FLGH_BUCAP
ID FLGH_BUCAP Reviewed; 238 AA.
AC Q8K9K3;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=BUsg_331;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(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 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; AE013218; AAM67885.1; -; Genomic_DNA.
DR RefSeq; WP_011053852.1; NC_004061.1.
DR AlphaFoldDB; Q8K9K3; -.
DR SMR; Q8K9K3; -.
DR STRING; 198804.BUsg_331; -.
DR EnsemblBacteria; AAM67885; AAM67885; BUsg_331.
DR KEGG; bas:BUsg_331; -.
DR eggNOG; COG2063; Bacteria.
DR HOGENOM; CLU_069313_0_0_6; -.
DR OMA; ITQQPMT; -.
DR OrthoDB; 1900876at2; -.
DR Proteomes; UP000000416; 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..23
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
FT CHAIN 24..238
FT /note="Flagellar L-ring protein"
FT /id="PRO_0000009432"
FT LIPID 24
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
FT LIPID 24
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
SQ SEQUENCE 238 AA; 26038 MW; 7905A0171245C509 CRC64;
MVKLFSYKIK YYLTAFFIII IQSCASVEHK PLVDGITTAI APNIIPKIKN GSLFQEKTPI
NYGYQPLFED HRSHNIGDTI TVVLQENISA SNSSSSNLTR DGKANVGVTV TPGTLNPILG
LNVNDNKTGI DSIGKNDFSG KGSNSAKNTF TGLITVTVKN VLPNGNLKVI GEKQVAINQG
TEFIRFSGVI NPNNINKNNL VASTQIADTR IEYVSNNRIN DIQKMGWLQR FLLKISPI