ProGP166

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ProGP ID ProGP166
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 glycopeptide
UniProtKB/SwissProt ID B0R8E4
NCBI RefSeq WP_012289536.1
EMBL-CDSAAG20702.1
UniProtKB Sequence >sp|B0R8E4|CSG_HALS3 Cell surface glycoprotein OS=Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1) GN=csg PE=1 SV=1 MTDTTGKLRAVLLTALMVGSVIGAGVAFTGGAAAANASDLNDYQRFNENTNYTYSTASED GKTEGSVASGATIFQGEEDVTFRKLDNEKEVSPATLSRTGGSDEGVPLQMPIPEDQSTGS YDSNGPDNDEADFGVTVQSPSVTMLEVRNNADNDVTGGVLNTQQDESSIAVDYNYYAAED LELTVEDEDGLDVTDEILAADQSGGAYEDGTGNNGPNTLRFDIDPNNVDAGDYTVSVEGV EDLDFGDATESASVTISSSNKASLNLAEDEVVQGANLKYTIENSPEGNYHAVTIDSSDFR DSSSGADAAKVMRSVGDTVDTGLVVDNDSTTEIVDDYENTSISDVDYAYAIVEIDDGNGV GSIETQYLDDSSADIDLYPASDTEDAPDYVNSNEELTNGSALDGVSTDDDTDFDVTQGDI TLDNPTGAYVVGSEVDINGTANEGTDDVVLYARDNNDFELVTVDGEKSIEVDSDDTFEEE DITLSDGDKGGDDILGLPGTYRLGIIAKSDAVNSSGGVKDNIDTSDFNQGVSSTSSIRVT DTELTASFETYNGQVADDDNQIDVEGTAPGKDNVAAIIIGSRGKVKFQSISVDSDDTFDE EDIDISELRQGSASAHILSSGRDGKFGEDTANSISDLEDEVGNYTSGSPTGDQIRDRILS NTVDDTASDDLIVTQQFRLVDGLTTIEATEGGEAGGSLTVMGTTNRKADDNTITVELLQG DASIEINSTDEWNSDGQWSVDVPLSNVEPGNYTVEADDGDNTDRQNVEIVEELEEPDQTT VDQPENNQTMTTTMTETTTETTTEMTTTQENTTENGSEGTSDGESGGSIPGFGVGVALVA VLGAALLALRQN
Sequence length 852 AA
Subcellular LocationSurface
Glycosylation Status
Glycosylation Type N- (Asn) linked
Experimentally Validated Glycosite(s) in Full Length ProteinN2 [Replacement of the Ser residue at the consensus sequence by Val, Leu, and Asn, did not abolish glycosylation of Asn-2. However, replacing Ser-481 in the sequence Asn-Ser-Ser for Val prevented glycosylation of Asn-479.]
Experimentally Validated Glycosite(s ) in Mature ProteinN2
Glycosite(s) Annotated Protein Sequence AN*(2)AVDLNDYQR
(csg mutants with Val, Leu or Asn at 4th position were created)
Technique(s) used for Glycosylation DetectionEdman degradation using an automated gas phase sequencer.
Technique(s) used for Glycosylated Residue(s) Detection Edman degradation using gas phase sequencing (known residues are mutated).
Glycan Information
Glycan Annotation Same sugar pattern like that of the wild-type is present. Galacturonic acid, 3-O-methyl-galacturonic acid, galactose, N-acetylglucosamine, and N-acetylgalactosamine have been observed.
Technique(s) used for Glycan Identification Gas chromatographic analysis of pentafluoropropionyl-methyl-glycosides.
Protein Glycosylation linked (PGL) gene(s)
OST Gene NameAglB/STT3 subunit
OST ProGT IDProGT82
Accessory Gene(s)Progt IDProGT82.1-ProGT82.10
Additional CommentEngineered glycopeptide.
It has been suggested that there may be two different N-glycosyltransferases in H.halobium, one of which does not use the typical consensus sequence Asn-Xaa-Ser/Thr necessary for all other N-glycosyltransferases.
Synthetic oligonucleotides corresponding to nucleotide 100–132 of the csg open reading frame were used to produce the peptides.
While the N-glycosyltransferase acting at N479 is a conventional one requiring the hydroxyamino acid in the N-glycosylation sequon, the transferase catalyzing glycosylation at N2 is not dependent on a hydroxyamino acid that follows the next but one to Asn.
Literature
Year of Identification1998
Year of Identification Month Wise1998.12.01
Year of Validation 1998
ReferenceZeitler, R., Hochmuth, E., Deutzmann, R. and Sumper, M. (1998) Exchange of Ser-4 for Val, Leu or Asn in the sequon Asn-Ala-Ser does not prevent N-glycosylation of the cell surface glycoprotein from Halobacterium halobium. Glycobiology, 8, 1157-1164.
AuthorZeitler, R., Hochmuth, E., Deutzmann, R. and Sumper, M
Research GroupDepartment of Biochemistry, University of Regensburg, Universit atsstrasse 31, 93040 Regensburg, Germany.
Corresponding Author Sumper, M
ContactDepartment of Biochemistry, University of Regensburg, Universit atsstrasse 31, 93040 Regensburg, Germany.