ID   ATPA_KLULA              Reviewed;         548 AA.
AC   P49375;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=ATP synthase subunit alpha, mitochondrial;
DE   Flags: Precursor;
GN   Name=ATP1; Synonyms=MGI2; OrderedLocusNames=KLLA0E06644g;
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], AND MUTANTS MGI2-1 AND MGI2-2.
RC   STRAIN=ATCC 76492 / CBS 2359/152 / CLIB 210;
RX   PubMed=7621839; DOI=10.1002/j.1460-2075.1995.tb07331.x;
RA   Chen X.J., Clark-Walker G.D.;
RT   "Specific mutations in alpha- and gamma-subunits of F1-ATPase affect
RT   mitochondrial genome integrity in the petite-negative yeast Kluyveromyces
RT   lactis.";
RL   EMBO J. 14:3277-3286(1995).
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. Subunits alpha and
CC       beta form the catalytic core in F(1). Rotation of the central stalk
CC       against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of
CC       ATP in three separate catalytic sites on the beta subunits. Subunit
CC       alpha does not bear the catalytic high-affinity ATP-binding sites (By
CC       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.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC       Note=Peripheral membrane protein.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
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DR   EMBL; X79106; CAA55723.1; -; Genomic_DNA.
DR   EMBL; CR382125; CAG99335.1; -; Genomic_DNA.
DR   PIR; S56152; S56152.
DR   RefSeq; XP_454248.1; XM_454248.1.
DR   AlphaFoldDB; P49375; -.
DR   SMR; P49375; -.
DR   STRING; 28985.XP_454248.1; -.
DR   PRIDE; P49375; -.
DR   EnsemblFungi; CAG99335; CAG99335; KLLA0_E06667g.
DR   GeneID; 2894293; -.
DR   KEGG; kla:KLLA0_E06667g; -.
DR   eggNOG; KOG1353; Eukaryota.
DR   HOGENOM; CLU_010091_2_0_1; -.
DR   InParanoid; P49375; -.
DR   OMA; LQAPGVM; -.
DR   Proteomes; UP000000598; Chromosome E.
DR   GO; GO:0042645; C:mitochondrial nucleoid; IEA:EnsemblFungi.
DR   GO; GO:0005754; C:mitochondrial proton-transporting ATP synthase, catalytic core; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:EnsemblFungi.
DR   CDD; cd18113; ATP-synt_F1_alpha_C; 1.
DR   CDD; cd01132; F1_ATPase_alpha; 1.
DR   Gene3D; 1.20.150.20; -; 1.
DR   Gene3D; 2.40.30.20; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_01346; ATP_synth_alpha_bact; 1.
DR   InterPro; IPR023366; ATP_synth_asu-like_sf.
DR   InterPro; IPR000793; ATP_synth_asu_C.
DR   InterPro; IPR038376; ATP_synth_asu_C_sf.
DR   InterPro; IPR033732; ATP_synth_F1_a.
DR   InterPro; IPR005294; ATP_synth_F1_asu.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR   InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF00306; ATP-synt_ab_C; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   PIRSF; PIRSF039088; F_ATPase_subunit_alpha; 1.
DR   SUPFAM; SSF50615; SSF50615; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00962; atpA; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   1: Evidence at protein level;
KW   ATP synthesis; ATP-binding; CF(1); Hydrogen ion transport; Ion transport;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding;
KW   Reference proteome; Transit peptide; Transport.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..548
FT                   /note="ATP synthase subunit alpha, mitochondrial"
FT                   /id="PRO_0000002430"
FT   BINDING         209..216
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   SITE            410
FT                   /note="Required for activity"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         333
FT                   /note="A->V: In MGI2-1; converts K.lactis into a petite-
FT                   positive form."
FT   MUTAGEN         443
FT                   /note="F->S: In MGI2-2; converts K.lactis into a petite-
FT                   positive form."
SQ   SEQUENCE   548 AA;  59103 MW;  FB51D7A2CB18A3DD CRC64;
     MLSRSAIRSA SRSVVAANLV RSMNRVARPA LVVAGRRFAS AKAQPTEVSS ILEERIRGVS
     EESNLNETGR VLAVGDGIAR VFGLNNVQAE ELVEFSSGVK GMALNLEPGQ VGIVLFGSDR
     LVKEGEVVKR TGKIVDVGVG PELLGRVVDA LGNPIDGKGP INASGRSRAQ VKAPGILPRR
     SVHEPVQTGL KSVDALVPIG RGQRELIIGD RQTGKTAVAL DTILNQKRWN NGTDESKKLY
     CVYVAVGQKR STVAQLVQTL EQHDALKYSI IVAATASEAA PLQYIAPFTA AAIGEWFRDN
     GRHALIIYDD LSKQAVAYRQ LSLLLRRPPG REAYPGDVFY LHSRLLERAA KMSEKNGGGS
     LTALPVIETQ GGDVSAYIPT NVISITDGQI FLEAELFYKG IRPAINVGLS VSRVGSAAQV
     KALKQVAGSL KLFLAQYREV AAFAQFGSDL DASTKQTLAR GERLTQLLKQ NQYSPLAAEE
     QVPLIYAGVN GYLDNIDISR IAEFETKFLA YLKANHDEIV SAIREKGELS KELLATLKSA
     TESFVATF