FLIM_THEMA
ID FLIM_THEMA Reviewed; 328 AA.
AC Q9WZE6; G4FDE5;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Flagellar motor switch protein FliM {ECO:0000312|EMBL:AAD35762.1};
GN Name=fliM {ECO:0000250|UniProtKB:P06974}; OrderedLocusNames=TM_0679;
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] {ECO:0000312|EMBL:AAD35762.1}
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] {ECO:0000305, ECO:0000312|PDB:2HP7}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 44-226, INTERACTION WITH CHEY,
RP AND MUTAGENESIS OF GLU-60.
RX PubMed=16882724; DOI=10.1073/pnas.0602811103;
RA Park S.Y., Lowder B., Bilwes A.M., Blair D.F., Crane B.R.;
RT "Structure of FliM provides insight into assembly of the switch complex in
RT the bacterial flagella motor.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11886-11891(2006).
RN [3] {ECO:0000305, ECO:0000312|PDB:3SOH}
RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 46-233 IN COMPLEX WITH FLIG, AND
RP INTERACTION WITH FLIG.
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 [4] {ECO:0000305, ECO:0000312|PDB:4FHR}
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 46-230 IN COMPLEX WITH FLIG, AND
RP INTERACTION WITH FLIG.
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: 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 CheX 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 -!- SUBUNIT: Interacts (via N-terminus) with unphosphorylated CheY.
CC Interacts (via central domain) with FliG (via central domain or via
CC central domain and C-terminus). {ECO:0000269|PubMed:16882724,
CC ECO:0000269|PubMed:21673656, ECO:0000269|PubMed:22896702}.
CC -!- INTERACTION:
CC Q9WZE6; Q56312: cheY; NbExp=2; IntAct=EBI-6981685, EBI-1039694;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Bacterial flagellum basal body
CC {ECO:0000250|UniProtKB:P06974}.
CC -!- SIMILARITY: Belongs to the FliM family. {ECO:0000255}.
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; AE000512; AAD35762.1; -; Genomic_DNA.
DR PIR; E72347; E72347.
DR RefSeq; NP_228487.1; NC_000853.1.
DR RefSeq; WP_004081085.1; NZ_CP011107.1.
DR PDB; 2HP7; X-ray; 2.00 A; A=44-226.
DR PDB; 3SOH; X-ray; 3.50 A; A/C=46-233.
DR PDB; 4FHR; X-ray; 1.93 A; A=46-230.
DR PDB; 4IGA; X-ray; 1.73 A; B=1-20.
DR PDB; 4QRM; X-ray; 4.32 A; A/C/E/G/I/K/M/O/Q/S/U=46-228.
DR PDBsum; 2HP7; -.
DR PDBsum; 3SOH; -.
DR PDBsum; 4FHR; -.
DR PDBsum; 4IGA; -.
DR PDBsum; 4QRM; -.
DR AlphaFoldDB; Q9WZE6; -.
DR SMR; Q9WZE6; -.
DR DIP; DIP-61248N; -.
DR IntAct; Q9WZE6; 2.
DR MINT; Q9WZE6; -.
DR STRING; 243274.THEMA_01270; -.
DR EnsemblBacteria; AAD35762; AAD35762; TM_0679.
DR KEGG; tma:TM0679; -.
DR eggNOG; COG1868; Bacteria.
DR InParanoid; Q9WZE6; -.
DR OMA; NPQFTQI; -.
DR OrthoDB; 1748746at2; -.
DR EvolutionaryTrace; Q9WZE6; -.
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:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:InterPro.
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..328
FT /note="Flagellar motor switch protein FliM"
FT /id="PRO_0000421240"
FT REGION 1..45
FT /note="Interaction with unphosphorylated CheY"
FT /evidence="ECO:0000269|PubMed:16882724"
FT MUTAGEN 60
FT /note="E->C: No appreciable effect on the binding affinity
FT for CheY."
FT /evidence="ECO:0000269|PubMed:16882724"
FT HELIX 7..16
FT /evidence="ECO:0007829|PDB:4IGA"
FT HELIX 49..73
FT /evidence="ECO:0007829|PDB:4FHR"
FT STRAND 79..88
FT /evidence="ECO:0007829|PDB:4FHR"
FT HELIX 89..95
FT /evidence="ECO:0007829|PDB:4FHR"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:4FHR"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:4FHR"
FT HELIX 120..130
FT /evidence="ECO:0007829|PDB:4FHR"
FT HELIX 145..165
FT /evidence="ECO:0007829|PDB:4FHR"
FT TURN 166..169
FT /evidence="ECO:0007829|PDB:4FHR"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:4FHR"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:4FHR"
FT STRAND 193..204
FT /evidence="ECO:0007829|PDB:4FHR"
FT STRAND 207..216
FT /evidence="ECO:0007829|PDB:4FHR"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:4FHR"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:4FHR"
FT TURN 228..232
FT /evidence="ECO:0007829|PDB:3SOH"
SQ SEQUENCE 328 AA; 37888 MW; 3E122C1FFAEBB093 CRC64;
MSDVLSQEEI NQLIEALMKG ELKEEDLLKE EEEKKVKPYD FKRPSKFSKE QLRTFQMIHE
NFGRALSTYL SGRLRTFVDV EISIDQLTYE EFIRSVMIPS FIVIFTGDVF EGSAIFEMRL
DLFYTMLDII MGGPGENPPN RPPTEIETSI MRKEVTNMLT LLAQAWSDFQ YFIPSIENVE
TNPQFVQIVP PNEIVLLVTA SVSWGEFTSF INVCWPFSLL EPLLEKLSDR FWMMGRKPEK
VEERMEELRK ASQKIPVTVQ AVIGETELRL KEILDLEVGD VIRLGTHYKD EIRIDVEGRP
KFRGIPGVFK GKYAVKVTGE FTNGGEYE
