ID   ATPJ_SCHPO              Reviewed;          92 AA.
AC   Q9URV6;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 3.
DT   24-JAN-2024, entry version 101.
DE   RecName: Full=ATP synthase subunit e, mitochondrial;
DE            Short=ATPase subunit e;
DE   AltName: Full=Translocase of the inner membrane protein 11;
GN   Name=tim11; ORFNames=SPBC106.05c;
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).
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. Minor subunit located with subunit a in the membrane (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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATPase e subunit family. {ECO:0000305}.
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DR   EMBL; CU329671; CAB53721.3; -; Genomic_DNA.
DR   PIR; T39262; T39262.
DR   RefSeq; NP_595154.3; NM_001021063.3.
DR   AlphaFoldDB; Q9URV6; -.
DR   BioGRID; 276601; 3.
DR   STRING; 284812.Q9URV6; -.
DR   iPTMnet; Q9URV6; -.
DR   MaxQB; Q9URV6; -.
DR   PaxDb; 4896-SPBC106-05c-1; -.
DR   EnsemblFungi; SPBC106.05c.1; SPBC106.05c.1:pep; SPBC106.05c.
DR   GeneID; 2540063; -.
DR   KEGG; spo:SPBC106.05c; -.
DR   PomBase; SPBC106.05c; tim11.
DR   VEuPathDB; FungiDB:SPBC106.05c; -.
DR   HOGENOM; CLU_159435_2_0_1; -.
DR   InParanoid; Q9URV6; -.
DR   OMA; RSHAKCE; -.
DR   PRO; PR:Q9URV6; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); ISO:PomBase.
DR   GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; ISO:PomBase.
DR   GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; ISO:PomBase.
DR   InterPro; IPR008386; ATP_synth_F0_esu_mt.
DR   Pfam; PF05680; ATP-synt_E; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; CF(0); Hydrogen ion transport; Ion transport; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Reference proteome; Transport.
FT   CHAIN           1..92
FT                   /note="ATP synthase subunit e, mitochondrial"
FT                   /id="PRO_0000116513"
SQ   SEQUENCE   92 AA;  10711 MW;  295F5A6EA7A3E3A7 CRC64;
     MNSINVKTLR WSALVLGLGA GMYEHRSHIQ CQKQKEIDEN YHRQESLIES AKIAYLNTKN
     TPPKEDSMLP NLKKDSEDFD MDEFVKELEK NV
//