FLIG_THEMA
ID FLIG_THEMA Reviewed; 335 AA.
AC Q9WY63;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 146.
DE RecName: Full=Flagellar motor switch protein FliG;
GN Name=fliG; OrderedLocusNames=TM_0220;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP PROTEIN SEQUENCE OF 209-214, AND X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF
RP 235-335.
RX PubMed=10440379; DOI=10.1038/22794;
RA Lloyd S.A., Whitby F.G., Blair D.F., Hill C.P.;
RT "Structure of the C-terminal domain of FliG, a component of the rotor in
RT the bacterial flagellar motor.";
RL Nature 400:472-475(1999).
RN [3]
RP SUBUNIT, INTERACTION WITH FLIF, AND NMR AND FLUORESCENCE SPECTROSCOPY OF
RP N-TERMINUS.
RX PubMed=22670715; DOI=10.1021/bi3004582;
RA Levenson R., Zhou H., Dahlquist F.W.;
RT "Structural insights into the interaction between the bacterial flagellar
RT motor proteins FliF and FliG.";
RL Biochemistry 51:5052-5060(2012).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 104-335.
RX PubMed=12093724; DOI=10.1093/emboj/cdf332;
RA Brown P.N., Hill C.P., Blair D.F.;
RT "Crystal structure of the middle and C-terminal domains of the flagellar
RT rotor protein FliG.";
RL EMBO J. 21:3225-3234(2002).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 117-193 IN COMPLEX WITH FLIM,
RP INTERACTION WITH FLIM, AND MOTIF.
RX PubMed=21673656; DOI=10.1038/emboj.2011.188;
RA Paul K., Gonzalez-Bonet G., Bilwes A.M., Crane B.R., Blair D.;
RT "Architecture of the flagellar rotor.";
RL EMBO J. 30:2962-2971(2011).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 104-335 OF MUTANT DEL 170-172.
RX PubMed=21572987; DOI=10.1371/journal.pbio.1000616;
RA Minamino T., Imada K., Kinoshita M., Nakamura S., Morimoto Y.V., Namba K.;
RT "Structural insight into the rotational switching mechanism of the
RT bacterial flagellar motor.";
RL PLoS Biol. 9:E1000616-E1000616(2011).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 115-327 IN COMPLEX WITH FLIM, AND
RP INTERACTION WITH FLIM.
RX PubMed=22896702; DOI=10.1074/jbc.c112.378380;
RA Vartanian A.S., Paz A., Fortgang E.A., Abramson J., Dahlquist F.W.;
RT "Structure of flagellar motor proteins in complex allows for insights into
RT motor structure and switching.";
RL J. Biol. Chem. 287:35779-35783(2012).
CC -!- FUNCTION: One of the proteins that forms a switch complex that is
CC proposed to be located at the base of the basal body. This complex
CC interacts with chemotaxis proteins (such as CheY) in addition to
CC contacting components of the motor that determine the direction of
CC flagellar rotation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer in the absence of FliF. Interacts (via N-terminus)
CC with FliF (via C-terminus) forming a heterodimer. Interacts (via
CC central domain or via central domain and C-terminus) with FliM (via
CC central domain). {ECO:0000269|PubMed:21673656,
CC ECO:0000269|PubMed:22670715, ECO:0000269|PubMed:22896702}.
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; AE000512; AAD35312.1; -; Genomic_DNA.
DR PIR; F72404; F72404.
DR RefSeq; NP_228035.1; NC_000853.1.
DR RefSeq; WP_004082903.1; NZ_CP011107.1.
DR PDB; 1LKV; X-ray; 2.80 A; X=104-335.
DR PDB; 1QC7; X-ray; 2.20 A; A/B=235-335.
DR PDB; 3AJC; X-ray; 2.30 A; A=104-335.
DR PDB; 3SOH; X-ray; 3.50 A; B/D=117-193.
DR PDB; 4FHR; X-ray; 1.93 A; B=115-327.
DR PDB; 4QRM; X-ray; 4.32 A; B/D/F/H/J/L/N/P/R/T/V=117-187.
DR PDB; 5TDY; X-ray; 2.10 A; B/D=1-98.
DR PDBsum; 1LKV; -.
