FLII_ECOLI
ID FLII_ECOLI Reviewed; 457 AA.
AC P52612; P78073;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Flagellum-specific ATP synthase;
DE EC=7.1.2.2;
GN Name=fliI; Synonyms=fla AIII, flaC; OrderedLocusNames=b1941, JW1925;
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;
RA Macnab R.M.;
RL Submitted (NOV-1995) 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).
CC -!- FUNCTION: Probable catalytic subunit of a protein translocase for
CC flagellum-specific export, or a proton translocase involved in local
CC circuits at the flagellum. May be involved in a specialized protein
CC export pathway that proceeds without signal peptide cleavage.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10106};
CC -!- INTERACTION:
CC P52612; P52612: fliI; NbExp=4; IntAct=EBI-1118363, EBI-1118363;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
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DR EMBL; L49147; AAA82637.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75008.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15766.1; -; Genomic_DNA.
DR PIR; B64958; B64958.
DR RefSeq; NP_416451.1; NC_000913.3.
DR RefSeq; WP_000213294.1; NZ_SSZK01000066.1.
DR AlphaFoldDB; P52612; -.
DR SMR; P52612; -.
DR BioGRID; 4260388; 18.
DR BioGRID; 850811; 5.
DR ComplexPortal; CPX-5885; Flagellar export complex.
DR DIP; DIP-9655N; -.
DR IntAct; P52612; 23.
DR STRING; 511145.b1941; -.
DR PaxDb; P52612; -.
DR PRIDE; P52612; -.
DR EnsemblBacteria; AAC75008; AAC75008; b1941.
DR EnsemblBacteria; BAA15766; BAA15766; BAA15766.
DR GeneID; 66674169; -.
DR GeneID; 946457; -.
DR KEGG; ecj:JW1925; -.
DR KEGG; eco:b1941; -.
DR PATRIC; fig|1411691.4.peg.310; -.
DR EchoBASE; EB4163; -.
DR eggNOG; COG1157; Bacteria.
DR HOGENOM; CLU_022398_5_1_6; -.
DR InParanoid; P52612; -.
DR OMA; MLMMDSV; -.
DR PhylomeDB; P52612; -.
DR BioCyc; EcoCyc:G377-MON; -.
DR PRO; PR:P52612; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009288; C:bacterial-type flagellum; IC:ComplexPortal.
DR GO; GO:0120102; C:bacterial-type flagellum secretion apparatus; IC:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central.
DR GO; GO:0030257; C:type III protein secretion system complex; IC:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR GO; GO:0044780; P:bacterial-type flagellum assembly; IEA:InterPro.
DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IC:ComplexPortal.
DR GO; GO:0006935; P:chemotaxis; IC:ComplexPortal.
DR GO; GO:0030254; P:protein secretion by the type III secretion system; IC:ComplexPortal.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR005714; ATPase_T3SS_FliI/YscN.
DR InterPro; IPR020005; FliI_clade1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR040627; T3SS_ATPase_C.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF18269; T3SS_ATPase_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR03496; FliI_clade1; 1.
DR TIGRFAMs; TIGR01026; fliI_yscN; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW ATP synthesis; ATP-binding; Bacterial flagellum biogenesis;
KW Bacterial flagellum protein export; Cytoplasm; Hydrogen ion transport;
KW Ion transport; Nucleotide-binding; Protein transport; Reference proteome;
KW Translocase; Transport.
FT CHAIN 1..457
FT /note="Flagellum-specific ATP synthase"
FT /id="PRO_0000144694"
FT BINDING 182..189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 112..113
FT /note="LG -> SV (in Ref. 1; AAA82637)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="G -> A (in Ref. 1; AAA82637)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="A -> R (in Ref. 1; AAA82637)"
FT /evidence="ECO:0000305"
FT CONFLICT 248..250
FT /note="QGA -> RMP (in Ref. 1; AAA82637)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="A -> G (in Ref. 1; AAA82637)"
FT /evidence="ECO:0000305"
FT CONFLICT 399..400
FT /note="QR -> HG (in Ref. 1; AAA82637)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 457 AA; 49316 MW; 962D4268E8428C93 CRC64;
MTTRLTRWLT TLDNFEAKMA QLPAVRRYGR LTRATGLVLE ATGLQLPLGA TCVIERQNGS
ETHEVESEVV GFNGQRLFLM PLEEVEGVLP GARVYAKNIS AEGLQSGKQL PLGPALLGRV
LDGSGKPLDG LPSPDTTETG ALITPPFNPL QRTPIEHVLD TGVRPINALL TVGRGQRMGL
FAGSGVGKSV LLGMMARYTR ADVIVVGLIG ERGREVKDFI ENILGAEGRA RSVVIAAPAD
VSPLLRMQGA AYATRIAEDF RDRGQHVLLI MDSLTRYAMA QREIALAIGE PPATKGYPPS
VFAKLPALVE RAGNGISGGG SITAFYTVLT EGDDQQDPIA DSARAILDGH IVLSRRLAEA
GHYPAIDIEA SISRAMTALI SEQHYARVRT FKQLLSSFQR NRDLVSVGAY AKGSDPMLDK
AIALWPQLEG YLQQGIFERA DWEASLQGLE RIFPTVS