ID   ATPO_DICDI              Reviewed;         296 AA.
AC   Q54RA8;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=ATP synthase subunit O, mitochondrial {ECO:0000305};
DE   AltName: Full=ATP synthase peripheral stalk subunit OSCP {ECO:0000305};
DE   AltName: Full=Oligomycin sensitivity conferral protein;
DE            Short=OSCP;
DE   Flags: Precursor;
GN   Name=atp5po {ECO:0000250|UniProtKB:P48047}; Synonyms=atp5O;
GN   ORFNames=DDB_G0283283;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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 and the peripheric stalk, which acts as a stator to hold
CC       the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static
CC       relative to the rotary elements (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. Mitochondrion inner membrane
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATPase delta chain family. {ECO:0000305}.
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DR   EMBL; AAFI02000052; EAL65782.1; -; Genomic_DNA.
DR   RefSeq; XP_639139.1; XM_634047.1.
DR   AlphaFoldDB; Q54RA8; -.
DR   SMR; Q54RA8; -.
DR   PaxDb; Q54RA8; -.
DR   EnsemblProtists; EAL65782; EAL65782; DDB_G0283283.
DR   GeneID; 8624009; -.
DR   KEGG; ddi:DDB_G0283283; -.
DR   dictyBase; DDB_G0283283; atp5O.
DR   eggNOG; ENOG502RBP1; Eukaryota.
DR   HOGENOM; CLU_941430_0_0_1; -.
DR   InParanoid; Q54RA8; -.
DR   OMA; YIIESPF; -.
DR   PhylomeDB; Q54RA8; -.
DR   PRO; PR:Q54RA8; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0000274; C:mitochondrial proton-transporting ATP synthase, stator stalk; IBA:GO_Central.
DR   GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; 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; IBA:GO_Central.
DR   InterPro; IPR026015; ATP_synth_OSCP/delta_N_sf.
DR   InterPro; IPR000711; ATPase_OSCP/dsu.
DR   PANTHER; PTHR11910; PTHR11910; 1.
DR   Pfam; PF00213; OSCP; 1.
DR   SUPFAM; SSF47928; SSF47928; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; Hydrogen ion transport; Ion transport; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Transit peptide; Transport.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..296
FT                   /note="ATP synthase subunit O, mitochondrial"
FT                   /id="PRO_0000350580"
SQ   SEQUENCE   296 AA;  33130 MW;  59A09D8AD9B9866B CRC64;
     MLARFSRTAI KSGRYFSTSA KNTAPVSEAE EIEILKAVEA PQFKDAVKKT RQQYQDMISK
     LTNDESGKSI TQSTGLRPTI NISTPSGKIA HALFDAASSM RSVGIVAKEL TQVKTIIDKT
     PGLKTALEGD IDNSEKTVML ELLQGSVTLS PVSGFFLYYM TYENNFKLIN PALTDFKRLV
     GSLDTEMSIK LTVAHQYSEA EKKDLETNVK SFFPPETQFK FSYNVDPEIQ KGYIIESPFI
     NHDASYSTAV KKVKAQEQSV LAEFLNDIKN GIKNQTAVWE TKEFRDKYLT LDESKN