analysis of peracetylated alditols.
Protein Glycosylation linked (PGL) gene(s)
OST Gene NameAglB/STT3 subunit
OST ProGT IDProGT82
Additional CommentFirst prokaryotic glycoprotein that was charcterized experimentally for the site of glycosylation as well as glycan attached. The features unique to N glycosylation in H salinarium are: the majority of glycans are linked via glucose instead of GlcNAc or GalNAc to the Asn in protein. Presence of sulfated oligosaccharides that bind to a C60-dolichol monophosphate carrier lipid. Protein associated glycans differ mainly in terminal sugars. S layer proteins of H salinarium and H. volcanii are the examples of a lesser understood and rare type of glycosylation namely O glycosylation in Archaea. A cluster of 14 threonine residues (yet uncharacterized) present at hydrophobic C terminus membrane anchor has also been reported glycosylated with glucosylgalactose disaccharides in S layer glycoprotein of H salinarium. Bacitracin inhibits growth of Halobacteria.
Sequon features: excluding the only unique Asn-GalNAc site, all sequon sequences are preceded by 1 or even 2 negatively charged amino acid residues.
Literature
Year of Identification1974
Year of Identification Month Wise1974
Year of Validation 1987
ReferenceMengele, 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.
AuthorMengele, R. and Sumper, M
Research GroupChair of Biochemistry, University of Regensburg, Federal Republic of Germany
Corresponding Author Sumper, M
ContactChair of Biochemistry, University of Regensburg, Federal Republic of Germany
Reference Lechner, J. and Sumper, M. (1987) The primary structure of a procaryotic glycoprotein. Cloning and sequencing of the cell surface glycoprotein gene of halobacteria. J Biol Chem, 262, 9724-9729. [PubMed: 3036870]
Author Lechner, J. and Sumper, M.
Research GroupInstitute of Biochemistry, Genetics and Microbiology, Uniuersitat Regensburg, Uniuersitatsstrasse 31, 8400 Regensburg, Federal Republic of Germany
Corresponding Author Sumper, M.
ContactInstitute of Biochemistry, Genetics and Microbiology, Uniuersitat Regensburg, Uniuersitatsstrasse 31, 8400 Regensburg, Federal Republic of Germany
Reference Lechner, J. and Sumper, M. (1987) The primary structure of a procaryotic glycoprotein. Cloning and sequencing of the cell surface glycoprotein gene of halobacteria. J Biol Chem, 262, 9724-9729. [PubMed: 3036870]
Author Lechner, J. Sumper, M.
Research GroupInstitute of Biochemistry, Genetics and Microbiology, Uniuersitat Regensburg, Uniuersitatsstrasse 31, 8400 Regensburg, Federal Republic of Germany
Corresponding Author Sumper, M.
ContactInstitute of Biochemistry, Genetics and Microbiology, Uniuersitat Regensburg, Uniuersitatsstrasse 31, 8400 Regensburg, Federal Republic of Germany
Reference Paul, G., Lottspeich, F. and Wieland, F. (1986) Asparaginyl-N-acetylgalactosamine. Linkage unit of halobacterial glycosaminoglycan. J Biol Chem, 261, 1020-1024. [PubMed: 3944078]
Author Paul, G., Lottspeich, F. Wiel
Research GroupInstitute for Biochemistry, University of Regensburg, Universitatsstraje 31, 8400 Regensburg andMax Planck Institute of Biochemistry, Gene Center, At the Klopferspitz, 8033 Martinsried, Federal Republic of Germany
ContactInstitute for Biochemistry, University of Regensburg, Universitatsstraje 31, 8400 Regensburg andMax Planck Institute of Biochemistry, Gene Center, At the Klopferspitz, 8033 Martinsried, Federal Republic of Germany
Reference Lechner, J., Wieland, F. and Sumper, M. (1985) Transient methylation of dolichyl oligosaccharides is an obligatory step in halobacterial sulfated glycoprotein biosynthesis. J Biol Chem, 260, 8984-8989. [PubMed: 4019460]
Author Lechner, J., Wieland, F. and Sumper, M.
Research GroupDepartment of Biochemistry, University of Regensburg, Federal Republic of Germany
Corresponding Author Sumper, M.
ContactDepartment of Biochemistry, University of Regensburg, Federal Republic of Germany
Reference Wieland, F., Paul, G. and Sumper, M. (1985) Halobacterial flagellins are sulfated glycoproteins. J Biol Chem, 260, 15180-15185. [PubMed: 3934156]
AuthorWieland, F., Paul, G. and Sumper, M.
Research GroupInstitute of Biochemistry, Genetics and Microbiology, University of Regensburg, 8400 Regensburg, Federal Republic of Germany
Corresponding Author Sumper, M.
ContactInstitute of Biochemistry, Genetics and Microbiology, University of Regensburg, 8400 Regensburg, Federal Republic of Germany
Reference Wieland, F., Heitzer, R. and Schaefer, W. (1983) Asparaginylglucose: Novel type of carbohydrate linkage. Proc Natl Acad Sci U S A, 80, 5470-5474. [PubMed: 16593364]
Author Wieland, F., Heitzer, R. and Schaefer, W
Research GroupInstitute of Biochemistry, University of Regensburg, D-8400 Regensburg, Federal Republic of Germany.
Corresponding Author Schaefer, W
ContactInstitute of Biochemistry, University of Regensburg, D-8400 Regensburg, Federal Republic of Germany.
Reference Mescher, M.F. and Strominger, J.L. (1976) Purification and characterization of a prokaryotic glucoprotein from the cell envelope of Halobacterium salinarium. J Biol Chem, 251, 2005-2014. [PubMed: 1270419]
Author Mescher, M.F. and Strominger, J.L
Research GroupBiological Laboratories, Harvard University, Cambridge, Massachusetts 02138
Corresponding Author Strominger, J.L.
ContactBiological Laboratories, Harvard University, Cambridge, Massachusetts 02138
Reference Mescher, M.F., Strominger, J.L. and Watson, S.W. (1974) Protein and carbohydrate composition of the cell envelope of Halobacterium salinarium. J Bacteriol, 120, 945-954. [PubMed: 4455689]
Author Mescher, M.F., Strominger, J.L. and Watson, S.W.
Research GroupThe Biological Laboratories, Harvard University, Cambridge, Massachusetts 02138, and Woods Hole Oceanographic Institution, Woods Hole, Massachusetts 02543
Corresponding Author Watson, S.W
ContactThe Biological Laboratories, Harvard University, Cambridge, Massachusetts 02138, and Woods Hole Oceanographic Institution, Woods Hole, Massachusetts 02543
Reference Wieland, F., Dompert, W., Bernhardt, G. and Sumper, M. (1980) Halobacterial glycoprotein saccharides contain covalently linked sulphate. FEBS Lett, 120, 110-114. [PubMed: 7439381]
Author Wieland, F., Dompert, W., Bernhardt, G. and Sumper, M.
Research GroupInstitute of Biochemistry, Cenetics and Microbiology, Biochemistry I, Universitiit, 8400 Regensburg, FRG
Corresponding Author Sumper, M.
ContactInstitute of Biochemistry, Cenetics and Microbiology, Biochemistry I, Universitiit, 8400 Regensburg, FRG