ID   ATP19_YARLI             Reviewed;          70 AA.
AC   B5FVB3;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=ATP synthase subunit K, mitochondrial {ECO:0000250|UniProtKB:P81451};
GN   Name=ATP19 {ECO:0000250|UniProtKB:P81451};
GN   OrderedLocusNames=YALI0_B11913g {ECO:0000312|EMBL:CAR64284.1};
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591 {ECO:0000312|Proteomes:UP000001300};
RN   [1] {ECO:0000312|Proteomes:UP000001300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
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).
RN   [2] {ECO:0000305}
RP   FUNCTION OF ATP SYNTHASE COMPLEX, AND SUBUNIT.
RC   STRAIN=CLIB 122 / E 150 {ECO:0000303|PubMed:25759169};
RX   PubMed=25759169; DOI=10.1042/bj20150197;
RA   Liu S., Charlesworth T.J., Bason J.V., Montgomery M.G., Harbour M.E.,
RA   Fearnley I.M., Walker J.E.;
RT   "The purification and characterization of ATP synthase complexes from the
RT   mitochondria of four fungal species.";
RL   Biochem. J. 468:167-175(2015).
RN   [3] {ECO:0000305}
RP   STRUCTURE BY ELECTRON MICROSCOPY (7.7 ANGSTROMS) OF DIMERIC ATP SYNTHASE
RP   COMPLEX, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=27373333; DOI=10.1016/j.molcel.2016.05.037;
RA   Hahn A., Parey K., Bublitz M., Mills D.J., Zickermann V., Vonck J.,
RA   Kuehlbrandt W., Meier T.;
RT   "Structure of a Complete ATP Synthase Dimer Reveals the Molecular Basis of
RT   Inner Mitochondrial Membrane Morphology.";
RL   Mol. Cell 63:445-456(2016).
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 (PubMed:25759169). F-type ATP synthases
CC       consist of two structural domains, F(1) - containing the
CC       extramembraneous catalytic core, and F(0) - containing the membrane
CC       proton channel, linked together by a central stalk and a peripheral
CC       stalk (PubMed:27373333). 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 (PubMed:27373333). Part
CC       of the complex F(0) domain (PubMed:27373333). Minor subunit located
CC       with subunit a/ATP6 in the membrane (PubMed:27373333). The K/ATP19
CC       chain binds the dimeric form by interacting with the G/ATP20 and
CC       E/TIM11 chains (PubMed:27373333). {ECO:0000269|PubMed:25759169,
CC       ECO:0000269|PubMed:27373333}.
CC   -!- SUBUNIT: F-type ATP synthases have 2 components, the catalytic core
CC       F(1) and the membrane-embedded component F(0), linked together by a
CC       central stalk and a peripheral stalk (PubMed:27373333). The central
CC       stalk, also called rotor shaft, is often seen as part of F(1)
CC       (PubMed:27373333). The peripheral stalk is seen as part of F(0)
CC       (PubMed:27373333). F(0) contains the membrane channel next to the rotor
CC       (PubMed:27373333). F-type ATP synthases form dimers but each monomer
CC       functions independently in ATP generation (PubMed:27373333). The dimer
CC       consists of 17 different polypeptides: ATP1 (subunit alpha, 3 molecules
CC       per monomer, part of F(1)), ATP2 (subunit beta, 3 copies per monomer,
CC       part of F(1)), ATP3 (subunit gamma, part of the central stalk), ATP4
CC       (subunit b, part of the peripheral stalk), ATP5/OSCP (subunit 5/OSCP,
CC       part of the peripheral stalk), ATP6 (subunit a, part of the peripheral
CC       stalk), ATP7 (subunit d, part of the peripheral stalk), ATP8 (subunit
CC       8, part of the peripheral stalk), OLI1 (subunit c, part of the rotor,
CC       10 molecules per monomer), ATP14 (subunit h, part of the peripheral
CC       stalk), ATP15 (subunit epsilon, part of the central stalk), ATP16
CC       (subunit delta, part of the central stalk), ATP17 (subunit f, part of
CC       the peripheral stalk), ATP18 (subunit i/j, part of the peripheral
CC       stalk), ATP19 (subunit k, dimer-specific, at interface between
CC       monomers), ATP20 (subunit g, at interface between monomers), TIM11
CC       (subunit e, at interface between monomers) (PubMed:27373333,
CC       PubMed:25759169). {ECO:0000269|PubMed:25759169,
CC       ECO:0000269|PubMed:27373333}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000305|PubMed:25759169}; Single-pass membrane protein
CC       {ECO:0000255}. Note=The F-type ATP synthase complex is anchored in the
CC       mitochondrial inner membrane via the F(0) domain with the F(1) domain
CC       and the peripheral stalk extending into the mitochondrial matrix.
CC       {ECO:0000305|PubMed:27373333}.
CC   -!- SIMILARITY: Belongs to the ATP19 family. {ECO:0000305}.
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DR   EMBL; CR382128; CAR64284.1; -; Genomic_DNA.
DR   RefSeq; XP_002143014.1; XM_002142978.1.
DR   AlphaFoldDB; B5FVB3; -.
DR   STRING; 4952.CAR64284; -.
DR   EnsemblFungi; CAR64284; CAR64284; YALI0_B11913g.
DR   GeneID; 7009411; -.
DR   KEGG; yli:YALI0B11913g; -.
DR   VEuPathDB; FungiDB:YALI0_B11913g; -.
DR   HOGENOM; CLU_172736_1_2_1; -.
DR   InParanoid; B5FVB3; -.
DR   OMA; YVAYSMK; -.
DR   Proteomes; UP000001300; Chromosome B.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IBA:GO_Central.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0065003; P:protein-containing complex assembly; IEA:EnsemblFungi.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR   InterPro; IPR021278; ATP19.
DR   PANTHER; PTHR28074; PTHR28074; 1.
DR   Pfam; PF11022; ATP19; 1.
PE   1: Evidence at protein level;
KW   ATP synthesis; CF(0); Hydrogen ion transport; Ion transport; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..70
FT                   /note="ATP synthase subunit K, mitochondrial"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000445306"
FT   TRANSMEM        15..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   70 AA;  7266 MW;  AE8DDEBE3A607E42 CRC64;
     MGAAYHILGK TVYPHQLAIG TIVSVVGGIV IASSGKKAEK PAAPAIQAGS SDEEKFIANF
     LKEQEAAEKK