FLIG_ECOL6
ID FLIG_ECOL6 Reviewed; 331 AA.
AC P0ABZ2; P31067; P76915;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Flagellar motor switch protein FliG;
GN Name=fliG; OrderedLocusNames=c2355;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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; AE014075; AAN80814.1; -; Genomic_DNA.
DR RefSeq; WP_000067950.1; NC_004431.1.
DR AlphaFoldDB; P0ABZ2; -.
DR SMR; P0ABZ2; -.
DR STRING; 199310.c2355; -.
DR EnsemblBacteria; AAN80814; AAN80814; c2355.
DR GeneID; 66674171; -.
DR KEGG; ecc:c2355; -.
DR eggNOG; COG1536; Bacteria.
DR HOGENOM; CLU_047835_2_0_6; -.
DR OMA; QVRPFEF; -.
DR BioCyc; ECOL199310:C2355-MON; -.
DR Proteomes; UP000001410; 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 PIRSF; PIRSF003161; FliG; 1.
DR PRINTS; PR00954; FLGMOTORFLIG.
DR SUPFAM; SSF48029; SSF48029; 2.
DR TIGRFAMs; TIGR00207; fliG; 1.
PE 3: Inferred from homology;
KW Bacterial flagellum; Cell inner membrane; Cell membrane; Chemotaxis;
KW Flagellar rotation; Membrane.
FT CHAIN 1..331
FT /note="Flagellar motor switch protein FliG"
FT /id="PRO_0000184091"
FT MOTIF 125..128
FT /note="Part of the EHPQR-motif"
FT SITE 160
FT /note="Part of the EHPQR-motif"
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