ID   ATP8_CANAL              Reviewed;          48 AA.
AC   Q9B8D3;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 2.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=ATP synthase protein 8;
DE   AltName: Full=A6L;
DE   AltName: Full=F-ATPase subunit 8;
GN   Name=ATP8; OrderedLocusNames=CM_00170C {ECO:0000312|CGD:CAL0000189026};
GN   ORFNames=CaalfMp07;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OG   Mitochondrion.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=11208783; DOI=10.1128/jb.183.3.865-872.2001;
RA   Anderson J.B., Wickens C., Khan M., Cowen L.E., Federspiel N.A., Jones T.,
RA   Kohn L.M.;
RT   "Infrequent genetic exchange and recombination in the mitochondrial genome
RT   of Candida albicans.";
RL   J. Bacteriol. 183:865-872(2001).
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. Part of the complex
CC       F(0) domain. Minor subunit located with subunit a in the membrane (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC       - and CF(0) - the membrane proton channel. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Single-pass membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the ATPase protein 8 family. {ECO:0000305}.
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DR   EMBL; AF285261; AAG59593.2; -; Genomic_DNA.
DR   RefSeq; NP_075036.2; NC_002653.1.
DR   AlphaFoldDB; Q9B8D3; -.
DR   SMR; Q9B8D3; -.
DR   GeneID; 802553; -.
DR   KEGG; cal:CaalfMp07; -.
DR   CGD; CAL0000189026; ATP8.
DR   VEuPathDB; FungiDB:CM_00170C; -.
DR   InParanoid; Q9B8D3; -.
DR   Proteomes; UP000000559; 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); ISS:CGD.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; ISS:CGD.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; ISS:CGD.
DR   InterPro; IPR009230; ATP_synth_su8_fun.
DR   Pfam; PF05933; Fun_ATP-synt_8; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; CF(0); Hydrogen ion transport; Ion transport; Membrane;
KW   Mitochondrion; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..48
FT                   /note="ATP synthase protein 8"
FT                   /id="PRO_0000356860"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   48 AA;  5352 MW;  E9D6F37787496D51 CRC64;
     MPQLVPFYWM NLLTTGIAAV SILLYLSATI ILPNVLRLLV ARAIIVRV