FLIM_ECOLI
ID FLIM_ECOLI Reviewed; 334 AA.
AC P06974;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 25-MAY-2022, entry version 174.
DE RecName: Full=Flagellar motor switch protein FliM;
GN Name=fliM; Synonyms=cheC2, fla AII, fla QII;
GN OrderedLocusNames=b1945, JW1929;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3519573; DOI=10.1128/jb.166.3.1007-1012.1986;
RA Kuo S.C., Koshland D.E. Jr.;
RT "Sequence of the flaA (cheC) locus of Escherichia coli and discovery of a
RT new gene.";
RL J. Bacteriol. 166:1007-1012(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 327-334.
RC STRAIN=K12;
RX PubMed=2651416; DOI=10.1128/jb.171.5.2728-2734.1989;
RA Malakooti J., Komeda Y., Matsumura P.;
RT "DNA sequence analysis, gene product identification, and localization of
RT flagellar motor components of Escherichia coli.";
RL J. Bacteriol. 171:2728-2734(1989).
RN [6]
RP INTERACTION WITH YCRG, AND MUTAGENESIS OF VAL-153; ASN-155; ARG-156;
RP LEU-160; ASP-167 AND GLU-176.
RC STRAIN=K12 / RP3098;
RX PubMed=20346719; DOI=10.1016/j.molcel.2010.03.001;
RA Paul K., Nieto V., Carlquist W.C., Blair D.F., Harshey R.M.;
RT "The c-di-GMP binding protein YcgR controls flagellar motor direction and
RT speed to affect chemotaxis by a 'backstop brake' mechanism.";
RL Mol. Cell 38:128-139(2010).
RN [7]
RP REVIEW.
RX PubMed=19081534; DOI=10.1016/s1937-6448(08)01402-0;
RA Terashima H., Kojima S., Homma M.;
RT "Flagellar motility in bacteria structure and function of flagellar
RT motor.";
RL Int. Rev. Cytol. 270:39-85(2008).
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.
CC -!- SUBUNIT: Interacts with flagellar brake protein YcgR.
CC {ECO:0000269|PubMed:20346719}.
CC -!- INTERACTION:
CC P06974; P0ABZ1: fliG; NbExp=16; IntAct=EBI-560439, EBI-1126524;
CC P06974; P15070: fliN; NbExp=7; IntAct=EBI-560439, EBI-2011987;
CC P06974; P76010: ycgR; NbExp=3; IntAct=EBI-560439, EBI-554507;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein.
CC Bacterial flagellum basal body.
CC -!- SIMILARITY: Belongs to the FliM family. {ECO:0000305}.
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DR EMBL; M12784; AAA23786.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75012.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15770.1; -; Genomic_DNA.
DR EMBL; M26294; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR PIR; B29842; XMECF2.
DR RefSeq; NP_416455.1; NC_000913.3.
DR RefSeq; WP_001350520.1; NZ_LN832404.1.
DR PDB; 1F4V; X-ray; 2.22 A; D/E/F=1-16.
DR PDB; 1U8T; X-ray; 1.50 A; E/F=1-16.
DR PDB; 2B1J; X-ray; 2.40 A; C/D=1-16.
DR PDBsum; 1F4V; -.
DR PDBsum; 1U8T; -.
DR PDBsum; 2B1J; -.
DR AlphaFoldDB; P06974; -.
DR SMR; P06974; -.
DR BioGRID; 4261570; 21.
DR BioGRID; 850797; 5.
DR ComplexPortal; CPX-1082; Flagellar Motor Switch Complex, CW variant.
DR ComplexPortal; CPX-1085; Flagellar Motor Switch Complex, CCW variant.
DR DIP; DIP-1100N; -.
DR IntAct; P06974; 18.
DR MINT; P06974; -.
DR STRING; 511145.b1945; -.
DR PaxDb; P06974; -.
DR PRIDE; P06974; -.
