ID   ATP6_EMEND              Reviewed;         256 AA.
AC   P00852;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=ATP synthase subunit a;
DE   AltName: Full=F-ATPase protein 6;
DE   Flags: Precursor;
GN   Name=atp6;
OS   Emericella nidulans (Aspergillus nidulans).
OG   Mitochondrion.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=162425;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=pabaA1 biA1;
RX   PubMed=6290989; DOI=10.1093/nar/10.15.4783;
RA   Netzker R., Koechel H.G., Basak N., Kuentzel H.;
RT   "Nucleotide sequence of Aspergillus nidulans mitochondrial genes coding for
RT   ATPase subunit 6, cytochrome oxidase subunit 3, seven unidentified
RT   proteins, four tRNAs and L-rRNA.";
RL   Nucleic Acids Res. 10:4783-4794(1982).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=yA2 pyroA4 cnxC3;
RX   PubMed=6285306; DOI=10.1093/nar/10.11.3531;
RA   Grisi E., Brown T.A., Waring R.B., Scazzocchio C., Davies R.W.;
RT   "Nucleotide sequence of a region of the mitochondrial genome of Aspergillus
RT   nidulans including the gene for ATPase subunit 6.";
RL   Nucleic Acids Res. 10:3531-3539(1982).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1588598; DOI=10.1007/bf00162974;
RA   Karlovsky P., Fartmann B.;
RT   "Genetic code and phylogenetic origin of oomycetous mitochondria.";
RL   J. Mol. Evol. 34:254-258(1992).
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; X01507; CAA25707.1; -; Genomic_DNA.
DR   EMBL; X04161; CAA27773.1; -; Genomic_DNA.
DR   EMBL; J01390; AAA99205.1; -; Genomic_DNA.
DR   PIR; C93436; PWAS6N.
DR   AlphaFoldDB; P00852; -.
DR   SMR; P00852; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); ISO:AspGD.
DR   GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; ISO:AspGD.
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   PROPEP          1..8
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000002612"
FT   CHAIN           9..256
FT                   /note="ATP synthase subunit a"
FT                   /id="PRO_0000002613"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        121..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        148..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        186..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        209..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        230..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   256 AA;  28401 MW;  2854065D9229730E CRC64;
     MYQFNFILSP LDQFEIRDLF SLNANVLGNI HLSITNIGLY LSIGLLLTLG YHLLAANNKI
     IPNNWSISQE AIYATVHSIV INQLNPTKGQ LYFPFIYALF IFILVNNLIG MVPYSFASTS
     HFILTFSMSF TIVLGATFLG LQRHGLKFFS LFVPSGCPLG LLPLLVLIEF ISYLSRNVSL
     GLRLAANILS GHMLLSILSG FTYNIMTSGI LFFFLGLIPL AFIIAFSGLE LAIAFIQAQV
     FVVLTCSYIK DGLDLH