ID   H2F4H3_9ASPA            Unreviewed;       507 AA.
AC   H2F4H3;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   29-SEP-2021, entry version 44.
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:AEX93556.1};
OS   Xanthorrhoea preissii.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:AEX93556.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Asphodelaceae;
OC   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 sequencing:
RT   Examples in Asparagales and Poaceae.";
RL   Am. J. Bot. 99:330-348(2012).
RN   [2] {ECO:0000313|EMBL:ATB18628.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Park H., Kim C., Kim J.-H.;
RT   "The comparative plastid genome analysis and its phylogenetic implication
RT   on Asparagaceae s.l.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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   -!- 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, b and c. {ECO:0000256|ARBA:ARBA00011648}.
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; JQ273591; AEX93556.1; -; Genomic_DNA.
DR   EMBL; KX822774; ATB18628.1; -; 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-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:AEX93556.1};
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:AEX93556.1};
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          29..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;  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
//