ProGP544 (Flagellin A2)

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ProGP ID ProGP544 (Flagellin A2)
Validation Status Characterized
Organism Information
Organism NameHaloferax volcanii H53
Domain Archaea
Classification Family: Halobacteriaceae
Order: Halobacteriales
Class: Halobacteria or Halomebacteria
Division or phylum: "Euryarchaeota"
Taxonomic ID (NCBI) 309800
Genome Information
GenBank CP001956.1
EMBL CP001956.1
Gene Information
Gene NameflgA2 (HVO_1211)
NCBI Gene ID 8924200
GenBank Gene Sequence NC_013967.1
Protein Information
Protein NameFlagellin A2
UniProtKB/SwissProt ID D4GWY2
NCBI RefSeq WP_013035369.1
EMBL-CDSADE03249.1
UniProtKB Sequence >sp|D4GWY2|FLGA2_HALVD Flagellin A2 OS=Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) OX=309800 GN=flgA2 PE=1 SV=1 MFNNITDDDRGQVGIGTLIVFIAMVLVAAIAAGVLVNTAGFLQATAEDAGEQSVNKVTNR VEVLNTHGTVGGEEDIDNITLTVRLAAGSDAVDMNETSIKYLSGDSVVTLTNQTVTSGAN SATNDSAEGVADSDEFGLSEVTDDDGSFGVLNSMNDRYEVTIDTAAIETSDGDNTNLIGG LSTGEQVTLEITSRTGGTTQVILTMPQQLAGKTQNEPVEL
Sequence length 220 AA
Function Minor flagellin. Forms the filaments of bacterial flagella.
Glycosylation Status
Glycosylation Type N- (Asn) linked
Experimentally Validated Glycosite(s) in Full Length ProteinN78 and N95
Glycosite(s) Annotated Protein Sequence >sp|D4GWY2|FLGA2_HALVD Flagellin A2 OS=Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) OX=309800 GN=flgA2 PE=1 SV=1 MFNNITDDDRGQVGIGTLIVFIAMVLVAAIAAGVLVNTAGFLQATAEDAGEQSVNKVTNR VEVLNTHGTVGGEEDIDN*(78)ITLTVRLAAGSDAVDMN*(95)ETSIKYLSGDSVVTLTNQTVTSGAN SATNDSAEGVADSDEFGLSEVTDDDGSFGVLNSMNDRYEVTIDTAAIETSDGDNTNLIGG LSTGEQVTLEITSRTGGTTQVILTMPQQLAGKTQNEPVEL
Sequence Around Glycosites (21 AA) GTVGGEEDIDNITLTVRLAAG
LAAGSDAVDMNETSIKYLSGD
Technique(s) used for Glycosylation DetectionAberrant migration on lithium dodecyl sulfate (LDS)-PAGE as detected through western blotting
Technique(s) used for Glycosylated Residue(s) Detection MS using HCD fragmentation
Protein Glycosylation- Implication Glycosylation has a role in the assembly and function of flagella. N-glycosylation may regulate the transition from planktonic cell to biofilm formation under stress conditions.
Glycan Information
Glycan Annotation A pentasaccharide composed of a hexose, two hexuronic acids, a methylated hexuronic acid, and a mannose
Technique(s) used for Glycan Identification MS using IS (in source)-CID
Protein Glycosylation linked (PGL) gene(s)
OST Gene NameAglB
Literature
Year of Identification1985
Year of Identification Month Wise1985.12
Year of Validation 2016
ReferenceEsquivel RN, Schulze S, Xu R, Hippler M, Pohlschroder M. (2016) Identification of Haloferax volcanii Pilin N-Glycans with Diverse Roles in Pilus Biosynthesis, Adhesion, and Microcolony Formation. J Biol Chem., 291(20), 10602-14. [PubMed: 26966177]
AuthorEsquivel RN, Schulze S, Xu R, Hippler M, Pohlschroder M.
Research Group1 Department of Biology, University of Pennsylvania, Philadelphia, Pennsylvania 19104. 2 Institute of Plant Biology and Biotechnology, University of Münster, Münster 48143, Germany. 3 Department of Biology, University of Pennsylvania, Philadelphia, Pennsylvania 19104.
Corresponding Author Pohlschroder M.
ContactDepartment of Biology, University of Pennsylvania, Philadelphia, Pennsylvania 19104.
ReferenceTripepi M, You J, Temel S, Önder Ö, Brisson D, Pohlschröder M. (2012) N-glycosylation of Haloferax volcanii flagellins requires known Agl proteins and is essential for biosynthesis of stable flagella. J Bacteriol., 194(18), 4876-87. [PubMed: 22730124]
AuthorTripepi M, You J, Temel S, Önder Ö, Brisson D, Pohlschröder M.
Research GroupDepartment of Biology, University of Pennsylvania, Philadelphia, Pennsylvania, USA.
Corresponding Author Pohlschröder M.
ContactDepartment of Biology, University of Pennsylvania, Philadelphia, Pennsylvania, USA.
ReferenceWieland F, Paul G, Sumper M. (1985) Halobacterial flagellins are sulfated glycoproteins. J Biol Chem., 260(28), 15180-5. [PubMed: 3934156]
AuthorWieland F, Paul G, Sumper M.
Research GroupInstitute of Biochemistry, Genetics and Microbology, University of Regensburg, Universitatsstra ee 31, 8400 Regensburg, Federal Republic of Germany.
Corresponding Author Sumper M.
ContactFrom the Institut fur Biochemie, Genetik und Mikrobwlogie, Universitat Regensburg, Universitatsstra~e 31, 8400 Regensburg, Federal Republic of Germany.