ID   ATP6_PODAN              Reviewed;         264 AA.
AC   P15994;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=ATP synthase subunit a;
DE   AltName: Full=F-ATPase protein 6;
GN   Name=ATP6;
OS   Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS   (Pleurage anserina).
OG   Mitochondrion.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC   Podospora anserina.
OX   NCBI_TaxID=515849;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A, and s;
RX   PubMed=2975708; DOI=10.1016/0022-2836(88)90044-7;
RA   Cummings D.J., Domenico J.M.;
RT   "Sequence analysis of mitochondrial DNA from Podospora anserina.
RT   Pervasiveness of a class I intron in three separate genes.";
RL   J. Mol. Biol. 204:815-839(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=s;
RX   PubMed=2357736; DOI=10.1007/bf00334517;
RA   Cummings D.J., McNally K.L., Domenico J.M., Matsuura E.T.;
RT   "The complete DNA sequence of the mitochondrial genome of Podospora
RT   anserina.";
RL   Curr. Genet. 17:375-402(1990).
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; X55026; CAA38770.1; -; Genomic_DNA.
DR   EMBL; X15602; CAA33625.1; -; Genomic_DNA.
DR   PIR; S02157; S02157.
DR   RefSeq; NP_074918.1; NC_001329.3.
DR   AlphaFoldDB; P15994; -.
DR   SMR; P15994; -.
DR   STRING; 515849.P15994; -.
DR   GeneID; 802471; -.
DR   KEGG; pan:PoanfMp10; -.
DR   Proteomes; UP000001197; Mitochondrion.
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; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..264
FT                   /note="ATP synthase subunit a"
FT                   /id="PRO_0000082156"
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        129..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        156..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        217..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        238..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   264 AA;  29318 MW;  8029AAEDB8402A17 CRC64;
     MNTLFNTVNF WRYNSSPLTQ FEIKDLISID TPILGNLHIS ITNIGFYLTM GAFFLLIINL
     LSTNYNKLIG NSWSISQESL YATLHSIVVN QINPKNGQIY FPFIYALFIF ILINNLIGMV
     PYSFASTSHF VLTFALSFTI VLGATILGFQ KHGLEFFSLL VPAGCPLGLL PLLVLIEFIS
     YLARNISLGL RLAANILSGH MLLHILAGFT YNIMTSGIIF FFLGLIPLAF IIAFSGLELG
     IAFIQAQVFV VLTSGYIKDA LDLH