ID   ATP6_TRITI              Reviewed;         386 AA.
AC   P68526; P20599;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=ATP synthase subunit a;
DE   AltName: Full=F-ATPase protein 6;
GN   Name=ATP6;
OS   Triticum timopheevii (Timopheev's wheat) (Triticum dicoccon var.
OS   timopheevii).
OG   Mitochondrion.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4570;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=I/2;
RX   AGRICOLA=IND93035141;
RA   Mohr S.K., Schulte-Kappert E., Oettler G., Odenbach W., Kueck U.;
RT   "Mitochondrial DNA of cytoplasmic male-sterile Triticum timopheevi:
RT   rearrangement of upstream sequences of the atp6 and orf25 genes.";
RL   Theor. Appl. Genet. 86:259-268(1993).
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   -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000305}.
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DR   EMBL; X62092; CAA44002.1; -; Genomic_DNA.
DR   PIR; JA0095; PWWT6.
DR   RefSeq; YP_008758162.1; NC_022714.1.
DR   AlphaFoldDB; P68526; -.
DR   SMR; P68526; -.
DR   GeneID; 17428077; -.
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   3: Inferred from homology;
KW   ATP synthesis; CF(0); Hydrogen ion transport; Ion transport; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..386
FT                   /note="ATP synthase subunit a"
FT                   /id="PRO_0000082182"
FT   TRANSMEM        150..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        243..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        270..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        310..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   386 AA;  42992 MW;  1FB2F2391E7F60DD CRC64;
     MRFLSTDMKD RNMLFAAITT NQPIRSKCSR LPDLHDFFPT NISQNFAITP NLDITPTPER
     IAGVTIVLQI EEYLGQNESE QGAVNLARTV LGARHRNGET WQGILEDIRA GGGMDNFIQN
     LPGAYPETPL DQFAIIPIID LHVGNFYLSF TNEVLYMLLT VVLVVFLFFV VTKKGGGKSV
     PNAWQSLVEL IYDFVLNLVN EQIGGLSGNV KQKFFPRISV TFTFSLFRNP QGMIPFSFTV
     TSHFLITLAL SFSIFIGITI VGFQRHGLHF FSFLLPAGVP LPLAPFLVLL ELISYCFRAL
     SLGIRLFANM MAGHSLVKIL SGFAWTMLFL NNIFYFIGDL GPLFIVLALT GLELGVAISQ
     AHVSTISICI YLNDATNLHQ NESFHN