ID   ATPA_SYNP1              Reviewed;         503 AA.
AC   Q05372;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   03-AUG-2022, entry version 125.
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   Synechococcus sp. (strain PCC 6716).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=32048;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-9.
RX   PubMed=8363578; DOI=10.1042/bj2940239;
RA   van Walraven H.S., Lutter R., Walker J.E.;
RT   "Organization and sequences of genes for the subunits of ATP synthase in
RT   the thermophilic cyanobacterium Synechococcus 6716.";
RL   Biochem. J. 294:239-251(1993).
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 four main
CC       subunits: a(1), b(1), b'(1) and c(9-12) (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid 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; X70431; CAA49875.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q05372; -.
DR   SMR; Q05372; -.
DR   GO; GO:0031676; C:plasma membrane-derived thylakoid 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   1: Evidence at protein level;
KW   ATP synthesis; ATP-binding; CF(1); Direct protein sequencing;
KW   Hydrogen ion transport; Ion transport; Membrane; Nucleotide-binding;
KW   Thylakoid; Translocase; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8363578"
FT   CHAIN           2..503
FT                   /note="ATP synthase subunit alpha"
FT                   /id="PRO_0000144360"
FT   BINDING         171..178
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT   SITE            364
FT                   /note="Required for activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
SQ   SEQUENCE   503 AA;  53904 MW;  3380D46BB8EE728B CRC64;
     MVSIRPDEIS SIIRQQIEQY EQSINVDNVG TVLQVGDGIA RVYGLDKVMA SELVEFEDGT
     VGIALNLEED NVGVVLMGAG LGIEEGSTVR ATGKIASVPV GEAVIGRVVD ALMRPIDGKG
     EIHATATRLL ESPAPGIVQR KSVCEPLQTG ITAIDAMIPI GRGQRELIIG DRQTGKTAVA
     IDTILNQKGQ DVICVYVAIG QKASSVAQVV NVLRERGALD YTIVVAANAS DPAALQYLAP
     YTGASIAEYF MYQGKHTLVI YDDLSKQAQA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE
     RAAKLNDALG GGSMTALPIV ETQAGDVSAY IPTNVISITD GQIFLSSDLF NAGLRPAINA
     GISVSRVGSA AQIKAMKQVA GKLKLELAQF DELQAFAQFA SDLDKATQNQ LARGQRLREI
     LKQPQYSPIP VEYQVATIYA GTNGYLDDIP VEAVAKFVAG LRDYLATSKP QYGEAVRSSQ
     KLDETAEALL KEAIAEYKAG FTA