ID   ATP9_SCHPO              Reviewed;          74 AA.
AC   P21537;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 3.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=ATP synthase subunit 9, mitochondrial;
DE   AltName: Full=Lipid-binding protein;
GN   Name=atp9; ORFNames=SPMIT.10;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OG   Mitochondrion.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AD7-50;
RA   Lang B.F.;
RT   "The mitochondrial genome of Schizosaccharomyces pombe.";
RL   (In) O'Brien S.J. (eds.);
RL   Genetic Maps (6th edition), pp.3118-3119, Cold Spring Harbor Laboratory
RL   Press, New York (1993).
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.
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; X54421; CAA38292.1; -; Genomic_DNA.
DR   PIR; S78203; S78203.
DR   RefSeq; NP_039507.1; NC_001326.1.
DR   AlphaFoldDB; P21537; -.
DR   SMR; P21537; -.
DR   STRING; 4896.SPMIT.10.1; -.
DR   PaxDb; P21537; -.
DR   EnsemblFungi; SPMIT.10.1; SPMIT.10.1:pep; SPMIT.10.
DR   GeneID; 1669532; -.
DR   KEGG; spo:ScpofMp09; -.
DR   PomBase; SPMIT.10; atp9.
DR   VEuPathDB; FungiDB:SPMIT.10; -.
DR   eggNOG; KOG3025; Eukaryota.
DR   HOGENOM; CLU_148047_4_1_1; -.
DR   InParanoid; P21537; -.
DR   OMA; CMGFCIL; -.
DR   PhylomeDB; P21537; -.
DR   Reactome; R-SPO-163210; Formation of ATP by chemiosmotic coupling.
DR   Reactome; R-SPO-8949613; Cristae formation.
DR   PRO; PR:P21537; -.
DR   Proteomes; UP000002485; 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:PomBase.
DR   GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IBA:GO_Central.
DR   GO; GO:0008289; F:lipid binding; 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; IBA:GO_Central.
DR   GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; ISO:PomBase.
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..74
FT                   /note="ATP synthase subunit 9, mitochondrial"
FT                   /id="PRO_0000112235"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        50..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   SITE            57
FT                   /note="Reversibly protonated during proton transport"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   74 AA;  7561 MW;  169F795336BF5FAA CRC64;
     MIQAAKYIGA GLATIGVSGA GVGIGLIFSN LISGTSRNPS VRPHLFSMAI LGFALTEATG
     LFCLMLAFLI IYAA