ID   FLGH_RALSO              Reviewed;         229 AA.
AC   Q8XSW9;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 2.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Flagellar L-ring protein;
DE   AltName: Full=Basal body L-ring protein;
DE   Flags: Precursor;
GN   Name=flgH; OrderedLocusNames=RSp0348; ORFNames=RS00749;
OS   Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OG   Plasmid megaplasmid Rsp.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=267608;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GMI1000;
RX   PubMed=11823852; DOI=10.1038/415497a;
RA   Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA   Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA   Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA   Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA   Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT   "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL   Nature 415:497-502(2002).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAD17499.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AL646053; CAD17499.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q8XSW9; -.
DR   SMR; Q8XSW9; -.
DR   STRING; 267608.RSp0348; -.
DR   EnsemblBacteria; CAD17499; CAD17499; RSp0348.
DR   KEGG; rso:RSp0348; -.
DR   eggNOG; COG2063; Bacteria.
DR   HOGENOM; CLU_069313_0_0_4; -.
DR   OMA; ITQQPMT; -.
DR   Proteomes; UP000001436; Plasmid megaplasmid Rsp.
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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Bacterial flagellum; Cell outer membrane; Lipoprotein; Membrane; Palmitate;
KW   Plasmid; Reference proteome; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..229
FT                   /note="Flagellar L-ring protein"
FT                   /id="PRO_0000009463"
FT   LIPID           19
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   LIPID           19
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   229 AA;  23835 MW;  FA7E0FF07BEA71F8 CRC64;
     MRILRLAALG TASLLAAACG MLPPPEPIVQ GPTTARPPMP VMAPRQNGAI YQEVASGSGG
     FRGMFEDRRA HMVGDTITIV ITENTAASKQ TSGSVDRSGS KTTSVPTFAG MNPGVLSLLG
     VSASDANKFD SKGANGATNN FTATITVTVV EVLSNGNLVV SGEKQMAVGQ GTESIKFSGV
     VNPTTVNNQN TVLSTQVADA RMEYRGTGYV AEAQQMGWLS RFFLSVSPF