ID   FLGH_BURPS              Reviewed;         240 AA.
AC   Q63YB2;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Flagellar L-ring protein;
DE   AltName: Full=Basal body L-ring protein;
DE   Flags: Precursor;
GN   Name=flgH; OrderedLocusNames=BPSL0276;
OS   Burkholderia pseudomallei (strain K96243).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=272560;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K96243;
RX   PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA   Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA   Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA   Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA   Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA   Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA   Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA   Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA   Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA   Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT   "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT   pseudomallei.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
CC   -!- FUNCTION: Assembles around the rod to form the L-ring and probably
CC       protects the motor/basal body from shearing forces during rotation.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: The basal body constitutes a major portion of the flagellar
CC       organelle and consists of four rings (L,P,S, and M) mounted on a
CC       central rod. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}. Bacterial
CC       flagellum basal body {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FlgH family. {ECO:0000305}.
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DR   EMBL; BX571965; CAH34264.1; -; Genomic_DNA.
DR   RefSeq; WP_004523041.1; NZ_CP009538.1.
DR   RefSeq; YP_106903.1; NC_006350.1.
DR   AlphaFoldDB; Q63YB2; -.
DR   SMR; Q63YB2; -.
DR   STRING; 272560.BPSL0276; -.
DR   EnsemblBacteria; CAH34264; CAH34264; BPSL0276.
DR   KEGG; bps:BPSL0276; -.
DR   PATRIC; fig|272560.51.peg.1429; -.
DR   eggNOG; COG2063; Bacteria.
DR   OMA; ITQQPMT; -.
DR   Proteomes; UP000000605; Chromosome 1.
DR   GO; GO:0009427; C:bacterial-type flagellum basal body, distal rod, L ring; IEA:InterPro.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR   GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:InterPro.
DR   HAMAP; MF_00415; FlgH; 1.
DR   InterPro; IPR000527; Flag_Lring.
DR   PANTHER; PTHR34933; PTHR34933; 1.
DR   Pfam; PF02107; FlgH; 1.
DR   PRINTS; PR01008; FLGLRINGFLGH.
PE   3: Inferred from homology;
KW   Bacterial flagellum; Cell outer membrane; Membrane; Reference proteome;
KW   Signal.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..240
FT                   /note="Flagellar L-ring protein"
FT                   /id="PRO_0000009435"
SQ   SEQUENCE   240 AA;  25339 MW;  6597B695EF8A47F4 CRC64;
     MKQVRFLPQP ARRARAAAAR RPGAAALAAA ALALAGCAQI PREPITQQPM SAMPPMPPAM
     QAPGSIYNPG YAGRPLFEDQ RPRNVGDILT IVIAENINAT KSSGANTNRQ GNTSFDVPTA
     GFLGGLFNKA NLSAQGANKF AATGGASAAN TFNGTITVTV TNVLPNGNLV VSGEKQMLIN
     QGNEFVRFSG IVNPNTISGQ NSVYSTQVAD ARIEYSAKGY INEAETMGWL QRFFLNIAPW