ID   ATPA_FUSBL              Reviewed;         512 AA.
AC   P05439;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   03-AUG-2022, entry version 131.
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};
OS   Fuscovulum blasticum (Rhodobacter blasticus) (Rhodopseudomonas blastica).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Fuscovulum.
OX   NCBI_TaxID=1075;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6209404; DOI=10.1016/0022-2836(84)90465-0;
RA   Tybulewicz V.L.J., Falk G., Walker J.E.;
RT   "Rhodopseudomonas blastica atp operon. Nucleotide sequence and
RT   transcription.";
RL   J. Mol. Biol. 179:185-214(1984).
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; Z00018; CAA77313.1; -; Genomic_DNA.
DR   PIR; S04672; S04672.
DR   AlphaFoldDB; P05439; -.
DR   SMR; P05439; -.
DR   PRIDE; P05439; -.
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..512
FT                   /note="ATP synthase subunit alpha"
FT                   /id="PRO_0000144344"
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   512 AA;  54939 MW;  21C26200C2CD6516 CRC64;
     MGIQAAEISA ILKEQIKNFG KDAEVAEVGR VLSVGDGIAR VYGLDNVQAG EMVEFPGGIR
     GMALNLEVDN VGIVIFGDDR DIKEGDTVKR TKSIVDVPAG NGLLGRVVDA LGNPIDGKGP
     IVASERRIAD VKAPGIIPRK GVHEPMATGL KAVDAMIPIG RGQRELIIGD RQTGKTAVAL
     DTILNQKVYN DAAGDDESKK LYCVYVAIGQ KRSTVAQLVK KLEETGAMAY TVVVAATASD
     PAPMQFLAPF SGTAIGEFFR DNGRHALMIY DDLSKQAVAY RQMSLLLRRP PGREAYPGDV
     FYLHSRLLER SAKMNGDFGA GSLTALPIIE TQAGDISAYI PTNVISITDG QIFLESELFY
     QGIRPAVNTG LSVSRVGSSA QTSAMKSVAG KVKLELAQYR EMAAFAQFGS DLDASTQALL
     NRGARLTELM KQPQYSPLTN AEIVCIIFAG TNGYLDKVAV RDVGRFEAGL LKHLRTKGKA
     LLDDMTKNDR KVAGDLEKAI RAELDAFAKD FA