ID   ATP7_KLULA              Reviewed;         174 AA.
AC   O13350; Q6CMS2;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=ATP synthase subunit d, mitochondrial;
GN   Name=ATP7; OrderedLocusNames=KLLA0E18172g;
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=ATCC 76492 / CBS 2359/152 / CLIB 210;
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
CC       F(0) - containing the membrane proton channel, linked together by a
CC       central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC       in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC       the 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   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATPase d subunit family. {ECO:0000305}.
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DR   EMBL; AF019223; AAC64861.1; -; Genomic_DNA.
DR   EMBL; CR382125; CAG99854.1; -; Genomic_DNA.
DR   RefSeq; XP_454767.1; XM_454767.1.
DR   AlphaFoldDB; O13350; -.
DR   SMR; O13350; -.
DR   STRING; 28985.XP_454767.1; -.
DR   EnsemblFungi; CAG99854; CAG99854; KLLA0_E18107g.
DR   GeneID; 2894292; -.
DR   KEGG; kla:KLLA0_E18107g; -.
DR   eggNOG; KOG3366; Eukaryota.
DR   HOGENOM; CLU_080463_0_0_1; -.
DR   InParanoid; O13350; -.
DR   OMA; VSKGRWA; -.
DR   Proteomes; UP000000598; Chromosome E.
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; 6.10.280.70; -; 1.
DR   InterPro; IPR008689; ATP_synth_F0_dsu_mt.
DR   InterPro; IPR036228; ATP_synth_F0_dsu_sf_mt.
DR   PANTHER; PTHR12700; PTHR12700; 1.
DR   Pfam; PF05873; Mt_ATP-synt_D; 1.
DR   PIRSF; PIRSF005514; ATPase_F0_D_mt; 1.
DR   SUPFAM; SSF161065; SSF161065; 1.
PE   3: Inferred from homology;
KW   Acetylation; ATP synthesis; CF(0); Hydrogen ion transport; Ion transport;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..174
FT                   /note="ATP synthase subunit d, mitochondrial"
FT                   /id="PRO_0000071678"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        42
FT                   /note="R -> I (in Ref. 1; AAC64861)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   174 AA;  19759 MW;  9634C227DB72C8E9 CRC64;
     MSLAKSAANK LDWAKVISSL KLTGKTATQL SSFKKRNDEA RRQLLELQSQ PTSVDFSHYR
     SVLKNTEVVD KIEQFYKSYK PVSVDVSKQL STIEAFESQA IENAAETEKL VAQELKDLKE
     TLNNIESARP FDQLTVDELT KARPEIDAKV EEMVKKGRWD VPGYKEKFGD LTIM