FLGA1_HALVD
ID FLGA1_HALVD Reviewed; 213 AA.
AC D4GWY0;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Flagellin A1;
DE Flags: Precursor;
GN Name=flgA1; OrderedLocusNames=HVO_1210; ORFNames=C498_12698;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [3]
RP IDENTIFICATION.
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=10632878; DOI=10.1046/j.1365-2958.2000.01677.x;
RA Tarasov V.Y., Pyatibratov M.G., Tang S.L., Dyall-Smith M., Fedorov O.V.;
RT "Role of flagellins from A and B loci in flagella formation of
RT Halobacterium salinarum.";
RL Mol. Microbiol. 35:69-78(2000).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20363933; DOI=10.1128/jb.00133-10;
RA Tripepi M., Imam S., Pohlschroeder M.;
RT "Haloferax volcanii flagella are required for motility but are not involved
RT in PibD-dependent surface adhesion.";
RL J. Bacteriol. 192:3093-3102(2010).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, GLYCOSYLATION AT ASN-70; ASN-115 AND
RP ASN-172, AND MUTAGENESIS OF ASN-70; ASN-115 AND ASN-172.
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=22730124; DOI=10.1128/jb.00731-12;
RA Tripepi M., You J., Temel S., Onder O., Brisson D., Pohlschroder M.;
RT "N-glycosylation of Haloferax volcanii flagellins requires known Agl
RT proteins and is essential for biosynthesis of stable flagella.";
RL J. Bacteriol. 194:4876-4887(2012).
CC -!- FUNCTION: Major flagellin required for motility. Not involved in PibD-
CC dependent surface adhesion. Much more abundant in cells compared to
CC FlgA2. {ECO:0000269|PubMed:20363933, ECO:0000269|PubMed:22730124}.
CC -!- SUBCELLULAR LOCATION: Archaeal flagellum {ECO:0000250}.
CC -!- PTM: Glycosylated by a pentasaccharide similar to the S-layer
CC glycoprotein, probably comprising a hexose, 2 hexuronic acids, a methyl
CC ester of a hexuronic acid and mannose. Glycosylation is required for
CC biosynthesis of stable flagella. {ECO:0000269|PubMed:22730124}.
CC -!- DISRUPTION PHENOTYPE: Cells are non-motile. Cells lacking both flgA1
CC and flgA2 show defects in motility, whitout affecting surface adhesion
CC ability. {ECO:0000269|PubMed:20363933, ECO:0000269|PubMed:22730124}.
CC -!- SIMILARITY: Belongs to the archaeal flagellin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001956; ADE02581.1; -; Genomic_DNA.
DR EMBL; AOHU01000091; ELY28105.1; -; Genomic_DNA.
DR RefSeq; WP_004043732.1; NZ_AOHU01000091.1.
DR AlphaFoldDB; D4GWY0; -.
DR SMR; D4GWY0; -.
DR STRING; 309800.C498_12698; -.
DR iPTMnet; D4GWY0; -.
DR EnsemblBacteria; ADE02581; ADE02581; HVO_1210.
DR EnsemblBacteria; ELY28105; ELY28105; C498_12698.
DR GeneID; 8924829; -.
DR KEGG; hvo:HVO_1210; -.
DR PATRIC; fig|309800.29.peg.2432; -.
DR eggNOG; arCOG01829; Archaea.
DR HOGENOM; CLU_051124_1_0_2; -.
DR OMA; THGIVND; -.
DR OrthoDB; 94462at2157; -.
DR Proteomes; UP000008243; Chromosome.
DR Proteomes; UP000011532; Unassembled WGS sequence.
DR GO; GO:0097589; C:archaeal-type flagellum; IEA:UniProtKB-SubCell.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0097588; P:archaeal or bacterial-type flagellum-dependent cell motility; IEA:InterPro.
DR InterPro; IPR013373; Flagellin/pilin_N.
DR InterPro; IPR002774; Flagellin_arc.
DR PANTHER; PTHR35903; PTHR35903; 1.
DR Pfam; PF01917; Arch_flagellin; 1.
DR TIGRFAMs; TIGR02537; arch_flag_Nterm; 1.
PE 1: Evidence at protein level;
KW Archaeal flagellum; Glycoprotein; Reference proteome.
FT PROPEP 1..10
FT /evidence="ECO:0000255"
FT /id="PRO_0000429052"
FT CHAIN 11..213
FT /note="Flagellin A1"
FT /id="PRO_0000429053"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22730124"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22730124"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22730124"
FT MUTAGEN 70
FT /note="N->Q: Defects in flagella motility. Decreased
FT glycosylation."
FT /evidence="ECO:0000269|PubMed:22730124"
FT MUTAGEN 115
FT /note="N->Q: Defects in flagella motility. Decreased
FT glycosylation."
FT /evidence="ECO:0000269|PubMed:22730124"
FT MUTAGEN 172
FT /note="N->Q: Defects in flagella motility. Decreased
FT glycosylation."
FT /evidence="ECO:0000269|PubMed:22730124"
SQ SEQUENCE 213 AA; 22312 MW; DCC01887B2C2C9F7 CRC64;
MFENINEDRG QVGIGTLIVF IAMVLVAAIA AGVLVNTAGF LQATAEDAGQ QSVNKVTNRV
DVVNAHGLVN KTGEERTVDQ IFLTVRLAAG SGSVSLEDTT VKYLSETTAR TLTYNDTVTG
SDTADPANLT TGNNFTAGVL EDGDDSFEVL NEQSDRAEMV INTSTVEGDN TNGTATGQTV
KLDITSRNGG TAQVILTMPQ QLAGKDNNDP IAL
