ID   ATP9_CANAL              Reviewed;          76 AA.
AC   Q9B8D5;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=ATP synthase subunit 9, mitochondrial;
DE   AltName: Full=Lipid-binding protein;
GN   Name=ATP9; OrderedLocusNames=CM_00140C {ECO:0000312|CGD:CAL0000186811};
GN   ORFNames=CaalfMp05;
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. A homomeric c-ring of probably 10 subunits is part of the
CC       complex rotary element (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.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000305}.
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DR   EMBL; AF285261; AAG59591.1; -; Genomic_DNA.
DR   RefSeq; NP_075034.1; NC_002653.1.
DR   AlphaFoldDB; Q9B8D5; -.
DR   SMR; Q9B8D5; -.
DR   STRING; 237561.Q9B8D5; -.
DR   GeneID; 802561; -.
DR   KEGG; cal:CaalfMp05; -.
DR   CGD; CAL0000186811; ATP9.
DR   VEuPathDB; FungiDB:CM_00140C; -.
DR   InParanoid; Q9B8D5; -.
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:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IBA:GO_Central.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
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   Gene3D; 1.20.20.10; -; 1.
DR   HAMAP; MF_01396; ATP_synth_c_bact; 1.
DR   InterPro; IPR000454; ATP_synth_F0_csu.
DR   InterPro; IPR020537; ATP_synth_F0_csu_DDCD_BS.
DR   InterPro; IPR038662; ATP_synth_F0_csu_sf.
DR   InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR   InterPro; IPR035921; F/V-ATP_Csub_sf.
DR   PANTHER; PTHR10031; PTHR10031; 1.
DR   Pfam; PF00137; ATP-synt_C; 1.
DR   PRINTS; PR00124; ATPASEC.
DR   SUPFAM; SSF81333; SSF81333; 1.
DR   PROSITE; PS00605; ATPASE_C; 1.
PE   3: Inferred from homology;
KW   CF(0); Hydrogen ion transport; Ion transport; Lipid-binding; Membrane;
KW   Mitochondrion; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..76
FT                   /note="ATP synthase subunit 9, mitochondrial"
FT                   /id="PRO_0000356858"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        52..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   SITE            59
FT                   /note="Reversibly protonated during proton transport"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   76 AA;  7790 MW;  07C2F17024E055A5 CRC64;
     MQLALAAKYI GASIATLGLG GAAIGIALVF VALINGTSRN PSLRSTLFPQ AILGFALSEA
     CGLFCLMISF LLLYAV