ID   ATP6_DEBHA              Reviewed;         246 AA.
AC   A9RAH2;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=ATP synthase subunit a;
DE   AltName: Full=ATP synthase subunit 6;
DE   AltName: Full=F-ATPase protein 6;
DE   Flags: Precursor;
GN   Name=ATP6;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OG   Mitochondrion.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=18673395; DOI=10.1111/j.1567-1364.2008.00409.x;
RA   Sacerdot C., Casaregola S., Lafontaine I., Tekaia F., Dujon B.,
RA   Ozier-Kalogeropoulos O.;
RT   "Promiscuous DNA in the nuclear genomes of hemiascomycetous yeasts.";
RL   FEMS Yeast Res. 8:846-857(2008).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000305}.
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DR   EMBL; DQ508940; ABF58073.1; -; Genomic_DNA.
DR   RefSeq; YP_001621424.1; NC_010166.1.
DR   AlphaFoldDB; A9RAH2; -.
DR   SMR; A9RAH2; -.
DR   STRING; 284592.A9RAH2; -.
DR   GeneID; 5845843; -.
DR   KEGG; dha:ATP6; -.
DR   InParanoid; A9RAH2; -.
DR   Proteomes; UP000000599; 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   PROPEP          1..3
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000355029"
FT   CHAIN           4..246
FT                   /note="ATP synthase subunit a"
FT                   /id="PRO_0000355030"
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        51..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        79..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        178..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        203..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   246 AA;  27189 MW;  236E5E99BCB1B748 CRC64;
     MIYSPTEQFE IKPLLTVNNM LTLSVNNYVM YVALVVTLMY SSVFLLNRTY LGFNRWGVAL
     LAVYDTILNM VKSQMGARGG MYFPFMFTLF TFMLVANLVS MMPYSFAMSA QLVAIVSFSL
     SLWFGCVLMG LSKHGWGFFA LFVPGGTPLA LVPVLVLIET LSYSSRAISL GLRLSANVLS
     GHLLMLILGT LMFNLMGSSM LGFMGGFMPV MGVIAIVVTE FAIGMMQAYV FTILLSSYIK
     DSVYLH