ID   ATPJ_YEAST              Reviewed;          96 AA.
AC   P81449; D6VSV5;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 166.
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; Synonyms=ATP21; OrderedLocusNames=YDR322C-A; ORFNames=YDR322BC;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [4]
RP   IDENTIFICATION, PROTEIN SEQUENCE OF 2-14, CLEAVAGE OF INITIATOR METHIONINE,
RP   AND ACETYLATION AT SER-2.
RC   STRAIN=ATCC 208353 / W303-1A;
RX   PubMed=9857174; DOI=10.1093/emboj/17.24.7170;
RA   Arnold I., Pfeiffer K., Neupert W., Stuart R.A., Schaegger H.;
RT   "Yeast mitochondrial F1F0-ATPase exists as a dimer: identification of three
RT   dimer-specific subunits.";
RL   EMBO J. 17:7170-7178(1998).
RN   [5]
RP   IDENTIFICATION.
RX   PubMed=9271204; DOI=10.1016/s0014-5793(97)00691-1;
RA   Arnold I., Bauer M.F., Brunner M., Neupert W., Stuart R.A.;
RT   "Yeast mitochondrial F1F0-ATPase: the novel subunit e is identical to
RT   Tim11.";
RL   FEBS Lett. 411:195-200(1997).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
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.
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.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC   -!- MISCELLANEOUS: Present with 4590 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the ATPase e subunit family. {ECO:0000305}.
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DR   EMBL; U32517; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AY557720; AAS56046.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA12165.1; -; Genomic_DNA.
DR   PIR; S78713; S78713.
DR   RefSeq; NP_010609.1; NM_001184348.1.
DR   AlphaFoldDB; P81449; -.
DR   SMR; P81449; -.
DR   BioGRID; 32380; 61.
DR   ComplexPortal; CPX-3281; Mitochondrial proton-transporting ATP synthase complex.
DR   DIP; DIP-3029N; -.
DR   MINT; P81449; -.
DR   STRING; 4932.YDR322C-A; -.
DR   iPTMnet; P81449; -.
DR   MaxQB; P81449; -.
DR   PaxDb; P81449; -.
DR   PRIDE; P81449; -.
DR   EnsemblFungi; YDR322C-A_mRNA; YDR322C-A; YDR322C-A.
DR   GeneID; 851922; -.
DR   KEGG; sce:YDR322C-A; -.
DR   SGD; S000007255; TIM11.
DR   VEuPathDB; FungiDB:YDR322C-A; -.
DR   eggNOG; ENOG502SDS3; Eukaryota.
DR   HOGENOM; CLU_159435_1_0_1; -.
DR   InParanoid; P81449; -.
DR   OMA; WARDHPS; -.
DR   BioCyc; YEAST:G3O-30090-MON; -.
DR   PRO; PR:P81449; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; P81449; protein.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR   GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IC:ComplexPortal.
DR   GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IMP:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IMP:SGD.
DR   GO; GO:0042407; P:cristae formation; IMP:SGD.
DR   GO; GO:0065003; P:protein-containing complex assembly; IMP:SGD.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; IDA:SGD.
DR   InterPro; IPR008386; ATP_synth_F0_esu_mt.
DR   Pfam; PF05680; ATP-synt_E; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP synthesis; CF(0); Direct protein sequencing;
KW   Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9857174"
FT   CHAIN           2..96
FT                   /note="ATP synthase subunit e, mitochondrial"
FT                   /id="PRO_0000071689"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:9857174"
SQ   SEQUENCE   96 AA;  10876 MW;  3A41A5F53EA75E98 CRC64;
     MSTVNVLRYS ALGLGLFFGF RNDMILKCNA KKKEEQAQYE EKLKLVEEAK KEYAKLHPVV
     TPKDVPANAS FNLEDPNIDF ERVILNAVES LKEAST