FLIM_BUCAI
ID FLIM_BUCAI Reviewed; 315 AA.
AC P57182;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Flagellar motor switch protein FliM;
GN Name=fliM; OrderedLocusNames=BU080;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
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; BA000003; BAB12800.1; -; Genomic_DNA.
DR RefSeq; NP_239914.1; NC_002528.1.
DR AlphaFoldDB; P57182; -.
DR SMR; P57182; -.
DR STRING; 107806.10038765; -.
DR EnsemblBacteria; BAB12800; BAB12800; BAB12800.
DR KEGG; buc:BU080; -.
DR PATRIC; fig|107806.10.peg.86; -.
DR eggNOG; COG1868; Bacteria.
DR HOGENOM; CLU_051805_0_0_6; -.
DR OMA; CKMGESK; -.
DR Proteomes; UP000001806; 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; IPR001543; FliN-like_C.
DR InterPro; IPR036429; SpoA-like_sf.
DR Pfam; PF02154; FliM; 1.
DR Pfam; PF01052; FliMN_C; 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..315
FT /note="Flagellar motor switch protein FliM"
FT /id="PRO_0000180924"
SQ SEQUENCE 315 AA; 36940 MW; FE5CC11D9573F198 CRC64;
MLACLLITFT CEACKMGESK NLHDEIKILE KINRHFSDEF TKFFSNFLKN SVELVSCSIK
IGSCTSNKEI ITNLRCLNLI EILPYKKKSF IIFPYNFLSN IIDILFGGQG DFKDHTKKIR
DITSTESLVN KKIMKFITNA FSEIYKKYFV KEINFFNTKT FFDFKKYNFD LNKLFLINCF
NFKINNTEIF FNFLIPKSIL KYQNEKKFFS TYDSHKNTCI EKNIENKVSL NDIYNVEVNI
ISKIIGISVS YDKIYNLSIG DVLSIKKPNK ITGFIQDQAI FLGNYKRFNE QSIIFIEEFI
DSSSESNQDK EYSNE