ID FLII_HELPY Reviewed; 434 AA. AC O07025; P94822; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 27-MAR-2024, entry version 159. DE RecName: Full=Flagellum-specific ATP synthase; DE EC=7.1.2.2; GN Name=fliI; OrderedLocusNames=HP_1420; OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=85962; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=N6; RX PubMed=9231413; DOI=10.1111/j.1574-6968.1997.tb10429.x; RA Jenks P.J., Foynes S., Ward S., Wren B.W.; RT "A flagellar-specific ATPase (FliI) is necessary for flagellar export in RT Helicobacter pylori."; RL FEMS Microbiol. Lett. 152:205-211(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700392 / 26695; RX PubMed=9252185; DOI=10.1038/41483; RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A., RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.; RT "The complete genome sequence of the gastric pathogen Helicobacter RT pylori."; RL Nature 388:539-547(1997). 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. 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 O07025; O25120: HP_0353; NbExp=4; IntAct=EBI-957989, EBI-958087; 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; Y08620; CAA69911.1; -; Genomic_DNA. DR EMBL; AE000511; AAD08462.1; -; Genomic_DNA. DR PIR; D64697; D64697. DR RefSeq; NP_208211.1; NC_000915.1. DR RefSeq; WP_001128709.1; NC_018939.1. DR AlphaFoldDB; O07025; -. DR SMR; O07025; -. DR DIP; DIP-3391N; -. DR IntAct; O07025; 1. DR MINT; O07025; -. DR STRING; 85962.HP_1420; -. DR PaxDb; 85962-C694_07345; -. DR EnsemblBacteria; AAD08462; AAD08462; HP_1420. DR KEGG; hpy:HP_1420; -. DR PATRIC; fig|85962.47.peg.1524; -. DR eggNOG; COG1157; Bacteria. DR InParanoid; O07025; -. DR OrthoDB; 9801639at2; -. DR PhylomeDB; O07025; -. DR Proteomes; UP000000429; 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: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:0044781; P:bacterial-type flagellum organization; IEA:UniProtKB-KW. 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; 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; IPR027417; P-loop_NTPase. DR InterPro; IPR040627; T3SS_ATPase_C. DR NCBIfam; TIGR01026; fliI_yscN; 1. DR PANTHER; PTHR15184; ATP SYNTHASE; 1. DR PANTHER; PTHR15184:SF9; SPI-1 TYPE 3 SECRETION SYSTEM ATPASE; 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 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..434 FT /note="Flagellum-specific ATP synthase" FT /id="PRO_0000144696" FT BINDING 164..171 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" FT CONFLICT 15 FT /note="D -> E (in Ref. 1; CAA69911)" FT /evidence="ECO:0000305" FT CONFLICT 115 FT /note="A -> V (in Ref. 1; CAA69911)" FT /evidence="ECO:0000305" FT CONFLICT 140 FT /note="I -> V (in Ref. 1; CAA69911)" FT /evidence="ECO:0000305" FT CONFLICT 323 FT /note="T -> A (in Ref. 1; CAA69911)" FT /evidence="ECO:0000305" FT CONFLICT 367 FT /note="C -> Y (in Ref. 1; CAA69911)" FT /evidence="ECO:0000305" FT CONFLICT 424 FT /note="T -> Q (in Ref. 1; CAA69911)" FT /evidence="ECO:0000305" SQ SEQUENCE 434 AA; 47636 MW; 6F04D67C988B4E22 CRC64; MPLKSLKNRL NQHFDLSPRY GSVKKIMPNI VYADGFNPSV GDVVKIEKSD GSECVGMVVV AEKEQFGFTP FNFIEGARAG DKVLFLKEGL NFPVGRNLLG RVLNPLGQVI DNKGALDYER LAPVITTPIA PLKRGLIDEI FSVGVKSIDG LLTCGKGQKL GIFAGSGVGK STLMGMITRG CLAPIKVIAL IGERGREIPE FIEKNLKGDL SSCVLVVATS DDSPLMRKYG AFCAMSVAEY FKNQGLDVLF IMDSVTRFAM AQREIGLALG EPPTSKGYPP SALSLLPQLM ERAGKEENKG SITAFFSVLV EGDDLSDPIA DQTRSILDGH IVLSRELTDY GIYPPINILN SASRVAKDII SESQNLCARK FRRLYALLKE NEMLIRIGSY QMGNDKELDE AIKKKALMEQ FLAQDENALQ PFETSFQQLE EILR //