ID   ATPA_BART1              Reviewed;         511 AA.
AC   A9IYX0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=ATP synthase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346};
DE            EC=7.1.2.2 {ECO:0000255|HAMAP-Rule:MF_01346};
DE   AltName: Full=ATP synthase F1 sector subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346};
DE   AltName: Full=F-ATPase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346};
GN   Name=atpA {ECO:0000255|HAMAP-Rule:MF_01346}; OrderedLocusNames=BT_2466;
OS   Bartonella tribocorum (strain CIP 105476 / IBS 506).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=382640;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 105476 / IBS 506;
RX   PubMed=18037886; DOI=10.1038/ng.2007.38;
RA   Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G.,
RA   Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.;
RT   "Genomic analysis of Bartonella identifies type IV secretion systems as
RT   host adaptability factors.";
RL   Nat. Genet. 39:1469-1476(2007).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. The alpha chain is a regulatory subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_01346}.
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|HAMAP-Rule:MF_01346};
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC       - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC       alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC       subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an
CC       alternating ring which encloses part of the gamma chain. CF(1) is
CC       attached to CF(0) by a central stalk formed by the gamma and epsilon
CC       chains, while a peripheral stalk is formed by the delta and b chains.
CC       {ECO:0000255|HAMAP-Rule:MF_01346}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01346}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01346}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000255|HAMAP-Rule:MF_01346}.
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DR   EMBL; AM260525; CAK02444.1; -; Genomic_DNA.
DR   RefSeq; WP_012232485.1; NC_010161.1.
DR   AlphaFoldDB; A9IYX0; -.
DR   SMR; A9IYX0; -.
DR   STRING; 382640.BT_2466; -.
DR   PRIDE; A9IYX0; -.
DR   EnsemblBacteria; CAK02444; CAK02444; BT_2466.
DR   KEGG; btr:BT_2466; -.
DR   eggNOG; COG0056; Bacteria.
DR   HOGENOM; CLU_010091_2_1_5; -.
DR   OMA; LQAPGVM; -.
DR   OrthoDB; 837522at2; -.
DR   Proteomes; UP000001592; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR   CDD; cd18113; ATP-synt_F1_alpha_C; 1.
DR   CDD; cd01132; F1_ATPase_alpha; 1.
DR   Gene3D; 1.20.150.20; -; 1.
DR   Gene3D; 2.40.30.20; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_01346; ATP_synth_alpha_bact; 1.
DR   InterPro; IPR023366; ATP_synth_asu-like_sf.
DR   InterPro; IPR000793; ATP_synth_asu_C.
DR   InterPro; IPR038376; ATP_synth_asu_C_sf.
DR   InterPro; IPR033732; ATP_synth_F1_a.
DR   InterPro; IPR005294; ATP_synth_F1_asu.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR   InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF00306; ATP-synt_ab_C; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   PIRSF; PIRSF039088; F_ATPase_subunit_alpha; 1.
DR   SUPFAM; SSF50615; SSF50615; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00962; atpA; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; ATP-binding; Cell inner membrane; Cell membrane; CF(1);
KW   Hydrogen ion transport; Ion transport; Membrane; Nucleotide-binding;
KW   Translocase; Transport.
FT   CHAIN           1..511
FT                   /note="ATP synthase subunit alpha"
FT                   /id="PRO_1000086866"
FT   BINDING         169..176
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT   SITE            372
FT                   /note="Required for activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
SQ   SEQUENCE   511 AA;  55666 MW;  AACA61AEA074DD55 CRC64;
     MDIRPSEISK ILKEQIKNFD QKAEVSEIGW VLSVGDGIAR VYGLDNVQAG EMVAFPNGVR
     GMALNLEVDN VGVVIFGSDR DIREGDCVKR LGAIVDVPVG PALLGRVVDA LGNPIDGKGP
     LKETERRRVD VKAPGIIPRQ SVHEPMSTGL KAIDALIPIG RGQRELVIGD RQTGKTAILL
     DTFLNQKPFH EKGAGREQDK VYCIYVAIGQ KRSTVAQFVK VLEERGALEY SIIVAATASD
     PAPLQFIAPL AGCAMGEYFR DNGQHALIGY DDLSKQAVAY RQMSLLLRRP PGREAYPGDV
     FYLHSRLLER AAKLNAENGS GSLTALPVIE TQANDVSAYI PTNVISITDG QIFLETNLFY
     QGIRPAVNVG LSVSRVGSAA QIKAMKQVAG SIKGELAQYR EMAAFAQFGS DLDASTQRLL
     NRGARLTELL KQPQFSPLKT EEQVVVIFAG VNGYLDSLAV SDVARFEQGL LVLLRSDYQD
     LLQAIAEQKQ ITDELKDKLI TVLNTYAKNF S