ID FLIF_SALTY Reviewed; 560 AA.
AC P15928;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 27-MAR-2024, entry version 139.
DE RecName: Full=Flagellar M-ring protein;
GN Name=fliF; Synonyms=fla AII.1, fla BI; OrderedLocusNames=STM1969;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2544561; DOI=10.1128/jb.171.7.3890-3900.1989;
RA Jones C.J., Homma M., Macnab R.M.;
RT "L-, P-, and M-ring proteins of the flagellar basal body of Salmonella
RT typhimurium: gene sequences and deduced protein sequences.";
RL J. Bacteriol. 171:3890-3900(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
RC STRAIN=SJW1103;
RX PubMed=1551848; DOI=10.1128/jb.174.7.2298-2304.1992;
RA Mueller V., Jones C.J., Kawagishi I., Aizawa S., Macnab R.M.;
RT "Characterization of the fliE genes of Escherichia coli and Salmonella
RT typhimurium and identification of the FliE protein as a component of the
RT flagellar hook-basal body complex.";
RL J. Bacteriol. 174:2298-2304(1992).
RN [4]
RP INDUCTION.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=21278297; DOI=10.1128/jb.01494-10;
RA Wada T., Morizane T., Abo T., Tominaga A., Inoue-Tanaka K., Kutsukake K.;
RT "EAL domain protein YdiV acts as an anti-FlhD4C2 factor responsible for
RT nutritional control of the flagellar regulon in Salmonella enterica Serovar
RT Typhimurium.";
RL J. Bacteriol. 193:1600-1611(2011).
CC -!- FUNCTION: The M ring may be actively involved in energy transduction.
CC -!- SUBUNIT: The basal body constitutes a major portion of the flagellar
CC organelle and consists of four rings (L,P,S, and M) mounted on a
CC central rod. The M ring is integral to the inner membrane of the cell
CC and may be connected to the flagellar rod via the S ring. The S
CC (supramembrane ring) lies just distal to the M ring. The L and P rings
CC lie in the outer membrane and the periplasmic space, respectively.
CC -!- INTERACTION:
CC P15928; P0A1J9: fliG; NbExp=4; IntAct=EBI-2012119, EBI-2012130;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC Bacterial flagellum basal body.
CC -!- INDUCTION: Inhibited in nutrient-poor medium.
CC {ECO:0000269|PubMed:21278297}.
CC -!- SIMILARITY: Belongs to the FliF 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; M24462; AAA27096.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20881.1; -; Genomic_DNA.
DR EMBL; M84993; AAA27094.1; -; Genomic_DNA.
DR PIR; C32887; D30930.
DR RefSeq; NP_460922.1; NC_003197.2.
DR RefSeq; WP_001276834.1; NC_003197.2.
DR PDB; 6SCN; EM; 3.10 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d=1-560.
DR PDB; 6SD1; EM; 2.60 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d=1-560.
DR PDB; 6SD2; EM; 3.10 A; A/C/D/F/G/I/J/L/N/O/Q/R/T/U/W/Y/Z/b/c/e/f=1-560.
DR PDB; 6SD3; EM; 3.30 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d=1-560.
DR PDB; 6SD4; EM; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d=1-560.
DR PDB; 6SD5; EM; 3.10 A; A/C/D/F/G/I/J/L/M/O/P/R/T/U/W/X/Z/a/c/d/f/g=1-560.
DR PDB; 6TRE; EM; 3.30 A; 1/2/3/4/5/6/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-560.
DR PDB; 7BK0; EM; 3.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d=1-560.
DR PDB; 7CG0; EM; 3.20 A; 5/6/7/8/9=311-331.
DR PDB; 7CG7; EM; 3.61 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d=1-560.
DR PDB; 7D84; EM; 3.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d=1-560.
DR PDB; 7E80; EM; 3.67 A; 5/6/7/8/9=311-331.
DR PDB; 7E81; EM; 4.50 A; Ca/Cb/Cc/Cd/Ce/Cf/Ch/Ci/Cj/Ck/Cl/Cm/Cn/Co/Cp/Cq/Cr/Cs/Ct/Cu/Cv/Cw/Cx/Cy/Cz/Da/Db/Dc/Dd/De=1-560.
DR PDB; 7E82; EM; 3.30 A; 5/6/7/8/9=311-331.
DR PDB; 7NVG; EM; 3.70 A; A1/B1/C1/D1/E1/F1/G1/H1/I1/J1/K1/L1/M1/N1/O1/P1/Q1/R1/S1/T1/U1/V1/W1/X1/Y1/Z1/a1/b1/c1/d1=1-560.
DR PDB; 8FTE; EM; 3.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/V/W=1-560.
DR PDB; 8FTF; EM; 2.90 A; A/AA/B/BA/C/CA/D/DA/E/EA/F/FA/G/GA/H/HA/I/J/K/L/M/N/O/P/Q/R/S/T/V/W=1-560.
DR PDBsum; 6SCN; -.
DR PDBsum; 6SD1; -.
DR PDBsum; 6SD2; -.
DR PDBsum; 6SD3; -.
DR PDBsum; 6SD4; -.
DR PDBsum; 6SD5; -.
DR PDBsum; 6TRE; -.
DR PDBsum; 7BK0; -.
DR PDBsum; 7CG0; -.
DR PDBsum; 7CG7; -.
DR PDBsum; 7D84; -.
DR PDBsum; 7E80; -.
DR PDBsum; 7E81; -.
