ID   ATPO_KLULA              Reviewed;         206 AA.
AC   O74190; Q6CTS7;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 2.
DT   25-MAY-2022, entry version 121.
DE   RecName: Full=ATP synthase subunit 5, mitochondrial;
DE            Short=ATP synthase chain 5;
DE   AltName: Full=Oligomycin sensitivity conferral protein;
DE            Short=OSCP;
DE   Flags: Precursor;
GN   Name=ATP5; OrderedLocusNames=KLLA0C10384g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CK56-7A;
RX   PubMed=9790576; DOI=10.1007/s004380050836;
RA   Chen X.J., Hansbro P.M., Clark-Walker G.D.;
RT   "Suppression of rho0 lethality by mitochondrial ATP synthase F1 mutations
RT   in Kluyveromyces lactis occurs in the absence of F0.";
RL   Mol. Gen. Genet. 259:457-467(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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   -!- SIMILARITY: Belongs to the ATPase delta chain family. {ECO:0000305}.
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DR   EMBL; AF008185; AAC64903.1; -; Genomic_DNA.
DR   EMBL; CR382123; CAH01513.1; -; Genomic_DNA.
DR   RefSeq; XP_452662.1; XM_452662.1.
DR   AlphaFoldDB; O74190; -.
DR   SMR; O74190; -.
DR   STRING; 28985.XP_452662.1; -.
DR   EnsemblFungi; CAH01513; CAH01513; KLLA0_C10384g.
DR   GeneID; 2891844; -.
DR   KEGG; kla:KLLA0_C10384g; -.
DR   eggNOG; KOG1662; Eukaryota.
DR   HOGENOM; CLU_085114_0_0_1; -.
DR   InParanoid; O74190; -.
DR   OMA; MVDNIQD; -.
DR   Proteomes; UP000000598; Chromosome C.
DR   GO; GO:0000274; C:mitochondrial proton-transporting ATP synthase, stator stalk; IEA:EnsemblFungi.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:EnsemblFungi.
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   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           ?..206
FT                   /note="ATP synthase subunit 5, mitochondrial"
FT                   /id="PRO_0000002653"
FT   CONFLICT        60
FT                   /note="A -> V (in Ref. 1; AAC64903)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   206 AA;  22092 MW;  FDC5FB4CB844614F CRC64;
     MFSRVFVRSM AASAKAGVKP PVQLFGLDGT YATALFTAAS KTTSVEAAAS SLNALKETVA
     KDTKLTSILE NPALSAEDRN IVVDTLSKKI NLDQSVQNLL KVLAENNRLS LLEHVTSQFS
     KLTDAYHGLV QATVTTAQPL DSKLFKRVEK ALAASSLVGK GKSLKLENVV KPEIQGGLIV
     EVSDRTVDLS IASRINKLNQ VLREAI