ProGP520 (Hag flagellin)

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ProGP ID ProGP520 (Hag flagellin)
Validation Status Characterized
Organism Information
Organism NamePaenibacillus alvei CCM 2051T (DSM 29 and ATCC 6344)
Domain Bacteria
Classification Family: Paenibacillaceae
Order: Bacillales
Class: Bacilli
Division or phylum: "Firmicutes"
Taxonomic ID (NCBI) 1206781
Genome Information
GenBank NZ_AMBZ01000002.1.
EMBL AMBZ01000002
Gene Information
Gene Namehag
NCBI Gene ID NZ_AMBZ01000002.1
Protein Information
Protein NameHag flagellin (PAV_2c01710)
UniProtKB/SwissProt ID K4Z8X9
NCBI RefSeq WP_005544722.1.
EMBL-CDSEJW18407.1.
UniProtKB Sequence >tr|K4Z8X9|K4Z8X9_PAEAL Flagellin OS=Paenibacillus alvei DSM 29 GN=hag PE=3 SV=1 MRINHNISSYNAHRQLTTNNFSQAKSLEKLSSGYRINRAADDAAGLAISEKMRNQIRGLE QASKNALDGISLIQTAEGALNETHSMLQRMSELMVQGANEVLTTTDAKKIDAEVNQLRSQ IDDIAKQTQFNTKKLLNAASTVIFQVGANSGEKISLALKKADSTALSIDKTAVTELSAAA GKLNATAASNLTAIQTAIDAVSGIRSDLGAVQNRLEHTINNLGTTAENLQAAESRIRDVD MAKEMSEFTKNNILQQAATAMLAQANQQPQGVLQLLR
Sequence length 277 AA
Glycosylation Status
Glycosylation Type O- (Ser/Thr) linked
Experimentally Validated Glycosite(s) in Full Length ProteinS140 or T141, and T192
Glycosite(s) Annotated Protein Sequence >tr|K4Z8X9|K4Z8X9_PAEAL Flagellin OS=Paenibacillus alvei DSM 29 GN=hag PE=3 SV=1 MRINHNISSYNAHRQLTTNNFSQAKSLEKLSSGYRINRAADDAAGLAISEKMRNQIRGLE QASKNALDGISLIQTAEGALNETHSMLQRMSELMVQGANEVLTTTDAKKIDAEVNQLRSQ IDDIAKQTQFNTKKLLNAAS*(140)T*(141)VIFQVGANSGEKISLALKKADSTALSIDKTAVTELSAAA GKLNATAASNLT*(192)AIQTAIDAVSGIRSDLGAVQNRLEHTINNLGTTAENLQAAESRIRDVD MAKEMSEFTKNNILQQAATAMLAQANQQPQGVLQLLR
Sequence Around Glycosites (21 AA) FNTKKLLNAASTVIFQVGANS
NTKKLLNAASTVIFQVGANSG
KLNATAASNLTAIQTAIDAVS
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Technique(s) used for Glycosylation DetectionAberrant migration on SDS-PAGE and PAS-staining
Technique(s) used for Glycosylated Residue(s) Detection MALDI-TOF-MS PMF and LC-ESI-IT-MS/MS
Protein Glycosylation- Implication O-Glycosylation is important for flagella formation and bacterial motility in vivo.
Glycan Information
Glycan Annotation A trisaccharide composed of one hexose and two N-acetyl-hexosamine residues
BCSDB ID 29572
GlyTouCan G08485BS
Technique(s) used for Glycan Identification MALDI-TOF-MS PMF and LC-ESI-IT-MS/MS
Literature
Year of Identification2016
Year of Identification Month Wise2016.1.1
Year of Validation 2016
ReferenceJanesch, B., Schirmeister, F., Maresch, D., Altmann, F., Messner, P., Kolarich, D. and Schäffer, C., 2016. Flagellin glycosylation in Paenibacillus alvei CCM 2051T. Glycobiology, 26(1), pp.74-87.
Corresponding Author Daniel Kolarich
Christina Schaffer
ContactDepartment of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, Potsdam 14424, Germany
ReferenceJanesch B, Schirmeister F, Maresch D, Altmann F, Messner P, Kolarich D, Schäffer C. (2016) Flagellin glycosylation in Paenibacillus alvei CCM 2051T. Glycobiology, 26(1):74-87. [PubMed: 26405108]
AuthorJanesch B, Schirmeister F, Maresch D, Altmann F, Messner P, Kolarich D, Schäffer C.
Research Group1 Department of NanoBiotechnology, NanoGlycobiology Unit, University of Natural Resources and Life Sciences Vienna, Muthgasse 11, Vienna A-1190, Austria. 2 Department of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, Potsdam 14424, Germany Institute of Chemistry and Biochemistry, Free University of Berlin, Arnimallee 22, Berlin 14195, Germany. 3 Department of Chemistry, Division of Biochemistry, Universität für Bodenkultur Wien, Muthgasse 18, Vienna A-1190, Austria. 4 Department of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, Potsdam 14424, Germany 5 Department of NanoBiotechnology, NanoGlycobiology Unit, Universität für Bodenkultur Wien, Muthgasse 11, Vienna A-1190, Austria
Corresponding Author Schäffer C.
ContactDepartment of NanoBiotechnology, NanoGlycobiology, Vienna Institute of BioTechnology, Universität für Bodenkultur Wien, Muthgasse 11, A-1190 Vienna, Austria.