DR PDBsum; 7E82; -.
DR PDBsum; 7NVG; -.
DR PDBsum; 8FTE; -.
DR PDBsum; 8FTF; -.
DR AlphaFoldDB; P15928; -.
DR EMDB; EMD-10143; -.
DR EMDB; EMD-10145; -.
DR EMDB; EMD-10146; -.
DR EMDB; EMD-10147; -.
DR EMDB; EMD-10148; -.
DR EMDB; EMD-10149; -.
DR EMDB; EMD-10560; -.
DR EMDB; EMD-12195; -.
DR EMDB; EMD-12603; -.
DR EMDB; EMD-30348; -.
DR EMDB; EMD-30351; -.
DR EMDB; EMD-30612; -.
DR EMDB; EMD-31006; -.
DR EMDB; EMD-31007; -.
DR EMDB; EMD-31008; -.
DR SMR; P15928; -.
DR IntAct; P15928; 2.
DR STRING; 99287.STM1969; -.
DR TCDB; 3.A.6.2.1; the type iii (virulence-related) secretory pathway (iiisp) family.
DR PaxDb; 99287-STM1969; -.
DR GeneID; 1253490; -.
DR KEGG; stm:STM1969; -.
DR PATRIC; fig|99287.12.peg.2086; -.
DR HOGENOM; CLU_028108_1_0_6; -.
DR OMA; INYEVNR; -.
DR PhylomeDB; P15928; -.
DR BioCyc; SENT99287:STM1969-MONOMER; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0009431; C:bacterial-type flagellum basal body, MS ring; IEA:InterPro.
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 Gene3D; 3.30.300.30; -; 1.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR013556; Flag_M-ring_C.
DR InterPro; IPR000067; FlgMring_FliF.
DR InterPro; IPR006182; FliF_N_dom.
DR InterPro; IPR043427; YscJ/FliF.
DR NCBIfam; TIGR00206; fliF; 1.
DR PANTHER; PTHR30046; FLAGELLAR M-RING PROTEIN; 1.
DR PANTHER; PTHR30046:SF0; FLAGELLAR M-RING PROTEIN; 1.
DR Pfam; PF01514; YscJ_FliF; 1.
DR Pfam; PF08345; YscJ_FliF_C; 1.
DR PIRSF; PIRSF004862; FliF; 1.
DR PRINTS; PR01009; FLGMRINGFLIF.
PE 1: Evidence at protein level;
KW 3D-structure; Bacterial flagellum; Cell inner membrane; Cell membrane;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..560
FT /note="Flagellar M-ring protein"
FT /id="PRO_0000180883"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 304..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 126..145
FT /evidence="ECO:0007829|PDB:6SCN"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:6SCN"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:6SCN"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:6SCN"
FT HELIX 188..199
FT /evidence="ECO:0007829|PDB:6SCN"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:6SCN"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:6SCN"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:6SCN"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:6SCN"
FT TURN 222..225
FT /evidence="ECO:0007829|PDB:6SCN"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:6SCN"
FT HELIX 232..252
FT /evidence="ECO:0007829|PDB:6SD1"
FT HELIX 254..257
FT /evidence="ECO:0007829|PDB:6SD1"
FT STRAND 259..271
FT /evidence="ECO:0007829|PDB:6SD1"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:6SD1"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:6SD1"
FT STRAND 292..302
FT /evidence="ECO:0007829|PDB:6SD1"
FT STRAND 316..319
FT /evidence="ECO:0007829|PDB:7CG0"
FT STRAND 358..367
FT /evidence="ECO:0007829|PDB:6SD1"
FT STRAND 370..376
FT /evidence="ECO:0007829|PDB:6SD1"
FT STRAND 381..391
FT /evidence="ECO:0007829|PDB:6SD1"
FT HELIX 406..420
FT /evidence="ECO:0007829|PDB:6SD1"
FT TURN 424..427
FT /evidence="ECO:0007829|PDB:6SD1"
FT STRAND 429..434
FT /evidence="ECO:0007829|PDB:6SD1"
SQ SEQUENCE 560 AA; 61230 MW; 7A5011F4EF17B488 CRC64;
MSATASTATQ PKPLEWLNRL RANPRIPLIV AGSAAVAIVV AMVLWAKTPD YRTLFSNLSD
QDGGAIVAQL TQMNIPYRFA NGSGAIEVPA DKVHELRLRL AQQGLPKGGA VGFELLDQEK
FGISQFSEQV NYQRALEGEL ARTIETLGPV KSARVHLAMP KPSLFVREQK SPSASVTVTL
EPGRALDEGQ ISAVVHLVSS AVAGLPPGNV TLVDQSGHLL TQSNTSGRDL NDAQLKFAND
VESRIQRRIE AILSPIVGNG NVHAQVTAQL DFANKEQTEE HYSPNGDASK ATLRSRQLNI
SEQVGAGYPG GVPGALSNQP APPNEAPIAT PPTNQQNAQN TPQTSTSTNS NSAGPRSTQR
NETSNYEVDR TIRHTKMNVG DIERLSVAVV VNYKTLADGK PLPLTADQMK QIEDLTREAM
GFSDKRGDTL NVVNSPFSAV DNTGGELPFW QQQSFIDQLL AAGRWLLVLV VAWILWRKAV
RPQLTRRVEE AKAAQEQAQV RQETEEAVEV RLSKDEQLQQ RRANQRLGAE VMSQRIREMS
DNDPRVVALV IRQWMSNDHE
//
