ID   FLGH_STRM5              Reviewed;         230 AA.
AC   B4SIL5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=Smal_1900;
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Taghavi S.,
RA   Monchy S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001111; ACF51604.1; -; Genomic_DNA.
DR   RefSeq; WP_012510987.1; NC_011071.1.
DR   AlphaFoldDB; B4SIL5; -.
DR   SMR; B4SIL5; -.
DR   STRING; 391008.Smal_1900; -.
DR   EnsemblBacteria; ACF51604; ACF51604; Smal_1900.
DR   KEGG; smt:Smal_1900; -.
DR   eggNOG; COG2063; Bacteria.
DR   HOGENOM; CLU_069313_0_1_6; -.
DR   OMA; ITQQPMT; -.
DR   OrthoDB; 1900876at2; -.
DR   BioCyc; SMAL391008:SMAL_RS09720-MON; -.
DR   Proteomes; UP000001867; 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   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
FT   CHAIN           23..230
FT                   /note="Flagellar L-ring protein"
FT                   /id="PRO_1000123960"
FT   LIPID           23
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
FT   LIPID           23
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
SQ   SEQUENCE   230 AA;  23975 MW;  A7F5C93D6B3046C9 CRC64;
     MSPLSNFART ALACAVAALL GGCVIAGDVR PYPTMAPIQP IMPPQAQPTA GAIYAAGPTL
     QLYSDRRARD VGDLLTISLL ENTTAQTSAN TATNKESNLS LGTPSIFGAP VTLGGKDILS
     ASAKGARDFT GKGNSAQSNR LQGNVTVTVI QRLPNGNLVV QGQKNLRLNQ GDELVQVQGI
     VRPGDISQDN TIPSSRVAEA RIVYGGRGPV AQSNAMGWLS RFFNSGLTPF