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Database: UniProt
Entry: Q7VYE8_BORPE
LinkDB: Q7VYE8_BORPE
Original site: Q7VYE8_BORPE 
ID   Q7VYE8_BORPE            Unreviewed;       477 AA.
AC   Q7VYE8;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 125.
DE   RecName: Full=Flagellum-specific ATP synthase {ECO:0000256|ARBA:ARBA00020580};
DE            EC=7.1.2.2 {ECO:0000256|ARBA:ARBA00012473};
GN   Name=fliI {ECO:0000313|EMBL:CAE41689.1};
GN   Synonyms=fla AIII {ECO:0000313|EMBL:CAE41689.1}, flaC
GN   {ECO:0000313|EMBL:CAE41689.1};
GN   OrderedLocusNames=BP1400 {ECO:0000313|EMBL:CAE41689.1};
OS   Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257313 {ECO:0000313|EMBL:CAE41689.1, ECO:0000313|Proteomes:UP000002676};
RN   [1] {ECO:0000313|Proteomes:UP000002676}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251
RC   {ECO:0000313|Proteomes:UP000002676};
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + cellular proteinSide 1 = ADP + phosphate +
CC         cellular proteinSide 2.; EC=7.4.2.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00034006};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000256|ARBA:ARBA00008936}.
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DR   EMBL; BX640415; CAE41689.1; -; Genomic_DNA.
DR   RefSeq; NP_880143.1; NC_002929.2.
DR   AlphaFoldDB; Q7VYE8; -.
DR   STRING; 257313.BP1400; -.
DR   PaxDb; 257313-BP1400; -.
DR   KEGG; bpe:BP1400; -.
DR   PATRIC; fig|257313.5.peg.1501; -.
DR   eggNOG; COG1157; Bacteria.
DR   HOGENOM; CLU_022398_5_1_4; -.
DR   Proteomes; UP000002676; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
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; 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; 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   3: Inferred from homology;
KW   ATP synthesis {ECO:0000256|ARBA:ARBA00023196};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Bacterial flagellum biogenesis {ECO:0000256|ARBA:ARBA00022795};
KW   Bacterial flagellum protein export {ECO:0000256|ARBA:ARBA00023225};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   CF(1) {ECO:0000256|ARBA:ARBA00023196};
KW   Hydrolase {ECO:0000313|EMBL:CAE41689.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002676};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          187..374
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   477 AA;  50896 MW;  26F3A857935F836A CRC64;
     MPVADRWQTQ LQIGSIRAAS TEPWLVSGRI TRAAGLVLHT TGLRLPVGAA CRIELARGHD
     HWADAEVVGF DGHTLYLMPQ SDISGLPPGA RVVPAEPAVQ RPVPLPRKAE LNGNAKPQVG
     RHLPVGNAML GRVVDGAGRP LDGLGPLAGA EQAPLTALPI NPLSRAPIDS VLDVGVRAIN
     GLLTVGRGQR MGLFAGSGVG KSVLLGMMAR YTRADIIVVG LIGERGREVK EFIEHNLGPE
     GLARSVVVAA PADVSPLLRL QGASYATRLA EHFRDQGLDV LLIMDSLTRF AMAQREIALA
     IGEPPATKGY PPSVFAKLPA LVERTGMGAP GPNGKAGSIT AFYTVLAEGD DQQDPIADSA
     RAILDGHVVL SRHLAEAGHY PAIDIEASIS RAMTSLITTE QFQQVRRFKQ ILSRYQRNRD
     LISVGAYVAG ADPQLDDAIA RYPRLEAYLQ QNIGDSVDYG TAIDQLQRSL ETREAYA
//
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