ID   ATPI_CUSEX              Reviewed;         247 AA.
AC   A8W3B2;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=ATP synthase subunit a, plastid {ECO:0000255|HAMAP-Rule:MF_01393};
DE   AltName: Full=ATP synthase F0 sector subunit a {ECO:0000255|HAMAP-Rule:MF_01393};
DE   AltName: Full=F-ATPase subunit IV {ECO:0000255|HAMAP-Rule:MF_01393};
GN   Name=atpI {ECO:0000255|HAMAP-Rule:MF_01393};
OS   Cuscuta exaltata (Tall dodder).
OG   Plastid.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Convolvulaceae; Cuscuteae; Cuscuta;
OC   Cuscuta subgen. Monogynella.
OX   NCBI_TaxID=476139;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17956636; DOI=10.1186/1471-2229-7-57;
RA   McNeal J.R., Kuehl J.V., Boore J.L., dePamphilis C.W.;
RT   "Complete plastid genome sequences suggest strong selection for retention
RT   of photosynthetic genes in the parasitic plant genus Cuscuta.";
RL   BMC Plant Biol. 7:57-57(2007).
CC   -!- FUNCTION: Key component of the proton channel; it plays a direct role
CC       in the translocation of protons across the membrane.
CC       {ECO:0000255|HAMAP-Rule:MF_01393}.
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_01393}.
CC   -!- SUBCELLULAR LOCATION: Plastid membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000255|HAMAP-Rule:MF_01393}.
CC   -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000255|HAMAP-
CC       Rule:MF_01393}.
CC   -!- CAUTION: Young tissue from this organism is photosynthetic and contains
CC       some thylakoids, although the photosynthetic activity does not exceed
CC       the light compensation point. {ECO:0000305}.
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DR   EMBL; EU189132; ABW83683.1; -; Genomic_DNA.
DR   RefSeq; YP_001542519.1; NC_009963.1.
DR   AlphaFoldDB; A8W3B2; -.
DR   SMR; A8W3B2; -.
DR   GeneID; 5729601; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042170; C:plastid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR   GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEA:InterPro.
DR   Gene3D; 1.20.120.220; -; 1.
DR   HAMAP; MF_01393; ATP_synth_a_bact; 1.
DR   InterPro; IPR045082; ATP_syn_F0_a_bact/chloroplast.
DR   InterPro; IPR000568; ATP_synth_F0_asu.
DR   InterPro; IPR023011; ATP_synth_F0_asu_AS.
DR   InterPro; IPR035908; F0_ATP_A_sf.
DR   PANTHER; PTHR42823; PTHR42823; 1.
DR   Pfam; PF00119; ATP-synt_A; 1.
DR   PRINTS; PR00123; ATPASEA.
DR   SUPFAM; SSF81336; SSF81336; 1.
DR   TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 1.
DR   PROSITE; PS00449; ATPASE_A; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; CF(0); Hydrogen ion transport; Ion transport; Membrane;
KW   Plastid; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..247
FT                   /note="ATP synthase subunit a, plastid"
FT                   /id="PRO_0000362548"
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        134..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        220..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
SQ   SEQUENCE   247 AA;  27039 MW;  03325C19B6565F3B CRC64;
     MDVLSCSINT LKGLYDISGV EVGQHFYWQI GDFLVHGQVL ITSWVVIAIL LGSATVAVRN
     PQTIPTGGQN FFEYVLEFIR DVSKTQIGEE YGPWVPFIGT MFLFIFVSNW SGALLPWKIL
     QLPHGELAAP TNDINTTVAL ALLTSAAYFY AGILKKGLGY FEKYIKPTPI LLPINILEDF
     TKPLSLSFRL FGNILADELV VVVLVSLVPS VVPIPVMLLG LFTSGIQALI FATLAAAYIG
     ESMEGHL