ID   H2F4H3_9ASPA            Unreviewed;       507 AA.
AC   H2F4H3;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   09-DEC-2015, entry version 23.
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:AEX93556.1};
OS   Xanthorrhoea preissii.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:AEX93556.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Asparagales;
OC   Xanthorrhoeaceae; Xanthorrhoeoideae; Xanthorrhoea.
OX   NCBI_TaxID=470286 {ECO:0000313|EMBL:AEX93556.1};
RN   [1] {ECO:0000313|EMBL:AEX93556.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=22291168; DOI=10.3732/ajb.1100491;
RA   Steele P.R., Hertweck K.L., Mayfield D., McKain M.R., Leebens-Mack J.,
RA   Pires J.C.;
RT   "Quality and quantity of data recovered from massively parallel
RT   sequencing: Examples in Asparagales and Poaceae.";
RL   Am. J. Bot. 99:330-348(2012).
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; JQ273591; AEX93556.1; -; Genomic_DNA.
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:AEX93556.1};
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:AEX93556.1};
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       29     93       ATP-synt_ab_N. {ECO:0000259|Pfam:
FT                                PF02874}.
FT   DOMAIN      150    365       ATP-synt_ab. {ECO:0000259|Pfam:PF00006}.
FT   DOMAIN      377    468       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;  55353 MW;  704ABCED02258312 CRC64;
     MATLRADEIS NIIRERIEQY NREVKIVNTG TVLQVGDGIA RIHGLDEVMA GELVEFEEGT
     IGIALNLESN NVGVVLMGDG LMIQEGSSVK ATGRIAQIPV SEAYLSRVIN ALAKPIDGRG
     EISASESRLI ESPAPGIISR RSVYEPLQTG LIAIDSMIPI GRGQRELIIG DRQTGKTAVA
     TDTILNQKGK NVICVYVAIG QKASSVAQVV TTFQERGAME YTIVVAETAD SPATLQYLAP
     YTGAALAEYF MYRERHTLII YDDLSKQAQA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE
     RAAKSSSSLG EGSMTALPIV ETQSGDVSAY IPTNVISITD GQIFLSADLF NAGIRPAINV
     GISVSRVGSA AQIKAMKQVA GKLKLELAQF AELEAFAQFA SDLDKATQNQ LARGQRLREL
     LKQSQSDPLT VEEQIATIYT GANGYLDSLE IGQVKKFLIQ LRTYLKKNKP QFQEIISSTK
     TFTEQAETLL KEAIQEQSEL FLLEEQA
//