ID   ATP6_OENBE              Reviewed;         281 AA.
AC   P05500;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 2.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=ATP synthase subunit a;
DE   AltName: Full=F-ATPase protein 6;
GN   Name=ATP6;
OS   Oenothera berteroana (Bertero's evening primrose).
OG   Mitochondrion.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Onagraceae; Onagroideae; Onagreae; Oenothera.
OX   NCBI_TaxID=3950;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Munzia;
RX   PubMed=2960954; DOI=10.1093/nar/15.21.9092;
RA   Schuster W., Brennicke A.;
RT   "Nucleotide sequence of the Oenothera ATPase subunit 6 gene.";
RL   Nucleic Acids Res. 15:9092-9092(1987).
RN   [2]
RP   RNA EDITING.
RX   PubMed=1837275; DOI=10.1016/0014-5793(91)81394-n;
RA   Schuster W., Brennicke A.;
RT   "RNA editing in ATPase subunit 6 mRNAs in Oenothera mitochondria. A new
RT   termination codon shortens the reading frame by 35 amino acids.";
RL   FEBS Lett. 295:97-101(1991).
CC   -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or
CC       Complex V) produces ATP from ADP in the presence of a proton gradient
CC       across the membrane which is generated by electron transport complexes
CC       of the respiratory chain. F-type ATPases consist of two structural
CC       domains, F(1) - containing the extramembraneous catalytic core and F(0)
CC       - containing the membrane proton channel, linked together by a central
CC       stalk and a peripheral stalk. During catalysis, ATP synthesis in the
CC       catalytic domain of F(1) is coupled via a rotary mechanism of the
CC       central stalk subunits to proton translocation. Key component of the
CC       proton channel; it may play a direct role in the translocation of
CC       protons across the membrane.
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.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane
CC       protein.
CC   -!- RNA EDITING: Modified_positions=55 {ECO:0000269|PubMed:1837275}, 81
CC       {ECO:0000269|PubMed:1837275}, 98 {ECO:0000269|PubMed:1837275}, 100
CC       {ECO:0000269|PubMed:1837275}, 119 {ECO:0000269|PubMed:1837275}, 121
CC       {ECO:0000269|PubMed:1837275}, 127 {ECO:0000269|PubMed:1837275}, 130
CC       {ECO:0000269|PubMed:1837275}, 132 {ECO:0000269|PubMed:1837275}, 176
CC       {ECO:0000269|PubMed:1837275}, 196 {ECO:0000269|PubMed:1837275}, 197
CC       {ECO:0000269|PubMed:1837275}, 204 {ECO:0000269|PubMed:1837275}, 218
CC       {ECO:0000269|PubMed:1837275}, 254 {ECO:0000269|PubMed:1837275}, 261
CC       {ECO:0000269|PubMed:1837275}, 266 {ECO:0000269|PubMed:1837275}, 278
CC       {ECO:0000269|PubMed:1837275}, 282 {ECO:0000269|PubMed:1837275};
CC       Note=The stop codon at position 282 is created by RNA editing.;
CC   -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000305}.
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DR   EMBL; Y00465; CAA68527.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; P05500; -.
DR   SMR; P05500; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner 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; IPR000568; ATP_synth_F0_asu.
DR   InterPro; IPR023011; ATP_synth_F0_asu_AS.
DR   InterPro; IPR045083; ATP_synth_F0_asu_bact/mt.
DR   InterPro; IPR035908; F0_ATP_A_sf.
DR   PANTHER; PTHR11410; PTHR11410; 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   2: Evidence at transcript level;
KW   ATP synthesis; CF(0); Hydrogen ion transport; Ion transport; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; RNA editing; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..281
FT                   /note="ATP synthase subunit a"
FT                   /id="PRO_0000082143"
FT   TRANSMEM        50..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        116..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        145..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        219..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        246..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   281 AA;  31348 MW;  25EA5251A037321F CRC64;
     MKRFYKTAFF SEIGSEEVSH FWADTMSSHS PLEQFSILPL IPMNIGNLYF SFTNSSLFML
     LTLSLVLLLV NFVTKKGGGN LVPNAWQSLV ELIYDFVLNL VNEQIGGLSG NVKQKFFPCI
     LVTFTFLLFC NLQGMIPYSF TVTSHFLITL GLSFSIFIGI TIVGFQRNGL HFLSFLLPAG
     VPLPLAPFLV LLELISYCFR ALSLGIRLFA NMMAGHSLVK ILSGFAWTML CMNDLFYFIG
     DLGPLFIVLA LTGLELGVAI LQAYVFTILI CIYLNDAINL H