ID   ATPO_IPOBA              Reviewed;         244 AA.
AC   P22778;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=ATP synthase subunit O, mitochondrial;
DE   AltName: Full=Oligomycin sensitivity conferral protein;
DE            Short=OSCP;
DE   Flags: Precursor;
OS   Ipomoea batatas (Sweet potato) (Convolvulus batatas).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Convolvulaceae; Ipomoeeae; Ipomoea.
OX   NCBI_TaxID=4120;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Kokei No. 14; TISSUE=Tuberous root;
RX   PubMed=1690722; DOI=10.1016/s0021-9258(19)39294-4;
RA   Kimura T., Takeda S., Asahi T., Nakamura K.;
RT   "Primary structure of a precursor for the delta-subunit of sweet potato
RT   mitochondrial F1-ATPase deduced from full length cDNA.";
RL   J. Biol. Chem. 265:6079-6085(1990).
RN   [2]
RP   PROTEIN SEQUENCE OF 46-78.
RC   STRAIN=cv. Kokei No. 14; TISSUE=Tuberous root;
RX   PubMed=2536736; DOI=10.1016/s0021-9258(18)94048-2;
RA   Kimura T., Nakamura K., Kajiura H., Hattori H., Nelson N., Asahi T.;
RT   "Correspondence of minor subunits of plant mitochondrial F1ATPase to
RT   F1F0ATPase subunits of other organisms.";
RL   J. Biol. Chem. 264:3183-3186(1989).
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.
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. Mitochondrion inner membrane.
CC   -!- SIMILARITY: Belongs to the ATPase delta chain family. {ECO:0000305}.
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DR   EMBL; J05397; AAA33388.1; -; mRNA.
DR   PIR; A35227; A35227.
DR   AlphaFoldDB; P22778; -.
DR   SMR; P22778; -.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR   Gene3D; 1.10.520.20; -; 1.
DR   HAMAP; MF_01416; ATP_synth_delta_bact; 1.
DR   InterPro; IPR026015; ATP_synth_OSCP/delta_N_sf.
DR   InterPro; IPR020781; ATPase_OSCP/d_CS.
DR   InterPro; IPR000711; ATPase_OSCP/dsu.
DR   PANTHER; PTHR11910; PTHR11910; 1.
DR   Pfam; PF00213; OSCP; 1.
DR   PRINTS; PR00125; ATPASEDELTA.
DR   SUPFAM; SSF47928; SSF47928; 1.
DR   TIGRFAMs; TIGR01145; ATP_synt_delta; 1.
DR   PROSITE; PS00389; ATPASE_DELTA; 1.
PE   1: Evidence at protein level;
KW   ATP synthesis; Direct protein sequencing; Hydrogen ion transport;
KW   Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Transit peptide; Transport.
FT   TRANSIT         1..45
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:2536736"
FT   CHAIN           46..244
FT                   /note="ATP synthase subunit O, mitochondrial"
FT                   /id="PRO_0000002644"
FT   VARIANT         4
FT                   /note="T -> A"
SQ   SEQUENCE   244 AA;  27201 MW;  45F6F85307465139 CRC64;
     MAMTGRARSM GFSILQKALS SAQRSNAHRS ILCPTLSNSE LLRNYATASA SKEQKIKVPL
     TMYGVSGNYA SALYLAAVKS NTLEKVESEL YDLVEASKKS PTFSQFMRDP SVPVDTRVNA
     IKEICAQAKF GDTTQNFLLI LAENGRLKHI DRIVKRFKEL TMAHRGEVKA TVTTVIPLPA
     DEEKELKATL QEMVGQGKSV QIEQKIDPTI LGGLVVEFGQ KVFDMSIRTR ARQMERFLRE
     PLNF