FLIF_ECOLI
ID FLIF_ECOLI Reviewed; 552 AA.
AC P25798; P76324; P76914;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 25-MAY-2022, entry version 150.
DE RecName: Full=Flagellar M-ring protein;
GN Name=fliF; Synonyms=fla AII.1, fla BI; OrderedLocusNames=b1938, JW1922;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA al Mamun A.A.M., Tominaga A., Enomoto M.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-5.
RC STRAIN=JA11;
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 532-552.
RX PubMed=8224881; DOI=10.1016/0378-1119(93)90232-r;
RA Roman S.J., Frantz B.B., Matsumura P.;
RT "Gene sequence, overproduction, purification and determination of the wild-
RT type level of the Escherichia coli flagellar switch protein FliG.";
RL Gene 133:103-108(1993).
RN [7]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
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 P25798; P0ABZ1: fliG; NbExp=4; IntAct=EBI-1126492, EBI-1126524;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15919996}. Bacterial flagellum basal body
CC {ECO:0000269|PubMed:15919996}.
CC -!- SIMILARITY: Belongs to the FliF family. {ECO:0000305}.
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DR EMBL; D89826; BAA14029.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75005.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15763.1; -; Genomic_DNA.
DR EMBL; M84992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L13243; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; G64957; G64957.
DR RefSeq; NP_416448.1; NC_000913.3.
DR RefSeq; WP_000994427.1; NZ_LN832404.1.
DR AlphaFoldDB; P25798; -.
DR SMR; P25798; -.
DR BioGRID; 4260383; 20.
DR BioGRID; 850802; 1.
DR DIP; DIP-401N; -.
DR IntAct; P25798; 4.
DR STRING; 511145.b1938; -.
DR PaxDb; P25798; -.
DR PRIDE; P25798; -.
DR EnsemblBacteria; AAC75005; AAC75005; b1938.
DR EnsemblBacteria; BAA15763; BAA15763; BAA15763.
DR GeneID; 946448; -.
DR KEGG; ecj:JW1922; -.
DR KEGG; eco:b1938; -.
DR PATRIC; fig|1411691.4.peg.313; -.
DR EchoBASE; EB1323; -.
DR eggNOG; COG1766; Bacteria.
DR HOGENOM; CLU_028108_1_0_6; -.
DR InParanoid; P25798; -.
DR OMA; NYEVNRI; -.
DR PhylomeDB; P25798; -.
DR BioCyc; EcoCyc:FLIF-FLAGELLAR-MS-RING; -.
DR PRO; PR:P25798; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009431; C:bacterial-type flagellum basal body, MS ring; TAS:EcoCyc.
DR GO; GO:0005829; C:cytosol; ISM:EcoCyc.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; ISM:EcoCyc.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; TAS:EcoCyc.
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 PANTHER; PTHR30046; PTHR30046; 1.
DR PANTHER; PTHR30046:SF0; PTHR30046:SF0; 1.
DR Pfam; PF01514; YscJ_FliF; 1.
DR Pfam; PF08345; YscJ_FliF_C; 1.
DR PIRSF; PIRSF004862; FliF; 1.
DR PRINTS; PR01009; FLGMRINGFLIF.
DR TIGRFAMs; TIGR00206; fliF; 1.
PE 1: Evidence at protein level;
KW Bacterial flagellum; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..552
FT /note="Flagellar M-ring protein"
FT /id="PRO_0000180882"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 447..467
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 272..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 260
FT /note="H -> R (in Ref. 1; BAA14029)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="Q -> H (in Ref. 1; BAA14029)"
FT /evidence="ECO:0000305"
FT CONFLICT 541
FT /note="L -> V (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 552 AA; 60589 MW; B2038FDBEA914DA5 CRC64;
MNATAAQTKS LEWLNRLRAN PKIPLIVAGS AAVAVMVALI LWAKAPDYRT LFSNLSDQDG
GAIVSQLTQM NIPYRFSEAS GAIEVPADKV HELRLRLAQQ GLPKGGAVGF ELLDQEKFGI
SQFSEQVNYQ RALEGELSRT IETIGPVKGA RVHLAMPKPS LFVREQKSPS ASVTVNLLPG
RALDEGQISA IVHLVSSAVA GLPPGNVTLV DQGGHLLTQS NTSGRDLNDA QLKYASDVEG
RIQRRIEAIL SPIVGNGNIH AQVTAQLDFA SKEQTEEQYR PNGDESHAAL RSRQLNESEQ
SGSGYPGGVP GALSNQPAPA NNAPISTPPA NQNNRQQQAS TTSNSGPRST QRNETSNYEV
DRTIRHTKMN VGDVQRLSVA VVVNYKTLPD GKPLPLSNEQ MKQIEDLTRE AMGFSEKRGD
SLNVVNSPFN SSDESGGELP FWQQQAFIDQ LLAAGRWLLV LLVAWLLWRK AVRPQLTRRA
EAMKAVQQQA QAREEVEDAV EVRLSKDEQL QQRRANQRLG AEVMSQRIRE MSDNDPRVVA
LVIRQWINND HE
