ID   FLIM_BUCBP              Reviewed;         331 AA.
AC   Q89AZ4;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Flagellar motor switch protein FliM;
GN   Name=fliM; OrderedLocusNames=bbp_074;
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: FliM 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}. Bacterial flagellum basal body
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FliM family. {ECO:0000305}.
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DR   EMBL; AE016826; AAO26810.1; -; Genomic_DNA.
DR   RefSeq; WP_011091211.1; NC_004545.1.
DR   AlphaFoldDB; Q89AZ4; -.
DR   SMR; Q89AZ4; -.
DR   STRING; 224915.bbp_074; -.
DR   EnsemblBacteria; AAO26810; AAO26810; bbp_074.
DR   GeneID; 56470618; -.
DR   KEGG; bab:bbp_074; -.
DR   eggNOG; COG1868; Bacteria.
DR   HOGENOM; CLU_838567_0_0_6; -.
DR   OMA; CKMGESK; -.
DR   OrthoDB; 1748746at2; -.
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   Gene3D; 3.40.1550.10; -; 1.
DR   InterPro; IPR028976; CheC-like_sf.
DR   InterPro; IPR001689; Flag_FliM.
DR   InterPro; IPR036429; SpoA-like_sf.
DR   Pfam; PF02154; FliM; 1.
DR   SUPFAM; SSF101801; SSF101801; 1.
PE   3: Inferred from homology;
KW   Bacterial flagellum; Cell inner membrane; Cell membrane; Chemotaxis;
KW   Flagellar rotation; Membrane; Reference proteome.
FT   CHAIN           1..331
FT                   /note="Flagellar motor switch protein FliM"
FT                   /id="PRO_0000180926"
SQ   SEQUENCE   331 AA;  38924 MW;  0014DD8FF8B169E4 CRC64;
     MQSDVISRVK KIYIKNKIDI SSKIFPYYQT TDYYLTYHNM KDRLENMHEC FLKQFTKHIS
     EYSDVDCKIS FYKFIIQKFK NIKKNIKNNS ISDCFEISPY KKLGIIFVSD NISDYLIEYL
     FGGCELKNSS NGLFKKLTLS TINIVKKMFK IILEQYYFLW NKVSLCKMKL ILNRLQNLNE
     ISNVNFINSK DTFVTFLFRL RIANKFGMLG ICLPTSLSFQ CNNEADVNSV HNVSHISYDN
     VVNTEIRKRL FQVIVYNCKI VLKIVLIENY ITLSKIIAFK VGDILPIHML DNVVAYSENV
     PILIGKYKMF KNKYVFCVVD YYNSTLNYKN G