FLII_HELPY
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 03-AUG-2022, entry version 150.
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; Proteobacteria; 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}.
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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.C694_07345; -.
DR PaxDb; O07025; -.
DR EnsemblBacteria; AAD08462; AAD08462; HP_1420.
DR KEGG; hpy:HP_1420; -.
DR PATRIC; fig|85962.47.peg.1524; -.
DR eggNOG; COG1157; Bacteria.
DR OMA; MDSATRF; -.
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 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 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; 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..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