DR PDBsum; 1QC7; -.
DR PDBsum; 3AJC; -.
DR PDBsum; 3SOH; -.
DR PDBsum; 4FHR; -.
DR PDBsum; 4QRM; -.
DR PDBsum; 5TDY; -.
DR AlphaFoldDB; Q9WY63; -.
DR BMRB; Q9WY63; -.
DR SMR; Q9WY63; -.
DR IntAct; Q9WY63; 1.
DR MINT; Q9WY63; -.
DR STRING; 243274.THEMA_03625; -.
DR EnsemblBacteria; AAD35312; AAD35312; TM_0220.
DR KEGG; tma:TM0220; -.
DR eggNOG; COG1536; Bacteria.
DR InParanoid; Q9WY63; -.
DR OMA; QVRPFEF; -.
DR OrthoDB; 847822at2; -.
DR EvolutionaryTrace; Q9WY63; -.
DR Proteomes; UP000008183; 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:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
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; 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; Direct protein sequencing; Flagellar rotation; Membrane;
KW Reference proteome.
FT CHAIN 1..335
FT /note="Flagellar motor switch protein FliG"
FT /id="PRO_0000184097"
FT MOTIF 126..129
FT /note="Part of the EHPQR-motif; important for interaction
FT with FliM"
FT SITE 161
FT /note="Part of the EHPQR-motif; important for interaction
FT with FliM"
FT HELIX 8..19
FT /evidence="ECO:0007829|PDB:5TDY"
FT HELIX 21..28
FT /evidence="ECO:0007829|PDB:5TDY"
FT HELIX 33..44
FT /evidence="ECO:0007829|PDB:5TDY"
FT HELIX 51..66
FT /evidence="ECO:0007829|PDB:5TDY"
FT HELIX 75..87
FT /evidence="ECO:0007829|PDB:5TDY"
FT HELIX 89..95
FT /evidence="ECO:0007829|PDB:5TDY"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:3AJC"
FT HELIX 116..123
FT /evidence="ECO:0007829|PDB:4FHR"
FT HELIX 128..136
FT /evidence="ECO:0007829|PDB:4FHR"
FT HELIX 140..148
FT /evidence="ECO:0007829|PDB:4FHR"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:4FHR"
FT HELIX 155..164
FT /evidence="ECO:0007829|PDB:4FHR"
FT HELIX 170..183
FT /evidence="ECO:0007829|PDB:4FHR"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:3SOH"
FT HELIX 198..207
FT /evidence="ECO:0007829|PDB:4FHR"
FT HELIX 210..223
FT /evidence="ECO:0007829|PDB:4FHR"
FT HELIX 225..235
FT /evidence="ECO:0007829|PDB:4FHR"
FT HELIX 238..243
FT /evidence="ECO:0007829|PDB:4FHR"
FT HELIX 246..253
FT /evidence="ECO:0007829|PDB:4FHR"
FT HELIX 258..265
FT /evidence="ECO:0007829|PDB:4FHR"
FT HELIX 270..277
FT /evidence="ECO:0007829|PDB:4FHR"
FT HELIX 282..294
FT /evidence="ECO:0007829|PDB:4FHR"
FT HELIX 300..319
FT /evidence="ECO:0007829|PDB:4FHR"
SQ SEQUENCE 335 AA; 37816 MW; 64C41D122622ABDA CRC64;
MPEKKIDGRR KAAVLLVALG PEKAAQVMKH LDEETVEQLV VEIANIGRVT PEEKKQVLEE
FLSLAKAKEM ISEGGIEYAK KVLEKAFGPE RARKIIERLT SSLQVKPFSF VRDTDPVQLV
NFLQSEHPQT IAVVLSYLDP PVAAQILGAL PEELQTEVLK RIALLERTSP EVVKEIERNL
EKKISGFVSR TFSKVGGIDT AAEIMNNLDR TTEKKIMDKL VQENPELADE IRRRMFVFED
ILKLDDRSIQ LVLREVDTRD LALALKGASD ELKEKIFKNM SKRAAALLKD ELEYMGPVRL
KDVEEAQQKI INIIRRLEEA GEIVIARGGG EELIM
