ProGP29

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ProGP ID ProGP29
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 NameFlaA2 (VNG_1009G)
NCBI Gene ID 1447728
GenBank Gene Sequence 1447728
Protein Information
Protein NameFlagellin A2
UniProtKB/SwissProt ID P13075
NCBI RefSeq NP_279945.1
EMBL-CDSAAG19425.1
UniProtKB Sequence >sp|P13075|FLAA2_HALSA Flagellin A2 OS=Halobacterium salinarium (strain ATCC 700922 / JCM 11081 / NRC-1) GN=flaA2 PE=3 SV=1 MFEFITDEDERGQVGIGTLIVFIAMVLVAAIAAGVLINTAGFLQSKGSATGEEASAQVSN RINIVSAYGNVNNEEVDYVNLTVRQAAGADNINLSKSTIQWIGPDKATTLTHANAADKTT LGEEFNTTSIKGNNDNVLVQQSDRIKVIMYAGGVSSKLGAGDEVQLTVTTQYGSKTTYWA NVPESLKDKNAVKL
Sequence length 194 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 ProteinN126
Experimentally Validated Glycosite(s ) in Mature ProteinN126
Glycosite(s) Annotated Protein Sequence >sp|P13075|FLAA2_HALSA Flagellin A2 OS=Halobacterium salinarium (strain ATCC 700922 / JCM 11081 / NRC-1) GN=flaA2 PE=3 SV=1 MFEFITDEDERGQVGIGTLIVFIAMVLVAAIAAGVLINTAGFLQSKGSATGEEASAQVSN RINIVSAYGNVNNEEVDYVNLTVRQAAGADNINLSKSTIQWIGPDKATTLTHANAADKTT LGEEFN*(126)TTSIKGNNDNVLVQQSDRIKVIMYAGGVSSKLGAGDEVQLTVTTQYGSKTTYWA NVPESLKDKNAVKL
Sequence Around Glycosites (21 AA) ADKTTLGEEFNTTSIKGNNDN
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
Year of Identification1985
Year of Identification Month Wise1985.12
Year of Validation 1989
ReferenceCohen-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]
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.
ReferenceGerl, 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]
AuthorGerl, L., Deutzmann, R. and Sumper, M.
Research GroupChair of Biochemistry, University of Regensburg, FRG.
Corresponding Author Sumper, M
ContactChair of Biochemistry, University of Regensburg, FRG.
ReferenceGerl, 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]
AuthorGerl, L. Sumper, M.
Research GroupInstitute of Biochemistry, Genetics and Microbiology, University of Regensburg, Federal Republic of Germany.
Corresponding Author Sumper, M.
ContactInstitute of Biochemistry, Genetics and Microbiology, University of Regensburg, Federal Republic of Germany.
ReferenceWieland, 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, Universitatsstraße 31, 8400 Regensburg, Federal Republic of Germany
Corresponding Author Sumper, M.
ContactInstitute of Biochemistry, Genetics and Microbiology, University of Regensburg, Universitatsstraße 31, 8400 Regensburg, Federal Republic of Germany