ID   FLII_BACSU              Reviewed;         438 AA.
AC   P23445;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 2.
DT   03-AUG-2022, entry version 165.
DE   RecName: Full=Flagellum-specific ATP synthase;
DE            EC=7.1.2.2;
GN   Name=fliI; OrderedLocusNames=BSU16240;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=1828465; DOI=10.1128/jb.173.11.3573-3579.1991;
RA   Albertini A.M., Caramori T., Crabb W.D., Scoffone F., Galizzi A.;
RT   "The flaA locus of Bacillus subtilis is part of a large operon coding for
RT   flagellar structures, motility functions, and an ATPase-like polypeptide.";
RL   J. Bacteriol. 173:3573-3579(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   SEQUENCE REVISION TO 113-120 AND N-TERMINUS.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
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; X56049; CAA39523.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13497.2; -; Genomic_DNA.
DR   PIR; D42365; PWBSAS.
DR   RefSeq; NP_389506.2; NC_000964.3.
DR   RefSeq; WP_003244825.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; P23445; -.
DR   SMR; P23445; -.
DR   STRING; 224308.BSU16240; -.
DR   PRIDE; P23445; -.
DR   EnsemblBacteria; CAB13497; CAB13497; BSU_16240.
DR   GeneID; 940136; -.
DR   KEGG; bsu:BSU16240; -.
DR   PATRIC; fig|224308.179.peg.1764; -.
DR   eggNOG; COG1157; Bacteria.
DR   InParanoid; P23445; -.
DR   OMA; MLMMDSV; -.
DR   PhylomeDB; P23445; -.
DR   BioCyc; BSUB:BSU16240-MON; -.
DR   Proteomes; UP000001570; 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:0044780; P:bacterial-type flagellum assembly; IMP:CACAO.
DR   GO; GO:0071978; P:bacterial-type flagellum-dependent swarming motility; IMP:CACAO.
DR   GO; GO:0030254; P:protein secretion by the type III secretion system; IEA:InterPro.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR000225; Armadillo.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR005714; ATPase_T3SS_FliI/YscN.
DR   InterPro; IPR022425; FliI_clade2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR040627; T3SS_ATPase_C.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   Pfam; PF18269; T3SS_ATPase_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR03497; FliI_clade2; 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; Reference proteome;
KW   Translocase; Transport.
FT   CHAIN           1..438
FT                   /note="Flagellum-specific ATP synthase"
FT                   /id="PRO_0000144688"
FT   REGION          119..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         165..172
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        1..11
FT                   /note="MKTQSLIDCIE -> MQLNEDTESDRLYR (in Ref. 1; CAA39523)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        113..120
FT                   /note="GKLLPKGL -> ESFCRKV (in Ref. 1; CAA39523)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   438 AA;  47338 MW;  A23628EAA7BB6687 CRC64;
     MKTQSLIDCI EMTDSYKRYG KVKRVIGLMI ESKGPASSIG DLCLIYAKGQ SGKVIKAEVV
     GFQEENILLM PYLEAASIAP GSIVEATGES LRVKVGTGLI GQVIDAFGEP LDGKLLPKGL
     SPVSTEQSPP NPMKRPPIRE KMGVGVRSID SLLTVGKGQR IGIFAGSGVG KSTLMGMIAK
     QTEADLNVIA LVGERGREVR EFIEKDLGKE GLKRSIVVVA TSDQPALMRL KAAYTATAIA
     EYFRDKGQNV MFMMDSVTRV AMAQREIGLA AGEPPTTKGY TPSVFAILPR LLERTGANEH
     GTITAFYTVL VDGDDMNEPI ADTVRGILDG HIVLDRALAN KGQFPAVNVL KSISRVMSNI
     STKQHLDAAN KFRELLSTYQ NSEDLINIGA YKRGSSREID EAIQFYPQLI QFLKQGTDEP
     ALLEESIAAL TSLTGNEE