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 27-MAR-2024, entry version 163. 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; Pseudomonadota; 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; 99287-STM1972; -. DR GeneID; 1253493; -. DR KEGG; stm:STM1972; -. DR PATRIC; fig|99287.12.peg.2089; -. DR HOGENOM; CLU_022398_5_1_6; -. DR OMA; LTCGRGQ; -. DR PhylomeDB; P26465; -. DR BioCyc; SENT99287:STM1972-MONOMER; -. 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 CDD; cd18114; ATP-synt_flagellum-secretory_path_III_C; 1. DR CDD; cd18117; ATP-synt_flagellum-secretory_path_III_N; 1. DR CDD; cd01136; ATPase_flagellum-secretory_path_III; 1. DR Gene3D; 3.40.50.12240; -; 1. 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 NCBIfam; TIGR03496; FliI_clade1; 1. DR NCBIfam; TIGR01026; fliI_yscN; 1. DR PANTHER; PTHR15184; ATP SYNTHASE; 1. DR PANTHER; PTHR15184:SF81; FLAGELLUM-SPECIFIC ATP SYNTHASE; 1. DR Pfam; PF00006; ATP-synt_ab; 1. DR Pfam; PF18269; T3SS_ATPase_C; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 //