ID   FLIG_BUCAP              Reviewed;         331 AA.
AC   Q8KA44;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Flagellar motor switch protein FliG;
GN   Name=fliG; OrderedLocusNames=BUsg_068;
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: FliG is one of three proteins (FliG, FliN, FliM) that forms
CC       the rotor-mounted switch complex (C ring), located at the base of the
CC       basal body. This complex interacts with the CheY and CheZ chemotaxis
CC       proteins, in addition to contacting components of the motor that
CC       determine the direction of flagellar rotation (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC       Bacterial flagellum basal body {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FliG family. {ECO:0000305}.
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DR   EMBL; AE013218; AAM67638.1; -; Genomic_DNA.
DR   RefSeq; WP_011053604.1; NC_004061.1.
DR   AlphaFoldDB; Q8KA44; -.
DR   SMR; Q8KA44; -.
DR   STRING; 198804.BUsg_068; -.
DR   EnsemblBacteria; AAM67638; AAM67638; BUsg_068.
DR   KEGG; bas:BUsg_068; -.
DR   eggNOG; COG1536; Bacteria.
DR   HOGENOM; CLU_047835_2_0_6; -.
DR   OMA; QVRPFEF; -.
DR   OrthoDB; 847822at2; -.
DR   Proteomes; UP000000416; Chromosome.
DR   GO; GO:0009425; C:bacterial-type flagellum basal body; IEA:UniProtKB-SubCell.
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   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR   InterPro; IPR000090; Flg_Motor_Flig.
DR   InterPro; IPR023087; Flg_Motor_Flig_C.
DR   InterPro; IPR011002; FliG_a-hlx.
DR   InterPro; IPR032779; FliG_M.
DR   InterPro; IPR028263; FliG_N.
DR   PANTHER; PTHR30534; PTHR30534; 1.
DR   Pfam; PF01706; FliG_C; 1.
DR   Pfam; PF14841; FliG_M; 1.
DR   Pfam; PF14842; FliG_N; 1.
DR   PRINTS; PR00954; FLGMOTORFLIG.
DR   SUPFAM; SSF48029; SSF48029; 2.
DR   TIGRFAMs; TIGR00207; fliG; 1.
PE   3: Inferred from homology;
KW   Bacterial flagellum; Cell inner membrane; Cell membrane; Chemotaxis;
KW   Flagellar rotation; Membrane.
FT   CHAIN           1..331
FT                   /note="Flagellar motor switch protein FliG"
FT                   /id="PRO_0000184086"
FT   MOTIF           125..128
FT                   /note="Part of the EHPQR-motif"
FT   SITE            160
FT                   /note="Part of the EHPQR-motif"
SQ   SEQUENCE   331 AA;  38302 MW;  B95E2A07A886E7AF CRC64;
     MTLNGTEKSA ILLMSIGADQ ASEVLKHLTP FEVQELVASM VNINQFSNTI LNTVLSECYD
     LFSKKNNLIC NNDENYISDV LTKTLGEKQG RILLNEVLET RNVKMCIETF NHMDPEKFIS
     LLDQEHPQIL TTILMYLDKR QSSKVLSRLS EKKCTEIVLR MAEFNCIKES NLIDLKKIIE
     NLLKRKKLIF SEKNGIKTVA EILNSMKIED EQNILKKINV LNKNLTRKII KEMFLFDNIV
     NIEDKYIQCL ISNLEKEKLC IALQGTSEVI RNKFFKNMNE EEANKLSIYL EEKSYISDIA
     IKNEQKLILI MLKNILDNGI FSLKKLGKYY V