ProGP543 (Flagellin A1)
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| ProGP ID | ProGP543 (Flagellin A1) |
| Validation Status | Characterized |
| Organism Information | |
| Organism Name | Haloferax 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 Name | flgA1 (HVO_1210) |
| NCBI Gene ID | 8924829 |
| GenBank Gene Sequence | NC_013967.1 |
| Protein Information | |
| Protein Name | Flagellin A1 |
| UniProtKB/SwissProt ID | D4GWY0 |
| NCBI RefSeq | WP_004043732.1 |
| EMBL-CDS | ADE02581.1 |
| 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 Protein | N70, 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 Detection | Aberrant 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 Name | AglB |
| Literature | |
| Year of Identification | 1985 |
| Year of Identification Month Wise | 1985.12 |
| Year of Validation | 2012 |
| Reference | Esquivel 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] |
| Author | Esquivel RN, Schulze S, Xu R, Hippler M, Pohlschroder M. |
| Research Group | 1 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. |
| Contact | Department of Biology, University of Pennsylvania, Philadelphia, Pennsylvania 19104. |
| Reference | Tripepi 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] |
| Author | Tripepi M, You J, Temel S, Önder Ö, Brisson D, Pohlschröder M. |
| Research Group | Department of Biology, University of Pennsylvania, Philadelphia, Pennsylvania, USA. |
| Corresponding Author | Pohlschröder M. |
| Contact | Department of Biology, University of Pennsylvania, Philadelphia, Pennsylvania, USA. |
| Reference | Wieland F, Paul G, Sumper M. (1985) Halobacterial flagellins are sulfated glycoproteins. J Biol Chem., 260(28), 15180-5. [PubMed: 3934156] |
| Author | Wieland F, Paul G, Sumper M. |
| Research Group | Institute of Biochemistry, Genetics and Microbology, University of Regensburg, Universitatsstra ee 31, 8400 Regensburg, Federal Republic of Germany. |
| Corresponding Author | Sumper M. |
| Contact | From the Institut fur Biochemie, Genetik und Mikrobwlogie, Universitat Regensburg, Universitatsstra~e 31, 8400 Regensburg, Federal Republic of Germany. |