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Database: UniProt
Entry: Q3ZVE2_ARATH
LinkDB: Q3ZVE2_ARATH
Original site: Q3ZVE2_ARATH 
ID   Q3ZVE2_ARATH            Unreviewed;       180 AA.
AC   Q3ZVE2;
DT   27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=ATPase alpha subunit {ECO:0000313|EMBL:CAI98996.1};
DE   Flags: Fragment;
GN   Name=atpA {ECO:0000313|EMBL:CAI98996.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OG   Plastid; Chloroplast {ECO:0000313|EMBL:CAI98996.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702 {ECO:0000313|EMBL:CAI98996.1};
RN   [1] {ECO:0000313|EMBL:CAI98996.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Cape Verde Islands {ECO:0000313|EMBL:CAI98996.1};
RX   PubMed=16115067; DOI=10.1111/j.1365-313X.2005.02484.x;
RA   Tillich M., Funk H.T., Schmitz-Linneweber C., Poltnigg P., Sabater B.,
RA   Martin M., Maier R.M.;
RT   "Editing of plastid RNA in Arabidopsis thaliana ecotypes.";
RL   Plant J. 43:708-715(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:0000256|ARBA:ARBA00003784}.
CC   -!- SUBCELLULAR LOCATION: Plastid membrane {ECO:0000256|ARBA:ARBA00037835};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00037835}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000256|ARBA:ARBA00008936}.
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DR   EMBL; AJ971658; CAI98996.1; -; Genomic_DNA.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
DR   GO; GO:0042170; C:plastid 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-KW.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR   Gene3D; 3.40.50.12240; -; 1.
DR   InterPro; IPR005294; ATP_synth_F1_asu.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR48082:SF12; ATP SYNTHASE SUBUNIT ALPHA, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR48082; ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   Chloroplast {ECO:0000313|EMBL:CAI98996.1};
KW   Plastid {ECO:0000313|EMBL:CAI98996.1}.
FT   DOMAIN          3..180
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT                   nucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00006"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CAI98996.1"
FT   NON_TER         180
FT                   /evidence="ECO:0000313|EMBL:CAI98996.1"
SQ   SEQUENCE   180 AA;  19678 MW;  218043BEE26E91DD CRC64;
     QTGLIAIDSM IPIGRGQREL IIGDRQTGKT AVATDTIXNQ QGQNVICVYV AIGQKASSVA
     QVVTSLQERG AMEYTIVVAE TADSPATLQY LAPYTGAALA EYFMYREQHT LIIYDDLSKQ
     AQAYRQMSLL LRRPPGREAY PGDVFYLHSR LLERAAKLSX QLGEGSMTAL PIVETQSGDV
//
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