ATPJ_YARLI
ID ATPJ_YARLI Reviewed; 90 AA.
AC B5FVG3;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=ATP synthase subunit e, mitochondrial {ECO:0000250|UniProtKB:P81449};
DE Short=ATPase subunit e {ECO:0000250|UniProtKB:P81449};
DE AltName: Full=Translocase of the inner membrane protein 11 {ECO:0000250|UniProtKB:P81449};
GN Name=TIM11 {ECO:0000250|UniProtKB:P81449};
GN Synonyms=ATP21 {ECO:0000250|UniProtKB:P81449};
GN OrderedLocusNames=YALI0_E32164g {ECO:0000312|EMBL:CAR64348.1};
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 PROTEIN SEQUENCE OF 2-9, IDENTIFICATION IN ATP SYNTHASE COMPLEX, FUNCTION
RP OF ATP SYNTHASE COMPLEX, SUBUNIT, SUBCELLULAR LOCATION, MASS SPECTROMETRY,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
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, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND ACETYLATION AT SER-2.
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). Together with
CC subunit g/ATP20, probably contributes to membrane curvature at the site
CC of the ATP synthase dimer, ultimately contributing to formation of
CC cristae (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:27373333}; 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 -!- MASS SPECTROMETRY: Mass=9900.5; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:25759169};
CC -!- SIMILARITY: Belongs to the ATPase e subunit family. {ECO:0000305}.
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DR EMBL; CR382131; CAR64348.1; -; Genomic_DNA.
DR RefSeq; XP_002143092.1; XM_002143056.1.
DR AlphaFoldDB; B5FVG3; -.
DR SMR; B5FVG3; -.
DR STRING; 4952.CAR64348; -.
DR iPTMnet; B5FVG3; -.
DR EnsemblFungi; CAR64348; CAR64348; YALI0_E32164g.
DR GeneID; 7009589; -.
DR KEGG; yli:YALI0E32164g; -.
DR VEuPathDB; FungiDB:YALI0_E32164g; -.
DR HOGENOM; CLU_159435_2_0_1; -.
DR InParanoid; B5FVG3; -.
DR OMA; FYGLYHQ; -.
DR Proteomes; UP000001300; Chromosome E.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IBA:GO_Central.
DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IEA:InterPro.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEA:InterPro.
DR InterPro; IPR008386; ATP_synth_F0_esu_mt.
DR PANTHER; PTHR12427; PTHR12427; 1.
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; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:27373333"
FT CHAIN 2..90
FT /note="ATP synthase subunit e, mitochondrial"
FT /evidence="ECO:0000305"
FT /id="PRO_0000445320"
FT TRANSMEM 7..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:27373333"
SQ SEQUENCE 90 AA; 9989 MW; 458F66D3B87037FC CRC64;
MSATLNVLRW SALGAGVVYG FVHNRTLYSQ AEKKVADAKF KKQEKLIEQA KAEWARLHPA
PVASTGVVTD ISDDKFDIEA YLNHAFPEKA
