FLIM_SALTY
ID FLIM_SALTY Reviewed; 334 AA.
AC P26418;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Flagellar motor switch protein FliM;
GN Name=fliM; Synonyms=cheC2, fla AII, fla QII; OrderedLocusNames=STM1976;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2656645; DOI=10.1128/jb.171.6.3247-3257.1989;
RA Kihara M., Homma M., Kutsukake K., Macnab R.M.;
RT "Flagellar switch of Salmonella typhimurium: gene sequences and deduced
RT protein sequences.";
RL J. Bacteriol. 171:3247-3257(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP MUTAGENESIS OF ASN-155 AND LEU-160.
RC STRAIN=ATCC 14028 / SGSC 2980 / CDC 6516-60 / NCTC 12023;
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).
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 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; Peripheral membrane protein.
CC Bacterial flagellum basal body.
CC -!- SIMILARITY: Belongs to the FliM family. {ECO:0000305}.
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DR EMBL; M24463; AAA27104.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20888.1; -; Genomic_DNA.
DR PIR; C44513; C30929.
DR RefSeq; NP_460929.1; NC_003197.2.
DR RefSeq; WP_000502811.1; NC_003197.2.
DR PDB; 4YXB; X-ray; 2.56 A; A/B=245-334.
DR PDB; 4YXC; X-ray; 2.30 A; B=245-334.
DR PDBsum; 4YXB; -.
DR PDBsum; 4YXC; -.
DR AlphaFoldDB; P26418; -.
DR SMR; P26418; -.
DR IntAct; P26418; 1.
DR STRING; 99287.STM1976; -.
DR PaxDb; P26418; -.
DR EnsemblBacteria; AAL20888; AAL20888; STM1976.
DR GeneID; 1253497; -.
DR GeneID; 66756493; -.
DR KEGG; stm:STM1976; -.
DR PATRIC; fig|99287.12.peg.2093; -.
DR HOGENOM; CLU_052646_1_2_6; -.
DR OMA; NPQFTQI; -.
DR PhylomeDB; P26418; -.
DR BioCyc; SENT99287:STM1976-MON; -.
DR Proteomes; UP000001014; 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..334
FT /note="Flagellar motor switch protein FliM"
FT /id="PRO_0000180929"
FT REGION 15..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 155
FT /note="N->E: Altered motor bias with clockwise rotation,
FT partially suppresses a yhjH disruption."
FT /evidence="ECO:0000269|PubMed:20346719"
FT MUTAGEN 160
FT /note="L->D: Altered motor bias with clockwise rotation,
FT partially suppresses a yhjH disruption."
FT /evidence="ECO:0000269|PubMed:20346719"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:4YXB"
FT STRAND 259..271
FT /evidence="ECO:0007829|PDB:4YXC"
FT HELIX 272..276
FT /evidence="ECO:0007829|PDB:4YXC"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:4YXC"
FT STRAND 290..296
FT /evidence="ECO:0007829|PDB:4YXC"
FT STRAND 299..309
FT /evidence="ECO:0007829|PDB:4YXC"
FT STRAND 312..322
FT /evidence="ECO:0007829|PDB:4YXC"
SQ SEQUENCE 334 AA; 37858 MW; 64E2F63FE9A6D06A CRC64;
MGDSILSQAE IDALLNGDSD TKDEPTPGIA SDSDIRPYDP NTQRRVVRER LQALEIINER
FARQFRMGLF NLLRRSPDIT VGAIRIQPYH EFARNLPVPT NLNLIHLKPL RGTGLVVFSP
SLVFIAVDNL FGGDGRFPTK VEGREFTHTE QRVINRMLKL ALEGYSDAWK AINPLEVEYV
RSEMQVKFTN ITTSPNDIVV NTPFHVEIGN LTGEFNICLP FSMIEPLREL LVNPPLENSR
HEDQNWRDNL VRQVQHSELE LVANFADIPL RLSQILKLKP GDVLPIEKPD RIIAHVDGVP
VLTSQYGTVN GQYALRVEHL INPILNSLNE EQPK
