ProGP31

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ProGP ID ProGP31
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 NameflaB2 (VNG_0961G)
NCBI Gene ID 1447686
GenBank Gene Sequence 1447686
Protein Information
Protein NameFlagellin B2
UniProtKB/SwissProt ID P13077
NCBI RefSeq NP_279904.1
EMBL-CDSAAG19384.1
UniProtKB Sequence >sp|P13077|FLAB2_HALSA Flagellin B2 OS=Halobacterium salinarium (strain ATCC 700922 / JCM 11081 / NRC-1) GN=flaB2 PE=3 SV=1 MFEFITDEDERGQVGIGTLIVFIAMVLVAAIAAGVLINTAGYLQSKGSATGEEASAQVSN RINIVSAYGNVDTSGSTEVVNYANLTVRQAAGADNINLSKSTIQWIGPDTATTLTYDGTT ADAENFTTNSIKGDNADVLVDQSDRIEIVMDAAEITTNGLKAGEEVQLTVTTQYGSKTTY WANVPESLKDKNAVTL
Sequence length 196 AA
Subcellular LocationFlagellum
Function Flagellin is the structural subunit of the flagellar filaments.
Glycosylation Status
Glycosylation Type N (Asn) linked
Experimentally Validated Glycosite(s) in Full Length ProteinN97, N125
Experimentally Validated Glycosite(s ) in Mature ProteinN97, N125
Glycosite(s) Annotated Protein Sequence >sp|P13077|FLAB2_HALSA Flagellin B2 OS=Halobacterium salinarium (strain ATCC 700922 / JCM 11081 / NRC-1) GN=flaB2 PE=3 SV=1 MFEFITDEDERGQVGIGTLIVFIAMVLVAAIAAGVLINTAGYLQSKGSATGEEASAQVSN RINIVSAYGNVDTSGSTEVVNYANLTVRQAAGADNIN*(97)LSKSTIQWIGPDTATTLTYDGTT ADAEN*(125)FTTNSIKGDNADVLVDQSDRIEIVMDAAEITTNGLKAGEEVQLTVTTQYGSKTTY WANVPESLKDKNAVTL
Sequence Around Glycosites (21 AA) VRQAAGADNINLSKSTIQWIG
TYDGTTADAENFTTNSIKGDN
Glycosite Sequence Logo
Technique(s) used for Glycosylation DetectionMass shift on SDS-PAGE after deglycosylation with anhydrous hydrogen fluoride.
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.
Literature
Additional CommentRemoval 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.
Year of Identification1985
Year of Identification Month Wise1985.12
Year of Validation 1989
Reference1) 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. J Mol Biol, 321, 383-395. [PubMed: 12162953]
2) Gerl, L., Deutzmann, R. and Sumper, M. (1989) Halobacterial flagellins are encoded by a multigene family. Identification of all five gene products. FEBS Lett, 244, 137-140. [PubMed: 2924901]
3) Gerl, L. and Sumper, M. (1988) Halobacterial flagellins are encoded by a multigene family. Characterization of five flagellin genes. J Biol Chem, 263, 13246-13251. [PubMed: 3417656]
4) Wieland, F., Paul, G. and Sumper, M. (1985) Halobacterial flagellins are sulfated glycoproteins. J Biol Chem, 260, 15180-15185. [PubMed: 3934156]
Author Cohen-Krausz, S. and Trachtenberg, S.
Research GroupDepartment of Membrane and Ultrastructure Research, Hebrew University of Jerusalem-Hadassah Medical School, P.O. Box 12272, 91120, Jerusalem, Israel.
Corresponding Author Trachtenberg, S.
ContactDepartment of Membrane and Ultrastructure Research, Hebrew University of Jerusalem-Hadassah Medical School, P.O. Box 12272, 91120, Jerusalem, Israel.