FLII_HELPJ
ID FLII_HELPJ Reviewed; 434 AA.
AC Q9ZJJ3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Flagellum-specific ATP synthase;
DE EC=7.1.2.2;
GN Name=fliI; OrderedLocusNames=jhp_1315;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
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DR EMBL; AE001439; AAD06888.1; -; Genomic_DNA.
DR PIR; D71823; D71823.
DR RefSeq; WP_001128788.1; NZ_CP011330.1.
DR AlphaFoldDB; Q9ZJJ3; -.
DR SMR; Q9ZJJ3; -.
DR STRING; 85963.jhp_1315; -.
DR EnsemblBacteria; AAD06888; AAD06888; jhp_1315.
DR KEGG; hpj:jhp_1315; -.
DR PATRIC; fig|85963.30.peg.1247; -.
DR eggNOG; COG1157; Bacteria.
DR OMA; MLMMDSV; -.
DR Proteomes; UP000000804; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 3: Inferred from homology;
KW ATP synthesis; ATP-binding; Bacterial flagellum biogenesis;
KW Bacterial flagellum protein export; Cytoplasm; Hydrogen ion transport;
KW Ion transport; Nucleotide-binding; Protein transport; Translocase;
KW Transport.
FT CHAIN 1..434
FT /note="Flagellum-specific ATP synthase"
FT /id="PRO_0000144697"
FT BINDING 164..171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 434 AA; 47703 MW; D7614669355EE816 CRC64;
MPLKSLKNRL NQHFELSPRY GSVKKIMPNI VYADGFNPSV GDVVKIEKSD GTECVGMVVV
AEKEQFGFTP FNFIEGARAG DKVLFLKEGL NFPVGRNLLG RVLNPLGQVI DNKGVLDYER
LAPVITTPIA PLKRGLIDEV FSVGVKSIDG LLTCGKGQKL GIFAGSGVGK STLMGMITRG
CLAPIKVIAL IGERGREIPE FIEKNLKGDL SSCVLVVATS DDSPLMRKYG AFCAMSVAEY
FKNQGLDVLF IMDSVTRFAM AQREIGLALG EPPTSKGYPP SALSLLPQLM ERAGKEENKG
SITAFFSVLV EGDDLSDPIA DQARSILDGH IVLSRELTDY GIYPPINILN SASRVAKDII
SESQNLCARK FRRLYALLKE NEMLIRIGSY QMGNDKELDE AIKKKALMEQ FLVQDENALQ
PFEQSFQQLE EILR