ID   A0A088CI87_9CHLO        Unreviewed;       507 AA.
AC   A0A088CI87;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   09-DEC-2015, entry version 7.
DE   RecName: Full=ATP synthase subunit alpha, chloroplastic {ECO:0000256|HAMAP-Rule:MF_01346, ECO:0000256|RuleBase:RU004286};
DE            EC=3.6.3.14 {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:0000313|EMBL:AID67503.1};
OS   Prasinoderma coloniale.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:AID67503.1}.
OC   Eukaryota; Viridiplantae; Chlorophyta; prasinophytes; Prasinococcales;
OC   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
RT   and the diversity of streamlined genome architecture in picoplanktonic
RT   species.";
RL   BMC Genomics 15:857-857(2014).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton
CC       gradient across the membrane. The alpha chain is a regulatory
CC       subunit. {ECO:0000256|HAMAP-Rule:MF_01346}.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate +
CC       H(+)(Out). {ECO:0000256|HAMAP-Rule:MF_01346,
CC       ECO:0000256|RuleBase:RU004286}.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
CC       core - and CF(0) - the membrane proton channel. CF(1) has five
CC       subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0)
CC       has four main subunits: a, b, b' and c. {ECO:0000256|HAMAP-
CC       Rule:MF_01346, 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|HAMAP-Rule:MF_01346, 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-HAMAP.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
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; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR023366; ATPase_asu-like.
DR   InterPro; IPR005294; ATPase_F1-cplx_asu.
DR   InterPro; IPR000793; ATPase_F1/V1/A1-cplx_a/bsu_C.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR004100; ATPase_F1_a/bsu_N.
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; SSF47917; SSF47917; 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|HAMAP-Rule:MF_01346};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01346};
KW   CF(1) {ECO:0000256|HAMAP-Rule:MF_01346};
KW   Chloroplast {ECO:0000256|RuleBase:RU000341,
KW   ECO:0000313|EMBL:AID67503.1};
KW   Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01346,
KW   ECO:0000256|RuleBase:RU000339};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01346};
KW   Ion transport {ECO:0000256|HAMAP-Rule:MF_01346,
KW   ECO:0000256|RuleBase:RU000339};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01346};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01346};
KW   Plastid {ECO:0000313|EMBL:AID67503.1};
KW   Thylakoid {ECO:0000256|HAMAP-Rule:MF_01346,
KW   ECO:0000256|RuleBase:RU000341};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01346,
KW   ECO:0000256|RuleBase:RU000339}.
FT   DOMAIN       28     93       ATP-synt_ab_N. {ECO:0000259|Pfam:
FT                                PF02874}.
FT   DOMAIN      150    365       ATP-synt_ab. {ECO:0000259|Pfam:PF00006}.
FT   DOMAIN      377    464       ATP-synt_ab_C. {ECO:0000259|Pfam:
FT                                PF00306}.
FT   NP_BIND     170    177       ATP. {ECO:0000256|HAMAP-Rule:MF_01346}.
FT   SITE        363    363       Required for activity.
FT                                {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
//