ProGP32 (Flagellin B3)
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| ProGP ID | ProGP32 (Flagellin B3) |
| 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 | flaB3 (VNG_0962G) |
| NCBI Gene ID | 1447687 |
| GenBank Gene Sequence | NC_002607.1 |
| Protein Information | |
| Protein Name | Flagellin B3 |
| UniProtKB/SwissProt ID | P13078 |
| NCBI RefSeq | WP_010902682.1 |
| EMBL-CDS | AAG19385.1 |
| UniProtKB Sequence | >sp|P13078|FLAB3_HALSA Flagellin B3 OS=Halobacterium salinarium (strain ATCC 700922 / JCM 11081 / NRC-1) GN=flaB3 PE=3 SV=1 MFEFITDEDERGQVGIGTLIVFIAMVLVAAIAAGVLINTAGYLQSKGSATGEEASAQVSN RINIVSAYGNVNSEKVDYVNLTVRQAAGADNINLTKSTIQWIGPDKATTLTYSSNSPSSL GENFTTESIKGNNADVLVEQSDRIKVIMYASGVSSTLGSGEEVQLTVTTQYGSKTTYWAH VPESLKDKNAVKL |
| Sequence length | 193 AA |
| Subcellular Location | Flagellum |
| Function | Flagellin is the structural subunit of the flagellar filaments. |
| Glycosylation Status | |
| Glycosylation Type | N- (Asn) linked |
| Experimentally Validated Glycosite(s) in Full Length Protein | N91, N56 |
| Experimentally Validated Glycosite(s ) in Mature Protein | N91 |
| Glycosite(s) Annotated Protein Sequence | >sp|P13078|FLAB3_HALSA Flagellin B3 OS=Halobacterium salinarium (strain ATCC 700922 / JCM 11081 / NRC-1) GN=flaB3 PE=3 SV=1 MFEFITDEDERGQVGIGTLIVFIAMVLVAAIAAGVLINTAGYLQSKGSATGEEASAQVSN RINIVSAYGNVNSEKVDYVNLTVRQAAGADN*(91)INLTKSTIQWIGPDKATTLTYSSNSPSSL GENFTTESIKGNNADVLVEQSDRIKVIMYASGVSSTLGSGEEVQLTVTTQYGSKTTYWAH VPESLKDKNAVKL |
| Sequence Around Glycosites (21 AA) | LTVRQAAGADNINLTKSTIQW |
| Technique(s) used for Glycosylation Detection | Mass shift on SDS-PAGE after deglycosylation with anhydrous hydrogen fluoride. LC ESI MS, MS/MS |
| Technique(s) used for Glycosylated Residue(s) Detection | Glycopeptide sequencing |
| Glycan Information | |
| Glycan Annotation | Linkage: Glc-Asn. Sulfated oligosaccharides that resemble those of the cell-suface glycoprotein in the bacterium are present. Glucose and glucuronic acid are the constituents of the glycans which are of the type GlcA-(1→4)-GlcA-(1→4)-GlcA-(1→4)-Glc. |
| Technique(s) used for Glycan Identification | GLC-MS (gas liquid chromatography-mass spectrometry) after perfluoropropionylation. |
| Protein Glycosylation linked (PGL) gene(s) | |
| Additional Comment | Removal of Mg++ ions in the growth medium inhibits glycosylation of proteins in vivo. This leads to the reduction in the molecular masses of newly synthesized flagellins. There might be another modification of the flagellins that is resistant to HF treatment. Halobacterial glycoproteins including flagellins are glycosylated at the extracellular surface of the cell membrane. |
| Literature | |
| Year of Identification | 1985 |
| Year of Identification Month Wise | 1985.12 |
| Year of Validation | 1988 |
| Reference | Cohen-Krausz, S. and Trachtenberg, S., 2002. The structure of the archeabacterial flagellar filament of the extreme halophile Halobacterium salinarum R1M1 and its relation to eubacterial flagellar filaments and type IV pili. Journal of molecular biology, 321(3), pp.383-395. |
| Corresponding Author | Shlomo Trachtenberg |
| Contact | Department of Membrane and Ultrastructure Research, Hebrew University of Jerusalem-Hadassah Medical School, P.O. Box 12272, 91120, Jerusalem, Israel. |
| Reference | Gerl, L., Deutzmann, R. and Sumper, M., 1989. Halobacterial flagellins are encoded by a multigene family Identification of all five gene products. FEBS letters, 244(1), pp.137-140. |
| Corresponding Author | Manfred Sumper |
| Contact | Institute of Biochemistry, Genetics and Microbiology, University of Regensburg, Federal Republic of Germany. |
| Reference | Gerl, L. and Sumper, M., 1988. Halobacterial flagellins are encoded by a multigene family. Characterization of five flagellin genes. Journal of Biological Chemistry, 263(26), pp.13246-13251. |
| Corresponding Author | Manfred Sumper |
| Contact | Institute of Biochemistry, Genetics and Microbiology, University of Regensburg, Federal Republic of Germany. |
| Reference | Wieland, F., Paul, G. and Sumper, M., 1985. Halobacterial flagellins are sulfated glycoproteins. Journal of Biological Chemistry, 260(28), pp.15180-15185. |
| Corresponding Author | Felix Wieland |
| Contact | Institute of Biochemistry, Genetics and Microbiology, University of Regensburg, Universitatsstraße 31, 8400 Regensburg, Federal Republic of Germany |
| Reference | Vershinin, Z., Zaretsky, M., Guan, Z. and Eichler, J., 2021. Revisiting N-glycosylation in Halobacterium salinarum: Characterizing a dolichol phosphate-and glycoprotein-bound tetrasaccharide. Glycobiology. |
| Corresponding Author | Jerry Eichler |
| Contact | Department of Life Sciences, Ben Gurion University of the Negev, PO Box 653, Beersheva 84105, Israel. |