ID   ATP19_SCHPO             Reviewed;          68 AA.
AC   C6Y4A3;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=ATP synthase subunit K, mitochondrial;
GN   Name=atp19; ORFNames=SPAC25H1.10c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   IDENTIFICATION.
RX   PubMed=18488015; DOI=10.1038/nature07002;
RA   Wilhelm B.T., Marguerat S., Watt S., Schubert F., Wood V., Goodhead I.,
RA   Penkett C.J., Rogers J., Baehler J.;
RT   "Dynamic repertoire of a eukaryotic transcriptome surveyed at single-
RT   nucleotide resolution.";
RL   Nature 453:1239-1243(2008).
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. Minor subunit located with subunit a in the membrane. The
CC       K chain binds the dimeric form by interacting with the G and E chains
CC       (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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATP19 family. {ECO:0000305}.
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DR   EMBL; CU329670; CBA11499.1; -; Genomic_DNA.
DR   RefSeq; XP_002742508.1; XM_002742462.2.
DR   AlphaFoldDB; C6Y4A3; -.
DR   STRING; 4896.SPAC25H1.10c.1; -.
DR   iPTMnet; C6Y4A3; -.
DR   MaxQB; C6Y4A3; -.
DR   PaxDb; C6Y4A3; -.
DR   PRIDE; C6Y4A3; -.
DR   EnsemblFungi; SPAC25H1.10c.1; SPAC25H1.10c.1:pep; SPAC25H1.10c.
DR   PomBase; SPAC25H1.10c; atp19.
DR   VEuPathDB; FungiDB:SPAC25H1.10c; -.
DR   eggNOG; ENOG502RDPM; Eukaryota.
DR   HOGENOM; CLU_172736_1_0_1; -.
DR   InParanoid; C6Y4A3; -.
DR   OMA; MSVYTIA; -.
DR   PRO; PR:C6Y4A3; -.
DR   Proteomes; UP000002485; Chromosome I.
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); ISO:PomBase.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR   GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; ISO:PomBase.
DR   InterPro; IPR021278; ATP19.
DR   PANTHER; PTHR28074; PTHR28074; 1.
DR   Pfam; PF11022; ATP19; 1.
PE   2: Evidence at transcript 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..68
FT                   /note="ATP synthase subunit K, mitochondrial"
FT                   /id="PRO_0000389140"
FT   TRANSMEM        13..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   68 AA;  7720 MW;  1DCF3AA79C033258 CRC64;
     MSVYTIAGRQ FQAHQLSLAV LGSVFVGPVI YSKLFKRNKP LSAKDVPPLN AKSKEEEEFI
     LKYIEEHK