FLII_SALTY
ID FLII_SALTY Reviewed; 456 AA.
AC P26465;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Flagellum-specific ATP synthase;
DE EC=7.1.2.2;
GN Name=fliI; Synonyms=fla AIII, flaC; OrderedLocusNames=STM1972;
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=1646201; DOI=10.1128/jb.173.11.3564-3572.1991;
RA Vogler A.P., Homma M., Irikura V.M., Macnab R.M.;
RT "Salmonella typhimurium mutants defective in flagellar filament regrowth
RT and sequence similarity of FliI to F0F1, vacuolar, and archaebacterial
RT ATPase subunits.";
RL J. Bacteriol. 173:3564-3572(1991).
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 CHARACTERIZATION, AND MUTAGENESIS.
RX PubMed=8491729; DOI=10.1128/jb.175.10.3131-3138.1993;
RA Dreyfus G., Williams A.W., Kawagishi I., Macnab R.M.;
RT "Genetic and biochemical analysis of Salmonella typhimurium FliI, a
RT flagellar protein related to the catalytic subunit of the F0F1 ATPase and
RT to virulence proteins of mammalian and plant pathogens.";
RL J. Bacteriol. 175:3131-3138(1993).
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 P26465; P26465: fliI; NbExp=2; IntAct=EBI-6515439, EBI-6515439;
CC P26465; P0A1K1: fliJ; NbExp=3; IntAct=EBI-6515439, EBI-6410293;
CC P26465; P0A1N2: fliT; NbExp=2; IntAct=EBI-6515439, EBI-15610664;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {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; M62408; AAA27101.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20884.1; -; Genomic_DNA.
DR PIR; C42364; C42364.
DR RefSeq; NP_460925.1; NC_003197.2.
DR RefSeq; WP_000213257.1; NC_003197.2.
DR PDB; 2DPY; X-ray; 2.40 A; A/B=19-456.
DR PDB; 5B0O; X-ray; 3.00 A; A/B/C/D=1-456.
DR PDB; 5KP0; NMR; -; A=1-25.
DR PDBsum; 2DPY; -.
DR PDBsum; 5B0O; -.
DR PDBsum; 5KP0; -.
DR AlphaFoldDB; P26465; -.
DR SMR; P26465; -.
DR DIP; DIP-59076N; -.
DR IntAct; P26465; 3.
DR STRING; 99287.STM1972; -.
DR TCDB; 3.A.6.2.1; the type iii (virulence-related) secretory pathway (iiisp) family.
DR PaxDb; P26465; -.
DR EnsemblBacteria; AAL20884; AAL20884; STM1972.
DR GeneID; 1253493; -.
DR KEGG; stm:STM1972; -.
DR PATRIC; fig|99287.12.peg.2089; -.
DR HOGENOM; CLU_022398_5_1_6; -.
DR OMA; MLMMDSV; -.
DR PhylomeDB; P26465; -.
DR BioCyc; SENT99287:STM1972-MON; -.
DR EvolutionaryTrace; P26465; -.
DR Proteomes; UP000001014; Chromosome.
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; IEA:InterPro.
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; IEA:InterPro.
DR GO; GO:0030254; P:protein secretion by the type III secretion system; IEA:InterPro.
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 3D-structure; 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..456
FT /note="Flagellum-specific ATP synthase"
FT /id="PRO_0000144695"
FT BINDING 182..189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MUTAGEN 188
FT /note="K->E: Loss of flagellum."
FT /evidence="ECO:0000269|PubMed:8491729"
FT MUTAGEN 188
FT /note="K->I: Loss of flagellum."
FT /evidence="ECO:0000269|PubMed:8491729"
FT MUTAGEN 272
FT /note="D->N: Loss of flagellum."
FT /evidence="ECO:0000269|PubMed:8491729"
FT MUTAGEN 363
FT /note="Y->S: Loss of flagellum."
FT /evidence="ECO:0000269|PubMed:8491729"
FT HELIX 3..19
FT /evidence="ECO:0007829|PDB:5B0O"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:2DPY"
FT STRAND 35..43
FT /evidence="ECO:0007829|PDB:2DPY"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:2DPY"
FT STRAND 63..71
FT /evidence="ECO:0007829|PDB:2DPY"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:2DPY"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:2DPY"
FT TURN 99..102
FT /evidence="ECO:0007829|PDB:5B0O"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:2DPY"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:2DPY"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:2DPY"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:2DPY"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:2DPY"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:5B0O"
FT HELIX 164..169
FT /evidence="ECO:0007829|PDB:2DPY"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:2DPY"
FT HELIX 188..198
FT /evidence="ECO:0007829|PDB:2DPY"
FT STRAND 202..210
FT /evidence="ECO:0007829|PDB:2DPY"
FT HELIX 213..221
FT /evidence="ECO:0007829|PDB:2DPY"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:2DPY"
FT HELIX 225..230
FT /evidence="ECO:0007829|PDB:2DPY"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:2DPY"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:5B0O"
FT HELIX 243..261
FT /evidence="ECO:0007829|PDB:2DPY"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:2DPY"
FT STRAND 266..272
FT /evidence="ECO:0007829|PDB:2DPY"
FT HELIX 274..287
FT /evidence="ECO:0007829|PDB:2DPY"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:2DPY"
FT HELIX 301..309
FT /evidence="ECO:0007829|PDB:2DPY"
FT STRAND 321..329
FT /evidence="ECO:0007829|PDB:2DPY"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:2DPY"
FT HELIX 338..346
FT /evidence="ECO:0007829|PDB:2DPY"
FT STRAND 347..353
FT /evidence="ECO:0007829|PDB:2DPY"
FT HELIX 355..359
FT /evidence="ECO:0007829|PDB:2DPY"
FT STRAND 366..373
FT /evidence="ECO:0007829|PDB:2DPY"
FT HELIX 376..379
FT /evidence="ECO:0007829|PDB:2DPY"
FT HELIX 382..400
FT /evidence="ECO:0007829|PDB:2DPY"
FT HELIX 401..403
FT /evidence="ECO:0007829|PDB:2DPY"
FT STRAND 405..408
FT /evidence="ECO:0007829|PDB:2DPY"
FT HELIX 416..422
FT /evidence="ECO:0007829|PDB:2DPY"
FT HELIX 425..432
FT /evidence="ECO:0007829|PDB:2DPY"
FT HELIX 442..452
FT /evidence="ECO:0007829|PDB:2DPY"
SQ SEQUENCE 456 AA; 49265 MW; 830867B657592BF1 CRC64;
MTTRLTRWLT ALDNFEAKMA LLPAVRRYGR LTRATGLVLE ATGLQLPLGA TCIIERQDGP
ETKEVESEVV GFNGQRLFLM PLEEVEGILP GARVYARNGH GDGLQSGKQL PLGPALLGRV
LDGGGKPLDG LPAPDTLETG ALITPPFNPL QRTPIEHVLD TGVRAINALL TVGRGQRMGL
FAGSGVGKSV LLGMMARYTR ADVIVVGLIG ERGREVKDFI ENILGPDGRA RSVVIAAPAD
VSPLLRMQGA AYATRIAEDF RDRGQHVLLI MDSLTRYAMA QREIALAIGE PPATKGYPPS
VFAKLPALVE RAGNGIHGGG SITAFYTVLT EGDDQQDPIA DSARAILDGH IVLSRRLAEA
GHYPAIDIEA SISRAMTALI TEQHYARVRL FKQLLSSFQR NRDLVSVGAY AKGSDPMLDK
AITLWPQLEA FLQQGIFERA DWEDSLQALD LIFPTV
