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