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 | Phylum : Euryarchaeota Class : Halobacteria Orders : Haloferacales Family : Haloferacaceae Genus : Haloferax Species : volcanii Strain : H53 |
| 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, R.N., Schulze, S., Xu, R., Hippler, M. and Pohlschroder, M., 2016. Identification of Haloferax volcanii pilin N-glycans with diverse roles in pilus biosynthesis, adhesion, and microcolony formation. Journal of Biological Chemistry, 291(20), pp.10602-10614. |
| Corresponding Author | Mechthild Pohlschroder |
| Contact | From the Department of Biology, University of Pennsylvania, Philadelphia, Pennsylvania 19104 |
| Reference | Tripepi, M., You, J., Temel, S., Önder, Ö., Brisson, D. and Pohlschröder, M., 2012. N-glycosylation of Haloferax volcanii flagellins requires known Agl proteins and is essential for biosynthesis of stable flagella. Journal of bacteriology, 194(18), pp.4876-4887. |
| Corresponding Author | Mechthild Pohlschroder |
| Contact | From the Department of Biology, University of Pennsylvania, Philadelphia, Pennsylvania 19104 |
| Reference | Wieland, F., Paul, G. and Sumper, M., 1985. Halobacterial flagellins are sulfated glycoproteins. Journal of Biological Chemistry, 260(28), pp.15180-15185. |
| Corresponding Author | Felix Wieland |
| Contact | Institute for Biochemistry, Genetics and Microbology, Universitat Regensburg, Universitatsstra ~ e 31, 8400 Regensburg, Federal Republic of Germany |