ProGP543 (Flagellin A1)

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ProGP ID ProGP543 (Flagellin A1)
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 NameflgA1 (HVO_1210)
NCBI Gene ID 8924829
GenBank Gene Sequence NC_013967.1
Protein Information
Protein NameFlagellin A1
UniProtKB/SwissProt ID D4GWY0
NCBI RefSeq WP_004043732.1
EMBL-CDSADE02581.1
UniProtKB Sequence >sp|D4GWY0|FLGA1_HALVD Flagellin A1 OS=Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) OX=309800 GN=flgA1 PE=1 SV=1 MFENINEDRGQVGIGTLIVFIAMVLVAAIAAGVLVNTAGFLQATAEDAGQQSVNKVTNRV DVVNAHGLVNKTGEERTVDQIFLTVRLAAGSGSVSLEDTTVKYLSETTARTLTYNDTVTG SDTADPANLTTGNNFTAGVLEDGDDSFEVLNEQSDRAEMVINTSTVEGDNTNGTATGQTV KLDITSRNGGTAQVILTMPQQLAGKDNNDPIAL
Sequence length 213 AA
Function Major flagellin. Forms the filaments of bacterial flagella.
Glycosylation Status
Glycosylation Type N- (Asn) linked
Experimentally Validated Glycosite(s) in Full Length ProteinN70, N115, N162 and N172
Glycosite(s) Annotated Protein Sequence >sp|D4GWY0|FLGA1_HALVD Flagellin A1 OS=Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) OX=309800 GN=flgA1 PE=1 SV=1 MFENINEDRGQVGIGTLIVFIAMVLVAAIAAGVLVNTAGFLQATAEDAGQQSVNKVTNRV DVVNAHGLVN*(70)KTGEERTVDQIFLTVRLAAGSGSVSLEDTTVKYLSETTARTLTYN*(115)DTVTG SDTADPANLTTGNNFTAGVLEDGDDSFEVLNEQSDRAEMVIN*(162)TSTVEGDNTN*(172)GTATGQTV KLDITSRNGGTAQVILTMPQQLAGKDNNDPIAL
Sequence Around Glycosites (21 AA) VDVVNAHGLVNKTGEERTVDQ
SETTARTLTYNDTVTGSDTAD
EQSDRAEMVINTSTVEGDNTN
NTSTVEGDNTNGTATGQTVKL
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 LC-MS/MS, and MS using HCD fragmentation
Protein Glycosylation- Implication Glycosylation has a role in the assembly and function of flagella. It is also needed for swimming motility. 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 (glucose), two hexuronic acids (glucuronic acid and galacturonic acid), a methylated hexuronic acid (methyl-O-4-glucuronic acid), and a mannose
Technique(s) used for Glycan Identification LC-MS/MS, and 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 2012
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.