ID   ATPA_ENTHA              Reviewed;         518 AA.
AC   P26679; I6SDC5;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 138.
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=EHR_08490;
OS   Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 /
OS   NBRC 3181 / NCIMB 6459 / NCDO 1258 / NCTC 12367 / WDCM 00089 / R).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=768486;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459
RC   / NCDO 1258 / NCTC 12367 / WDCM 00089 / R;
RX   PubMed=1328152; DOI=10.1128/jb.174.19.6117-6124.1992;
RA   Shibata C., Ehara T., Tomura K., Igarashi K., Kobayashi H.;
RT   "Gene structure of Enterococcus hirae (Streptococcus faecalis) F1F0-ATPase,
RT   which functions as a regulator of cytoplasmic pH.";
RL   J. Bacteriol. 174:6117-6124(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459
RC   / NCDO 1258 / NCTC 12367 / WDCM 00089 / R;
RX   PubMed=22933757; DOI=10.1128/jb.01075-12;
RA   Gaechter T., Wunderlin C., Schmidheini T., Solioz M.;
RT   "Genome sequence of Enterococcus hirae (Streptococcus faecalis) ATCC 9790,
RT   a model organism for the study of ion transport, bioenergetics, and copper
RT   homeostasis.";
RL   J. Bacteriol. 194:5126-5127(2012).
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   -!- 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 membrane {ECO:0000255|HAMAP-Rule:MF_01346};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-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; M64265; AAA26864.1; -; Genomic_DNA.
DR   EMBL; M90060; AAA26857.1; -; Genomic_DNA.
DR   EMBL; CP003504; AFM70623.1; -; Genomic_DNA.
DR   RefSeq; WP_010737987.1; NZ_KB946231.1.
DR   AlphaFoldDB; P26679; -.
DR   SMR; P26679; -.
DR   STRING; 768486.EHR_08490; -.
DR   PRIDE; P26679; -.
DR   EnsemblBacteria; AFM70623; AFM70623; EHR_08490.
DR   KEGG; ehr:EHR_08490; -.
DR   eggNOG; COG0056; Bacteria.
DR   HOGENOM; CLU_010091_2_1_9; -.
DR   OrthoDB; 837522at2; -.
DR   Proteomes; UP000002895; 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 membrane; CF(1); Hydrogen ion transport;
KW   Ion transport; Membrane; Nucleotide-binding; Translocase; Transport.
FT   CHAIN           1..518
FT                   /note="ATP synthase subunit alpha"
FT                   /id="PRO_0000144328"
FT   BINDING         169..176
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT   SITE            362
FT                   /note="Required for activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
SQ   SEQUENCE   518 AA;  56549 MW;  F2405FC32EBB9F55 CRC64;
     MAIKAEEISA LIKEQIENYQ NVLSVEEIGT VTYVGDGIAR AHGLENAMSG ELLEFSNGSY
     GMAQNLESND VGIIILGDFE SIREGDKVKR TGKIMEVPVG DALIGRVVNP LGQPIDGLGE
     IVTDKVRPVE AMAPGVMQRK SVNEPMQTGL KAIDALVPIG RGQRELVIGD RKTGKTSIAI
     DTILNQKGQD MICIYVAIGQ KDSTVRTQVE TLKKYGAMDY TIVVNAGASQ PAPLLYIAPY
     AGTAMGEEFM YNGKHVLIIF DDLSKQAVAY RELSLLLRRP PGREAYPGDV FYLHSRLLER
     AAKLSDDLGG GSMTALPFVE TQAGDISAYI PTNVISITDG QIFLESDLFY AGTRPAVDAG
     LSVSRVGGSA QIKAMKKVAG TLRLDLASYR ELEAFTQFGS DLDAATQAKL NRGRRTVEIL
     KQKLHAPLAV EKQVVILYAL THGFLDSIPV DSILDFEHEL FEYLDTNHAD IFETIRTTKD
     LPEEERLNQA IQEYKDIFLA TKGNTSSTED KLKSIQNA