FLIG_ECOLI
ID FLIG_ECOLI Reviewed; 331 AA.
AC P0ABZ1; P31067; P76915;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Flagellar motor switch protein FliG;
GN Name=fliG; Synonyms=fla AII.2, fla BII; OrderedLocusNames=b1939, JW1923;
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=8224881; DOI=10.1016/0378-1119(93)90232-r;
RA Roman S.J., Frantz B.B., Matsumura P.;
RT "Gene sequence, overproduction, purification and determination of the wild-
RT type level of the Escherichia coli flagellar switch protein FliG.";
RL Gene 133:103-108(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8631704; DOI=10.1128/jb.178.5.1289-1294.1996;
RA Marykwas D.L., Berg H.C.;
RT "A mutational analysis of the interaction between FliG and FliM, two
RT components of the flagellar motor of Escherichia coli.";
RL J. Bacteriol. 178:1289-1294(1996).
RN [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-47.
RC STRAIN=K12;
RA al Mamun A.A.M., Tominaga A., Enomoto M.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP INTERACTION WITH YCGR, HOMOOLIGOMERIZATION, AND MUTAGENESIS OF GLN-252;
RP ASP-284; ASN-292; PRO-295 AND LEU-298.
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 [8]
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: 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.
CC -!- SUBUNIT: Forms dimers and other homooligomers. Interacts with MotA via
CC residues in its C-terminus. Interacts with flagellar brake protein
CC YcgR. {ECO:0000269|PubMed:20346719}.
CC -!- INTERACTION:
CC P0ABZ1; P25798: fliF; NbExp=4; IntAct=EBI-1126524, EBI-1126492;
CC P0ABZ1; P0ABZ1: fliG; NbExp=6; IntAct=EBI-1126524, EBI-1126524;
CC P0ABZ1; P06974: fliM; NbExp=16; IntAct=EBI-1126524, EBI-560439;
CC P0ABZ1; P76010: ycgR; NbExp=3; IntAct=EBI-1126524, EBI-554507;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein;
CC Cytoplasmic side. Bacterial flagellum basal body.
CC -!- SIMILARITY: Belongs to the FliG family. {ECO:0000305}.
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DR EMBL; L13243; AAA75241.1; -; Genomic_DNA.
DR EMBL; U46011; AAB60186.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75006.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15764.1; -; Genomic_DNA.
DR EMBL; D89826; BAA14030.1; -; Genomic_DNA.
DR PIR; H64957; H64957.
DR RefSeq; NP_416449.1; NC_000913.3.
DR RefSeq; WP_000067950.1; NZ_STEB01000050.1.
DR AlphaFoldDB; P0ABZ1; -.
DR SMR; P0ABZ1; -.
DR BioGRID; 4260384; 25.
DR BioGRID; 850805; 7.
DR ComplexPortal; CPX-1082; Flagellar Motor Switch Complex, CW variant.
DR ComplexPortal; CPX-1085; Flagellar Motor Switch Complex, CCW variant.
DR DIP; DIP-408N; -.
DR IntAct; P0ABZ1; 26.
DR MINT; P0ABZ1; -.
DR STRING; 511145.b1939; -.
DR PaxDb; P0ABZ1; -.
DR PRIDE; P0ABZ1; -.
DR EnsemblBacteria; AAC75006; AAC75006; b1939.
DR EnsemblBacteria; BAA15764; BAA15764; BAA15764.
DR GeneID; 66674171; -.
DR GeneID; 946451; -.
DR KEGG; ecj:JW1923; -.
DR KEGG; eco:b1939; -.
DR PATRIC; fig|1411691.4.peg.312; -.
DR EchoBASE; EB1607; -.
DR eggNOG; COG1536; Bacteria.
DR HOGENOM; CLU_047835_2_0_6; -.
DR InParanoid; P0ABZ1; -.
DR OMA; QVRPFEF; -.
DR PhylomeDB; P0ABZ1; -.
DR BioCyc; EcoCyc:FLIG-FLAGELLAR-SWITCH-PROTEIN; -.
DR PRO; PR:P0ABZ1; -.
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; IDA:EcoCyc.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0044780; P:bacterial-type flagellum assembly; IMP:EcoCyc.
DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IMP:EcoCyc.
DR GO; GO:0071977; P:bacterial-type flagellum-dependent swimming motility; IC:ComplexPortal.
DR GO; GO:0006935; P:chemotaxis; IC:ComplexPortal.
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 PIRSF; PIRSF003161; FliG; 1.
DR PRINTS; PR00954; FLGMOTORFLIG.
DR SUPFAM; SSF48029; SSF48029; 2.
DR TIGRFAMs; TIGR00207; fliG; 1.
PE 1: Evidence at protein level;
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 FliG"
FT /id="PRO_0000184089"
FT MOTIF 125..128
FT /note="Part of the EHPQR-motif"
FT SITE 160
FT /note="Part of the EHPQR-motif"
FT MUTAGEN 252
FT /note="Q->W: Decreases binding to YcgR, significantly
FT improves motility in a pdeH disruption mutant."
FT /evidence="ECO:0000269|PubMed:20346719"
FT MUTAGEN 284
FT /note="D->W: Slightly improves motility in a pdeH
FT disruption mutant."
FT /evidence="ECO:0000269|PubMed:20346719"
FT MUTAGEN 292
FT /note="N->W: Decreases binding to YcgR, significantly
FT improves motility in a pdeH disruption mutant."
FT /evidence="ECO:0000269|PubMed:20346719"
FT MUTAGEN 295
FT /note="P->W: Decreases binding to YcgR, significantly
FT improves motility in a pdeH disruption mutant."
FT /evidence="ECO:0000269|PubMed:20346719"
FT MUTAGEN 298
FT /note="L->W: Slightly improves motility in a pdeH
FT disruption mutant."
FT /evidence="ECO:0000269|PubMed:20346719"
FT CONFLICT 159..170
FT /note="LRIATFGGVQPA -> FVSHLWRRAPS (in Ref. 1; AAA75241)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 331 AA; 36776 MW; E5CB4C0415C6E178 CRC64;
MSNLTGTDKS VILLMTIGED RAAEVFKHLS QREVQTLSAA MANVTQISNK QLTDVLAEFE
QEAEQFAALN INANDYLRSV LVKALGEERA ASLLEDILET RDTASGIETL NFMEPQSAAD
LIRDEHPQII ATILVHLKRA QAADILALFD ERLRHDVMLR IATFGGVQPA ALAELTEVLN
GLLDGQNLKR SKMGGVRTAA EIINLMKTQQ EEAVITAVRE FDGELAQKII DEMFLFENLV
DVDDRSIQRL LQEVDSESLL IALKGAEQPL REKFLRNMSQ RAADILRDDL ANRGPVRLSQ
VENEQKAILL IVRRLAETGE MVIGSGEDTY V
