ID   ATP62_ARATH             Reviewed;         349 AA.
AC   P92547; Q1ZXW9;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=ATP synthase subunit a-2;
DE   AltName: Full=F-ATPase protein 6;
DE   AltName: Full=P6-2;
DE   Flags: Precursor;
GN   Name=ATP6-2; OrderedLocusNames=AtMg01170;
OS   Arabidopsis thaliana (Mouse-ear cress).
OG   Mitochondrion.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND RNA EDITING.
RC   STRAIN=cv. Columbia;
RX   PubMed=9039497; DOI=10.1093/dnares/3.5.287;
RA   Marienfeld J.R., Unseld M., Brandt P., Brennicke A.;
RT   "Genomic recombination of the mitochondrial atp6 gene in Arabidopsis
RT   thaliana at the protein processing site creates two different
RT   presequences.";
RL   DNA Res. 3:287-290(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. C24;
RX   PubMed=8988169; DOI=10.1038/ng0197-57;
RA   Unseld M., Marienfeld J.R., Brandt P., Brennicke A.;
RT   "The mitochondrial genome of Arabidopsis thaliana contains 57 genes in
RT   366,924 nucleotides.";
RL   Nat. Genet. 15:57-61(1997).
RN   [3]
RP   GENOME REANNOTATION (AT2G07699).
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND RNA EDITING.
RX   PubMed=10611383; DOI=10.1073/pnas.96.26.15324;
RA   Giege P., Brennicke A.;
RT   "RNA editing in Arabidopsis mitochondria effects 441 C to U changes in
RT   ORFs.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:15324-15329(1999).
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 (By similarity). {ECO:0000250}.
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=123 {ECO:0000269|PubMed:10611383,
CC       ECO:0000269|PubMed:9039497};
CC   -!- MISCELLANEOUS: The atp6 gene is located on the border of one of the
CC       mitochondrial DNA repeats resulting in two identical copies of the
CC       mature protein with different propeptide extensions.
CC   -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000305}.
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DR   EMBL; Y08501; CAA69800.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_085569.1; NC_001284.2.
DR   AlphaFoldDB; P92547; -.
DR   SMR; P92547; -.
DR   STRING; 3702.ATMG01170.1; -.
DR   PaxDb; P92547; -.
DR   PRIDE; P92547; -.
DR   Araport; ATMG01170; -.
DR   eggNOG; KOG4665; Eukaryota.
DR   InParanoid; P92547; -.
DR   OrthoDB; 1095315at2759; -.
DR   PRO; PR:P92547; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   Proteomes; UP000006548; Mitochondrion (cv. C24).
DR   ExpressionAtlas; P92547; baseline and differential.
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; IBA:GO_Central.
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; Reference proteome;
KW   RNA editing; Transmembrane; Transmembrane helix; Transport.
FT   PROPEP          1..97
FT                   /id="PRO_0000002604"
FT   CHAIN           98..349
FT                   /note="ATP synthase subunit a-2"
FT                   /id="PRO_0000002605"
FT   TRANSMEM        118..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        184..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        213..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        280..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        303..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        326..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   349 AA;  39729 MW;  092504C68791ECA6 CRC64;
     MERLTRLNHF LVNMRWDFYE GVIQAGYIRN LQRELDHTPA ELLGSKLDLI FFRESLNLST
     YVNNWYMQNL GVPGPVNFIE KYHDACFSNY MKLMEIPSPL DQFEIVPLIP MHIGNFYFSF
     TNSSLFMLLT LSFFLLLIHF VTKKGGGNLV PNAWQSLVEL LYDFVLNLVK EQIGGLSGNV
     KQMFFPCILV TFLFLLFCNL QGMIPYSFTV TSHFLITLAL SFSIFIGITI VGFQRHGLHF
     FSFLLPAGVP LPLAPFLVLL ELISYCFRAL SLGIRLFANM MAGHSLVKIL SGFAWTMLCM
     NDIFYFIGAL GPLFIVLALT GLELGVAILQ AYVFTILICI YLNDAINLH