ID   FLGH_RHOPA              Reviewed;         252 AA.
AC   Q6N2Z5;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Flagellar L-ring protein {ECO:0000255|HAMAP-Rule:MF_00415};
DE   AltName: Full=Basal body L-ring protein {ECO:0000255|HAMAP-Rule:MF_00415};
DE   Flags: Precursor;
GN   Name=flgH {ECO:0000255|HAMAP-Rule:MF_00415}; OrderedLocusNames=RPA3902;
OS   Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=258594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-98 / CGA009;
RX   PubMed=14704707; DOI=10.1038/nbt923;
RA   Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA   Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA   Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA   Harrison F.H., Gibson J., Harwood C.S.;
RT   "Complete genome sequence of the metabolically versatile photosynthetic
RT   bacterium Rhodopseudomonas palustris.";
RL   Nat. Biotechnol. 22:55-61(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:0000255|HAMAP-Rule:MF_00415}.
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:0000255|HAMAP-Rule:MF_00415}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00415}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_00415}.
CC       Bacterial flagellum basal body {ECO:0000255|HAMAP-Rule:MF_00415}.
CC   -!- SIMILARITY: Belongs to the FlgH family. {ECO:0000255|HAMAP-
CC       Rule:MF_00415}.
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DR   EMBL; BX572605; CAE29343.1; -; Genomic_DNA.
DR   RefSeq; WP_011159438.1; NC_005296.1.
DR   AlphaFoldDB; Q6N2Z5; -.
DR   SMR; Q6N2Z5; -.
DR   STRING; 258594.RPA3902; -.
DR   PRIDE; Q6N2Z5; -.
DR   EnsemblBacteria; CAE29343; CAE29343; RPA3902.
DR   GeneID; 66895018; -.
DR   KEGG; rpa:RPA3902; -.
DR   eggNOG; COG2063; Bacteria.
DR   HOGENOM; CLU_069313_1_2_5; -.
DR   OMA; QARISYG; -.
DR   PhylomeDB; Q6N2Z5; -.
DR   BioCyc; RPAL258594:TX73_RS19920-MON; -.
DR   Proteomes; UP000001426; 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   Reference proteome; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
FT   CHAIN           26..252
FT                   /note="Flagellar L-ring protein"
FT                   /id="PRO_0000009466"
FT   LIPID           26
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
FT   LIPID           26
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
SQ   SEQUENCE   252 AA;  27024 MW;  8F6A64C9729F58E9 CRC64;
     MSKSVPLQRI VLVAALMATG GLAGGCSSID RLAAIGERPA LTPIENPTTQ PGYKPVQMPM
     PKPEVASYNA NSLWRNGSRA FFKDQRAAKV GDILTVTVNF TDKANIANET QRSRTSKEDS
     GITDFIGSKT ITTPATAVLP GRILTTDSTS SSDGKGSVQR QEALQTNVAA VVTQVLPNGN
     LVVEGKQEIR VNFEIRELIV AGIVRPEDIQ SDNTIDSSKI AQARIAYGGR GQITDVQQPR
     YGQQVMDVLL PF