ID   A0A088CI87_9VIRI        Unreviewed;       507 AA.
AC   A0A088CI87;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   19-JAN-2022, entry version 30.
DE   RecName: Full=ATP synthase subunit alpha, chloroplastic {ECO:0000256|HAMAP-Rule:MF_01346, ECO:0000256|RuleBase:RU004286};
DE            EC=7.1.2.2 {ECO:0000256|HAMAP-Rule:MF_01346, ECO:0000256|RuleBase:RU004286};
DE   AltName: Full=ATP synthase F1 sector subunit alpha {ECO:0000256|HAMAP-Rule:MF_01346};
DE   AltName: Full=F-ATPase subunit alpha {ECO:0000256|HAMAP-Rule:MF_01346};
GN   Name=atpA {ECO:0000256|HAMAP-Rule:MF_01346,
GN   ECO:0000256|RuleBase:RU004286, ECO:0000313|EMBL:AID67503.1};
OS   Prasinoderma coloniale.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:AID67503.1}.
OC   Eukaryota; Viridiplantae; Prasinodermophyta; Prasinodermophyceae;
OC   Prasinodermales; Prasinodermaceae; Prasinoderma.
OX   NCBI_TaxID=156133 {ECO:0000313|EMBL:AID67503.1};
RN   [1] {ECO:0000313|EMBL:AID67503.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25281016; DOI=10.1186/1471-2164-15-857;
RA   Lemieux C., Otis C., Turmel M.;
RT   "Six newly sequenced chloroplast genomes from prasinophyte green algae
RT   provide insights into the relationships among prasinophyte lineages and the
RT   diversity of streamlined genome architecture in picoplanktonic species.";
RL   BMC Genomics 15:857-857(2014).
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:0000256|HAMAP-Rule:MF_01346, ECO:0000256|RuleBase:RU004286}.
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:0000256|HAMAP-Rule:MF_01346,
CC         ECO:0000256|RuleBase:RU004286};
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, b, b' and c. {ECO:0000256|HAMAP-Rule:MF_01346,
CC       ECO:0000256|RuleBase:RU004286}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000256|HAMAP-Rule:MF_01346, ECO:0000256|RuleBase:RU000341};
CC       Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01346,
CC       ECO:0000256|RuleBase:RU000341}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000256|ARBA:ARBA00008936, ECO:0000256|HAMAP-Rule:MF_01346,
CC       ECO:0000256|RuleBase:RU000339}.
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DR   EMBL; KJ746598; AID67503.1; -; Genomic_DNA.
DR   RefSeq; YP_009057535.1; NC_024817.1.
DR   GeneID; 20357960; -.
DR   GO; GO:0009535; C:chloroplast 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   3: Inferred from homology;
KW   ATP synthesis {ECO:0000256|ARBA:ARBA00023310, ECO:0000256|HAMAP-
KW   Rule:MF_01346};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01346};
KW   CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|HAMAP-Rule:MF_01346};
KW   Chloroplast {ECO:0000256|RuleBase:RU000341, ECO:0000313|EMBL:AID67503.1};
KW   Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781, ECO:0000256|HAMAP-
KW   Rule:MF_01346};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW   Rule:MF_01346};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01346};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01346};
KW   Plastid {ECO:0000256|RuleBase:RU004286, ECO:0000313|EMBL:AID67503.1};
KW   Thylakoid {ECO:0000256|HAMAP-Rule:MF_01346, ECO:0000256|RuleBase:RU000341};
KW   Translocase {ECO:0000256|HAMAP-Rule:MF_01346,
KW   ECO:0000256|RuleBase:RU004286};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01346}.
FT   DOMAIN          28..93
FT                   /note="ATP-synt_ab_N"
FT                   /evidence="ECO:0000259|Pfam:PF02874"
FT   DOMAIN          150..365
FT                   /note="ATP-synt_ab"
FT                   /evidence="ECO:0000259|Pfam:PF00006"
FT   DOMAIN          372..496
FT                   /note="ATP-synt_ab_C"
FT                   /evidence="ECO:0000259|Pfam:PF00306"
FT   NP_BIND         170..177
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01346"
FT   SITE            363
FT                   /note="Required for activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01346"
SQ   SEQUENCE   507 AA;  54127 MW;  3891B459E64BF32E CRC64;
     MVAIRPDEIS SIIRQQIEDY ASTVKVTNVG TVLQVGDGIA RVYGLNKVMA GELLEFEDGT
     VGIALNLEAD NVGVVLMGGG FEIQEGSSVK ATGKIAQVPV GEGFLGRVVN ALAIPVDGKG
     DITADETRLI ESPAPGIISR RSVYEPLQTG LVAIDAMIPI GRGQRELIIG DRQTGKTAVA
     IDTIINQKET GVICVYVAIG QKASSVAQIV TSLEEAGALE NTIIVAENAD SPAPLQYLAP
     YTGAALAEYF MYTNRHTLAI YDDLSKQAAA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE
     RAAKLSDALG EGSMTALPVV ETQAGDVSAY IPTNVISITD GQVFLSGDLF NSGIRPAINV
     GISVSRVGSA AQIKAMKQVA GTLKLELAQF AELEAFSQFA SDLDKATQNQ LARGQRLREL
     LKQAQGAPLS VPQQVVTIYT GINGYLDDVE VADVREFLSG LREYVGTSAS KIIDSINSSQ
     KFDDDAEAML LEAIATYKES FFASKKK
//