ID   ATP5E_IPOBA             Reviewed;          70 AA.
AC   Q06450;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=ATP synthase subunit epsilon, mitochondrial;
DE            Short=ATPase subunit epsilon;
OS   Ipomoea batatas (Sweet potato) (Convolvulus batatas).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Convolvulaceae; Ipomoeeae; Ipomoea.
OX   NCBI_TaxID=4120;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Kokei No. 14; TISSUE=Petiole;
RX   PubMed=8349605; DOI=10.1016/s0021-9258(19)85323-1;
RA   Morikami A., Ehara G., Yuuki K., Nakamura K.;
RT   "Molecular cloning and characterization of cDNAs for the gamma- and
RT   epsilon-subunits of mitochondrial F1F0 ATP synthase from the sweet
RT   potato.";
RL   J. Biol. Chem. 268:17205-17210(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-36.
RC   STRAIN=cv. Kokei No. 14; TISSUE=Tuberous root;
RX   PubMed=2536736; DOI=10.1016/s0021-9258(18)94048-2;
RA   Kimura T., Nakamura K., Kajiura H., Hattori H., Nelson N., Asahi T.;
RT   "Correspondence of minor subunits of plant mitochondrial F1ATPase to
RT   F1F0ATPase subunits of other organisms.";
RL   J. Biol. Chem. 264:3183-3186(1989).
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(1) domain and of the central stalk which is part of the complex
CC       rotary element. Rotation of the central stalk against the surrounding
CC       alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate
CC       catalytic sites on the beta subunits.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC       - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC       alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC       subunits: a, b and c.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC   -!- SIMILARITY: Belongs to the eukaryotic ATPase epsilon family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D14700; BAA03527.1; -; mRNA.
DR   PIR; B47493; B47493.
DR   AlphaFoldDB; Q06450; -.
DR   SMR; Q06450; -.
DR   GO; GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1); IEA:InterPro.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR   CDD; cd12153; F1-ATPase_epsilon; 1.
DR   Gene3D; 1.10.1620.20; -; 1.
DR   InterPro; IPR006721; ATP_synth_F1_esu_mt.
DR   InterPro; IPR036742; ATP_synth_F1_esu_sf_mt.
DR   PANTHER; PTHR12448; PTHR12448; 1.
DR   Pfam; PF04627; ATP-synt_Eps; 1.
DR   SUPFAM; SSF48690; SSF48690; 1.
PE   1: Evidence at protein level;
KW   ATP synthesis; CF(1); Direct protein sequencing; Hydrogen ion transport;
KW   Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2536736"
FT   CHAIN           2..70
FT                   /note="ATP synthase subunit epsilon, mitochondrial"
FT                   /id="PRO_0000071669"
FT   CONFLICT        10
FT                   /note="W -> S (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   70 AA;  7928 MW;  5C86EF9FCBB793F6 CRC64;
     MASNAAVPFW RAAGMTYITY SNLCANMVRN CLKEPYRAEA LSREKVHFSF SKWVDGKPQK
     PAIRSDTGEE