ProGP165 (S-layer glycopeptide)
Home -> ProGPdb -> Search ProGP -> Display data
| ProGP ID | ProGP165 (S-layer glycopeptide) |
| Validation Status | Characterized |
| Organism Information | |
| Organism Name | Halobacterium salinarum (Halobium) R1M1/NRC-1 |
| Domain | Archaea |
| Classification | Phylum : Euryarchaeota Class : Halobacteria Orders : Halobacteriales Family : Halobacteriaceae Genus : Halobacterium Species : salinarum Strain : R1M1/NRC-1 |
| Taxonomic ID (NCBI) | 64091 |
| Genome Information | |
| GenBank | AE004437.1 |
| EMBL | AE004437 |
| Gene Information | |
| Gene Name | csg (VNG_2679G) |
| NCBI Gene ID | 1449008 |
| GenBank Gene Sequence | NC_002607 |
| Protein Information | |
| Protein Name | S-layer glycopeptide |
| UniProtKB/SwissProt ID | B0R8E4 |
| NCBI RefSeq | WP_012289536.1 |
| EMBL-CDS | AAG20702.1 |
| 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 Location | Surface |
| Glycosylation Status | |
| Glycosylation Type | N- (Asn) linked |
| Experimentally Validated Glycosite(s) in Full Length Protein | N2 [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 Protein | N2 |
| 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 Detection | Edman 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 Name | AglB/STT3 subunit |
| OST ProGT ID | ProGT80 |
| Accessory Gene(s)Progt ID | ProGT82.1, ProGT82.3, Pro |
| Additional Comment | Engineered 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 Identification | 1998 |
| Year of Identification Month Wise | 1998.12.01 |
| Year of Validation | 1998 |
| Reference | Zeitler, 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(12), pp.1157-1164. |
| Corresponding Author | R Zeitler |
| Contact | Chair of Biochemistry I, University of Regensburg, Universitätsstrasse 31, 93040 Regensburg, Germany. |