FLIG_AQUAE
ID FLIG_AQUAE Reviewed; 328 AA.
AC O66891;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Flagellar motor switch protein FliG;
GN Name=fliG; OrderedLocusNames=aq_653;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS).
RX PubMed=20676082; DOI=10.1038/nature09300;
RA Lee L.K., Ginsburg M.A., Crovace C., Donohoe M., Stock D.;
RT "Structure of the torque ring of the flagellar motor and the molecular
RT basis for rotational switching.";
RL Nature 466:996-1000(2010).
CC -!- FUNCTION: FliG is one of 2 proteins (FliG, FliN) that might form the
CC rotor-mounted switch complex (C ring), located at the base of the basal
CC 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000657; AAC06845.1; -; Genomic_DNA.
DR PIR; G70357; G70357.
DR RefSeq; NP_213451.1; NC_000918.1.
DR RefSeq; WP_010880389.1; NC_000918.1.
DR PDB; 3HJL; X-ray; 2.40 A; A=1-328.
DR PDBsum; 3HJL; -.
DR AlphaFoldDB; O66891; -.
DR SMR; O66891; -.
DR STRING; 224324.aq_653; -.
DR EnsemblBacteria; AAC06845; AAC06845; aq_653.
DR KEGG; aae:aq_653; -.
DR PATRIC; fig|224324.8.peg.532; -.
DR eggNOG; COG1536; Bacteria.
DR HOGENOM; CLU_047835_1_1_0; -.
DR InParanoid; O66891; -.
DR OMA; QVRPFEF; -.
DR OrthoDB; 847822at2; -.
DR EvolutionaryTrace; O66891; -.
DR Proteomes; UP000000798; 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; IBA:GO_Central.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR InterPro; IPR001810; F-box_dom.
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 3D-structure; Bacterial flagellum; Cell inner membrane; Cell membrane;
KW Chemotaxis; Flagellar rotation; Membrane; Reference proteome.
FT CHAIN 1..328
FT /note="Flagellar motor switch protein FliG"
FT /id="PRO_0000184081"
FT MOTIF 127..130
FT /note="Part of the EHPQR-motif"
FT SITE 162
FT /note="Part of the EHPQR-motif"
FT HELIX 6..20
FT /evidence="ECO:0007829|PDB:3HJL"
FT HELIX 23..32
FT /evidence="ECO:0007829|PDB:3HJL"
FT HELIX 35..46
FT /evidence="ECO:0007829|PDB:3HJL"
FT HELIX 53..69
FT /evidence="ECO:0007829|PDB:3HJL"
FT HELIX 77..87
FT /evidence="ECO:0007829|PDB:3HJL"
FT HELIX 92..113
FT /evidence="ECO:0007829|PDB:3HJL"
FT HELIX 117..124
FT /evidence="ECO:0007829|PDB:3HJL"
FT HELIX 129..136
FT /evidence="ECO:0007829|PDB:3HJL"
FT HELIX 141..149
FT /evidence="ECO:0007829|PDB:3HJL"
FT HELIX 153..165
FT /evidence="ECO:0007829|PDB:3HJL"
FT HELIX 171..192
FT /evidence="ECO:0007829|PDB:3HJL"
FT HELIX 198..208
FT /evidence="ECO:0007829|PDB:3HJL"
FT HELIX 211..224
FT /evidence="ECO:0007829|PDB:3HJL"
FT HELIX 226..236
FT /evidence="ECO:0007829|PDB:3HJL"
FT HELIX 239..244
FT /evidence="ECO:0007829|PDB:3HJL"
FT HELIX 247..254
FT /evidence="ECO:0007829|PDB:3HJL"
FT HELIX 259..267
FT /evidence="ECO:0007829|PDB:3HJL"
FT HELIX 271..278
FT /evidence="ECO:0007829|PDB:3HJL"
FT HELIX 283..295
FT /evidence="ECO:0007829|PDB:3HJL"
FT HELIX 301..319
FT /evidence="ECO:0007829|PDB:3HJL"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:3HJL"
SQ SEQUENCE 328 AA; 37032 MW; 0C5DF04156A2C0F6 CRC64;
MAQEKSALSK AQKAAVLLLS LPEEVSMNIV KELSEEELQK LFALAKDLES VPEEEIENIA
EELLDEIKKA GIKIKKPEEF IENIKKVIPP TLAEKFRGIL ELGDAEKILK EIEKVDSRIL
ASLLKNEHPQ TIALFLSQLS PKKSAEIIQN LPEELKKEVV KRIATLENVN VQYVKELAQI
LLEEISSLGA KEALKLEGTA VAAELLNTLD KETRELILQS IGQEDPLLEE RIREKMFTFE
DIRKLSDRDI IEILKVVDKN TLMIALLGAP EDIKQKFLSN MSKRAAKLFL EDMEALGPVK
KSEIEKAQRQ VVNIIRKMID EGKIEIGD
