ID   ATPF_CANGA              Reviewed;         242 AA.
AC   Q6FRW0;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=ATP synthase subunit 4, mitochondrial;
DE   Flags: Precursor;
GN   Name=ATP4; OrderedLocusNames=CAGL0H05489g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC       - and CF(0) - the membrane proton channel. In yeast, the dimeric form
CC       of ATP synthase consists of 17 polypeptides: alpha, beta, gamma, delta,
CC       epsilon, 4 (B), 5 (OSCP), 6 (A), 8, 9 (C), d, E (Tim11), f, g, h, i/j
CC       and k (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Mitochondrion inner
CC       membrane {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ATPase B chain family.
CC       {ECO:0000305}.
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DR   EMBL; CR380954; CAG59967.1; -; Genomic_DNA.
DR   RefSeq; XP_447034.1; XM_447034.1.
DR   AlphaFoldDB; Q6FRW0; -.
DR   SMR; Q6FRW0; -.
DR   STRING; 5478.XP_447034.1; -.
DR   EnsemblFungi; CAG59967; CAG59967; CAGL0H05489g.
DR   GeneID; 2888579; -.
DR   KEGG; cgr:CAGL0H05489g; -.
DR   CGD; CAL0131524; CAGL0H05489g.
DR   VEuPathDB; FungiDB:CAGL0H05489g; -.
DR   eggNOG; KOG3976; Eukaryota.
DR   HOGENOM; CLU_077208_0_0_1; -.
DR   InParanoid; Q6FRW0; -.
DR   OMA; IYAISNE; -.
DR   Proteomes; UP000002428; Chromosome H.
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   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:EnsemblFungi.
DR   GO; GO:0065003; P:protein-containing complex assembly; IEA:EnsemblFungi.
DR   InterPro; IPR008688; ATP_synth_Bsub_B/MI25.
DR   InterPro; IPR013837; ATP_synth_F0_suB.
DR   PANTHER; PTHR12733; PTHR12733; 1.
DR   Pfam; PF05405; Mt_ATP-synt_B; 1.
PE   3: Inferred from homology;
KW   CF(0); Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW   Transport.
FT   TRANSIT         1..35
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           36..242
FT                   /note="ATP synthase subunit 4, mitochondrial"
FT                   /id="PRO_0000002519"
SQ   SEQUENCE   242 AA;  26629 MW;  043D343F48BC8A61 CRC64;
     MSFRALTMRS AVARTALNNT IRSARVATPY LGIRHSSSTP TPDPKTKAAS LIDALPGNTA
     LTKTGILGTS AAAIIYGISN QLYVINDESI LLLIFLGFSG LVAKFLAPLY KDFADARIKK
     IGSILNSSRE RHVDAVKDRI ESVSELQNVS ETTKVLFDVS KETVELEAKA FELKQKVELA
     HEAKSVLDSW VRYEASLRQL QQKQIAEGII SKVESELTNP KFQDRVLQQS IAEVEQVLAN
     IK