ID   FLIG_BUCBP              Reviewed;         320 AA.
AC   Q89AZ9;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Flagellar motor switch protein FliG;
GN   Name=fliG; OrderedLocusNames=bbp_069;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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; AE016826; AAO26805.1; -; Genomic_DNA.
DR   RefSeq; WP_011091206.1; NC_004545.1.
DR   AlphaFoldDB; Q89AZ9; -.
DR   SMR; Q89AZ9; -.
DR   STRING; 224915.bbp_069; -.
DR   EnsemblBacteria; AAO26805; AAO26805; bbp_069.
DR   GeneID; 56470613; -.
DR   KEGG; bab:bbp_069; -.
DR   eggNOG; COG1536; Bacteria.
DR   HOGENOM; CLU_047835_2_0_6; -.
DR   OMA; QVRPFEF; -.
DR   OrthoDB; 847822at2; -.
DR   Proteomes; UP000000601; 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.
PE   3: Inferred from homology;
KW   Bacterial flagellum; Cell inner membrane; Cell membrane; Chemotaxis;
KW   Flagellar rotation; Membrane; Reference proteome.
FT   CHAIN           1..320
FT                   /note="Flagellar motor switch protein FliG"
FT                   /id="PRO_0000184087"
FT   MOTIF           126..129
FT                   /note="Part of the EHPQR-motif"
FT   SITE            161
FT                   /note="Part of the EHPQR-motif"
SQ   SEQUENCE   320 AA;  37071 MW;  82F74CDEE72DE287 CRC64;
     MNLNGEQKSA VLLALVGIDK AIEILKELSI QEIENIAKCM SYMDVISSIT ADLVLSEFCN
     EVRINKDQNI SFINNNFIIS LLKKVLGEHH AVLLLDKFKN QKNISDNIKK LNLINPEKIV
     SLIKGEHPQI IATILIYLNR NHAANILSYF EDNLSLDIIR RIANFSSLKK LGQEEFVKII
     DNLINKYQNS MLNQQGIVTA VELLKLIKRD QETKILTKMF SSDKVLAKRI KTKMLEFSDI
     INLDDVYIRR LIKVFPLYEL SEIMKVEKEE FKKKFYKNMS LENTNLIKNY CSKKIFISND
     LIQKKRNNLL NSVKKILYNS