ID   ATPE_PROWI              Reviewed;         134 AA.
AC   Q9TJR8;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=ATP synthase epsilon chain, plastid {ECO:0000255|HAMAP-Rule:MF_00530};
DE   AltName: Full=ATP synthase F1 sector epsilon subunit {ECO:0000255|HAMAP-Rule:MF_00530};
DE   AltName: Full=F-ATPase epsilon subunit {ECO:0000255|HAMAP-Rule:MF_00530};
GN   Name=atpE {ECO:0000255|HAMAP-Rule:MF_00530};
OS   Prototheca wickerhamii.
OG   Plastid; Non-photosynthetic plastid.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Prototheca.
OX   NCBI_TaxID=3111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=263-11;
RX   PubMed=12111556; DOI=10.1007/s00438-002-0681-6;
RA   Knauf U., Hachtel W.;
RT   "The genes encoding subunits of ATP synthase are conserved in the reduced
RT   plastid genome of the heterotrophic alga Prototheca wickerhamii.";
RL   Mol. Genet. Genomics 267:492-497(2002).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. {ECO:0000255|HAMAP-Rule:MF_00530}.
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. {ECO:0000255|HAMAP-Rule:MF_00530}.
CC   -!- SUBCELLULAR LOCATION: Plastid membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000255|HAMAP-Rule:MF_00530}.
CC   -!- SIMILARITY: Belongs to the ATPase epsilon chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_00530}.
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DR   EMBL; AJ245645; CAB53103.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9TJR8; -.
DR   SMR; Q9TJR8; -.
DR   GO; GO:0042170; C:plastid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR   CDD; cd12152; F1-ATPase_delta; 1.
DR   Gene3D; 2.60.15.10; -; 1.
DR   HAMAP; MF_00530; ATP_synth_epsil_bac; 1.
DR   InterPro; IPR001469; ATP_synth_F1_dsu/esu.
DR   InterPro; IPR020546; ATP_synth_F1_dsu/esu_N.
DR   InterPro; IPR036771; ATPsynth_dsu/esu_N.
DR   PANTHER; PTHR13822; PTHR13822; 1.
DR   Pfam; PF02823; ATP-synt_DE_N; 1.
DR   SUPFAM; SSF51344; SSF51344; 1.
DR   TIGRFAMs; TIGR01216; ATP_synt_epsi; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; CF(1); Hydrogen ion transport; Ion transport; Membrane;
KW   Plastid; Transport.
FT   CHAIN           1..134
FT                   /note="ATP synthase epsilon chain, plastid"
FT                   /id="PRO_0000188289"
SQ   SEQUENCE   134 AA;  14810 MW;  2410E049A5258E8C CRC64;
     MILKILIMIP DGIFWNNKAE EIILPTNTGQ IGILKNHAPL ITALDIGVIL IRTDKKWVPF
     IIMGGFALIK QNKITILVNG AESAGTLKLV QSEAAFQEAT NKLENAKSKK QYVDALFLFK
     CAKARYQAAK QLVS