ID   ATP6_CANGA              Reviewed;         260 AA.
AC   Q85Q99;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 97.
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   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OG   Mitochondrion.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=12527359; DOI=10.1016/s0014-5793(02)03749-3;
RA   Koszul R., Malpertuy A., Frangeul L., Bouchier C., Wincker P., Thierry A.,
RA   Duthoy S., Ferris S., Hennequin C., Dujon B.;
RT   "The complete mitochondrial genome sequence of the pathogenic yeast Candida
RT   (Torulopsis) glabrata.";
RL   FEBS Lett. 534:39-48(2003).
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; Multi-pass membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000305}.
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DR   EMBL; AJ511533; CAD54424.1; -; Genomic_DNA.
DR   RefSeq; NP_818783.1; NC_004691.1.
DR   AlphaFoldDB; Q85Q99; -.
DR   SMR; Q85Q99; -.
DR   STRING; 284593.Q85Q99; -.
DR   GeneID; 807015; -.
DR   KEGG; cgr:CaglfMp09; -.
DR   CGD; CAL0139480; ATP6.
DR   VEuPathDB; FungiDB:CaglfMp09; -.
DR   InParanoid; Q85Q99; -.
DR   Proteomes; UP000002428; Mitochondrion.
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:CGD.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:EnsemblFungi.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; ISO:CGD.
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..11
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000002608"
FT   CHAIN           12..260
FT                   /note="ATP synthase subunit a"
FT                   /id="PRO_0000002609"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        96..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        126..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        152..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        192..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        217..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   260 AA;  29317 MW;  3698505FC40F46BC CRC64;
     MQNTLLRTYI NSPLEQFEVK TFLGLNTPFI DLSGLNITTF TLYTIIVLLV VSSLYVLSNN
     NNKIIGSRWL LSQEVIYDTI LNMVKGQIKG KDWGYYFPFI YTLFMFILIS NLISMIPYSY
     ALTAQFVFII SLSMIIWLGI TILSLFKHGW VFFSLFVPSG TALPLVPLLV VIELLSYVAR
     AFSLGLRLSA NIFSGHLLMA ILAGLTMTFV QINIFTLILG FIPLAIILII MCLEFGIAII
     QAYVFSILAS SYLKDGLYLH