DR EnsemblBacteria; AAC75012; AAC75012; b1945.
DR EnsemblBacteria; BAA15770; BAA15770; BAA15770.
DR GeneID; 946442; -.
DR KEGG; ecj:JW1929; -.
DR KEGG; eco:b1945; -.
DR PATRIC; fig|1411691.4.peg.306; -.
DR EchoBASE; EB0319; -.
DR eggNOG; COG1868; Bacteria.
DR HOGENOM; CLU_052646_1_2_6; -.
DR InParanoid; P06974; -.
DR OMA; NPQFTQI; -.
DR PhylomeDB; P06974; -.
DR BioCyc; EcoCyc:FLIM-FLAGELLAR-C-RING-SWITCH; -.
DR EvolutionaryTrace; P06974; -.
DR PRO; PR:P06974; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009288; C:bacterial-type flagellum; IC:ComplexPortal.
DR GO; GO:0009433; C:bacterial-type flagellum basal body, C ring; IC:ComplexPortal.
DR GO; GO:0120107; C:bacterial-type flagellum rotor complex; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR GO; GO:0071977; P:bacterial-type flagellum-dependent swimming motility; IC:ComplexPortal.
DR GO; GO:0006935; P:chemotaxis; IC:ComplexPortal.
DR GO; GO:0050918; P:positive chemotaxis; IBA:GO_Central.
DR CDD; cd17908; FliM; 1.
DR Gene3D; 2.30.330.10; -; 1.
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 PIRSF; PIRSF002888; FliM; 1.
DR PRINTS; PR00955; FLGMOTORFLIM.
DR SUPFAM; SSF101801; SSF101801; 1.
DR SUPFAM; SSF103039; SSF103039; 1.
DR TIGRFAMs; TIGR01397; fliM_switch; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Bacterial flagellum; Cell inner membrane; Cell membrane;
KW Chemotaxis; Flagellar rotation; Membrane; Reference proteome.
FT CHAIN 1..334
FT /note="Flagellar motor switch protein FliM"
FT /id="PRO_0000180928"
FT MUTAGEN 153
FT /note="V->D: Decreases binding to YcgR."
FT /evidence="ECO:0000269|PubMed:20346719"
FT MUTAGEN 155
FT /note="N->E: Decreases binding to YcgR."
FT /evidence="ECO:0000269|PubMed:20346719"
FT MUTAGEN 156
FT /note="R->D: Obviates binding to YcgR."
FT /evidence="ECO:0000269|PubMed:20346719"
FT MUTAGEN 160
FT /note="L->E: Obviates binding to YcgR."
FT /evidence="ECO:0000269|PubMed:20346719"
FT MUTAGEN 167
FT /note="D->R: Decreases binding to YcgR."
FT /evidence="ECO:0000269|PubMed:20346719"
FT MUTAGEN 176
FT /note="E->R: Decreases binding to YcgR."
FT /evidence="ECO:0000269|PubMed:20346719"
FT HELIX 8..15
FT /evidence="ECO:0007829|PDB:1U8T"
SQ SEQUENCE 334 AA; 37849 MW; 05DC012B9364BFD6 CRC64;
MGDSILSQAE IDALLNGDSE VKDEPTASVS GESDIRPYDP NTQRRVVRER LQALEIINER
FARHFRMGLF NLLRRSPDIT VGAIRIQPYH EFARNLPVPT NLNLIHLKPL RGTGLVVFSP
SLVFIAVDNL FGGDGRFPTK VEGREFTHTE QRVINRMLKL ALEGYSDAWK AINPLEVEYV
RSEMQVKFTN ITTSPNDIVV NTPFHVEIGN LTGEFNICLP FSMIEPLREL LVNPPLENSR
NEDQNWRDNL VRQVQHSQLE LVANFADISL RLSQILKLNP GDVLPIEKPD RIIAHVDGVP
VLTSQYGTLN GQYALRIEHL INPILNSLNE EQPK
