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FLGH_WIGBR
ID   FLGH_WIGBR              Reviewed;         228 AA.
AC   Q8D3F7;
DT   23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-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=WIGBR0440;
OS   Wigglesworthia glossinidia brevipalpis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Wigglesworthia.
OX   NCBI_TaxID=36870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12219091; DOI=10.1038/ng986;
RA   Akman L., Yamashita A., Watanabe H., Oshima K., Shiba T., Hattori M.,
RA   Aksoy S.;
RT   "Genome sequence of the endocellular obligate symbiont of tsetse flies,
RT   Wigglesworthia glossinidia.";
RL   Nat. Genet. 32:402-407(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: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 membrane {ECO:0000255|HAMAP-Rule:MF_00415};
CC       Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_00415}. Bacterial flagellum
CC       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; BA000021; BAC24190.1; -; Genomic_DNA.
DR   RefSeq; WP_011069848.1; NC_004344.2.
DR   AlphaFoldDB; Q8D3F7; -.
DR   SMR; Q8D3F7; -.
DR   STRING; 36870.25165999; -.
DR   EnsemblBacteria; BAC24190; BAC24190; BAC24190.
DR   KEGG; wbr:flgH; -.
DR   eggNOG; COG2063; Bacteria.
DR   HOGENOM; CLU_069313_0_0_6; -.
DR   OMA; ITQQPMT; -.
DR   OrthoDB; 1900876at2; -.
DR   Proteomes; UP000000562; 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-UniRule.
DR   GO; GO:0005886; C:plasma 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 membrane; Lipoprotein; Membrane; Palmitate;
KW   Reference proteome; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
FT   CHAIN           18..228
FT                   /note="Flagellar L-ring protein"
FT                   /id="PRO_0000009482"
FT   LIPID           18
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
FT   LIPID           18
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
SQ   SEQUENCE   228 AA;  25316 MW;  316AEDC68143DD45 CRC64;
     MHYLRYFAIA FLLLLSSCSV TRHKPLIEGS TTTIPNTPSS NFINGSIFQQ DNSLYYGYQP
     LFEDRRPKNI GDILTVLLQE NVSASKSSSS NASRKSNANL EMNALPKIIN KIIGNDQLST
     DINSNNGFNG KGGSSAANTF SGTITVTVID ILTNGNLKVI GEKKISINQG TESIRFYGIV
     NPKTIDHNNQ VMSNLISDSK IEYIGDGYIN EVQKMNWLQR LFLNYFPF
 
 
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