ATPA_ZYGCR
ID ATPA_ZYGCR Reviewed; 505 AA.
AC Q32RL1;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=ATP synthase subunit alpha, chloroplastic {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 Zygnema circumcarinatum (Green alga).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Zygnemophyceae; Zygnematophycidae;
OC Zygnematales; Zygnemataceae; Zygnema.
OX NCBI_TaxID=35869;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16236178; DOI=10.1186/1741-7007-3-22;
RA Turmel M., Otis C., Lemieux C.;
RT "The complete chloroplast DNA sequences of the charophycean green algae
RT Staurastrum and Zygnema reveal that the chloroplast genome underwent
RT extensive changes during the evolution of the Zygnematales.";
RL BMC Biol. 3:22-22(2005).
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:0000255|HAMAP-Rule:MF_01346}.
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, b, b' and c. {ECO:0000255|HAMAP-Rule:MF_01346}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_01346}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-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; AY958086; AAX45795.1; -; Genomic_DNA.
DR RefSeq; YP_636515.1; NC_008117.1.
DR AlphaFoldDB; Q32RL1; -.
DR SMR; Q32RL1; -.
DR GeneID; 4108255; -.
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; ATP-binding; CF(1); Chloroplast; Hydrogen ion transport;
KW Ion transport; Membrane; Nucleotide-binding; Plastid; Thylakoid;
KW Translocase; Transport.
FT CHAIN 1..505
FT /note="ATP synthase subunit alpha, chloroplastic"
FT /id="PRO_0000238445"
FT BINDING 170..177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT SITE 363
FT /note="Required for activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
SQ SEQUENCE 505 AA; 54792 MW; D3BDE439E5F5962C CRC64;
MVNIRPDEIS SIIRKQIEQY TQEVKVVNIG TVLQVGDGIA RIYGLDKVMA GELLEFEDGT
IGIALNLESD NVGAVLMGDG LTIQEGSSVK ATGKIAQIPV SDGYLGRVVN ALARPIDGKG
DIASSEFRLI ESPAPGIISR RSVYEPMQTG LIAIDAMIPI GRGQRELIIG DRQTGKTAVA
TDTILNQKGQ NVICVYVAIG QKASSVAQVV NTFEERGAMD YTIVVAETAN APATLQYLAP
YTGAALAEYF MYKGQHTLVV YDDLSKQAQA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE
RAAKLGSQLG EGSMTALPIV ETQAGDVSAY IPTNVISITD GQIFLSADLF NSGIRPAINV
GISVSRVGSA AQIKAMKQVA GKLKLELAQF AELEAFSQFA SDLDKATQNQ LARGQRLREL
LKQAQSAPLS VEQQVATIFT GVNGYLDVIE VSQVRSFLTQ LREYIITNKP QFGEIIRSTK
TFTDEAQTIL KQAIQEHTEA FLLQQ