ID   FLGH_RHILO              Reviewed;         235 AA.
AC   Q98HD3;
DT   03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Flagellar L-ring protein;
DE   AltName: Full=Basal body L-ring protein;
DE   Flags: Precursor;
GN   Name=flgH; OrderedLocusNames=mlr2921;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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; BA000012; BAB49933.1; -; Genomic_DNA.
DR   RefSeq; WP_010911280.1; NC_002678.2.
DR   AlphaFoldDB; Q98HD3; -.
DR   SMR; Q98HD3; -.
DR   STRING; 266835.14023326; -.
DR   EnsemblBacteria; BAB49933; BAB49933; BAB49933.
DR   GeneID; 66682308; -.
DR   KEGG; mlo:mlr2921; -.
DR   eggNOG; COG2063; Bacteria.
DR   HOGENOM; CLU_069313_1_2_5; -.
DR   OMA; PRAQHIG; -.
DR   OrthoDB; 1900876at2; -.
DR   Proteomes; UP000000552; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Bacterial flagellum; Cell outer membrane; Lipoprotein; Membrane; Palmitate;
KW   Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..235
FT                   /note="Flagellar L-ring protein"
FT                   /id="PRO_0000009464"
FT   LIPID           17
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   LIPID           17
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   235 AA;  25524 MW;  99CBBC6537659670 CRC64;
     MIRRTLILCA VAALSGCGTN LREVGKEPSL SPVGSGIDGG NTSALYKYPE PPRAPVKKFS
     LWDDRQSRLF TDPRALSQGD ILTVRIKIND RANFKNQNDR SRTANRKLGF DLSAQWDKWS
     TAGKGAGALN SATDTTADGE IKRSETLELN VAAIVTDVLP NGNLMITGSQ EVRVNAELRV
     LTIAGIVRPA DIGAENTIPY ERIAEARISY GGRGRISEIQ QPAYGQQVLD QVLPF