ID   FLGH_AQUAE              Reviewed;         216 AA.
AC   O67609;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Flagellar L-ring protein;
DE   AltName: Full=Basal body L-ring protein;
DE   Flags: Precursor;
GN   Name=flgH; OrderedLocusNames=aq_1714;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
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}; Lipid-anchor
CC       {ECO:0000250}. Bacterial flagellum basal body {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FlgH family. {ECO:0000305}.
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DR   EMBL; AE000657; AAC07570.1; -; Genomic_DNA.
DR   PIR; G70447; G70447.
DR   RefSeq; NP_214175.1; NC_000918.1.
DR   RefSeq; WP_010881112.1; NC_000918.1.
DR   AlphaFoldDB; O67609; -.
DR   SMR; O67609; -.
DR   STRING; 224324.aq_1714; -.
DR   EnsemblBacteria; AAC07570; AAC07570; aq_1714.
DR   KEGG; aae:aq_1714; -.
DR   eggNOG; COG2063; Bacteria.
DR   HOGENOM; CLU_069313_1_1_0; -.
DR   InParanoid; O67609; -.
DR   OMA; ITQQPMT; -.
DR   OrthoDB; 1900876at2; -.
DR   Proteomes; UP000000798; Chromosome.
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; Lipoprotein; Membrane; Palmitate;
KW   Reference proteome; Signal.
FT   SIGNAL          1..13
FT                   /evidence="ECO:0000255"
FT   CHAIN           14..216
FT                   /note="Flagellar L-ring protein"
FT                   /id="PRO_0000009422"
FT   LIPID           14
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   LIPID           14
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   216 AA;  23767 MW;  267B2A50D3EDE0E9 CRC64;
     MLYLFFALIF IISCSTKVES KKKYTYSFPK TYKEEKPTRG SLFKSPQSAY LYGSVRASEV
     GDVIYIRVIE SINAIESVST NVGRSTSFSN AISSFFGVHP ATLKNLGAGG KSSFASKGGS
     KFQQSGVLTT TLAGRVVKVF PNGTMLVEAK KYIEVNGVKR EFLLRGIVRP EDIDSNNTVT
     SDKIADMEIF FEGRGYIVRG GEPGWLAKIF AILFPF