ID   ATPE_CHLRE              Reviewed;         141 AA.
AC   P07891; B7U1G5; Q9T2G5;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=ATP synthase epsilon chain, chloroplastic {ECO:0000255|HAMAP-Rule:MF_00530, ECO:0000303|PubMed:8543042};
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, ECO:0000303|Ref.1};
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Woessner J.P., Gillham N.W., Boynton J.E.;
RT   "Chloroplast genes encoding subunits of the H(+)-ATPase complex of
RT   Chlamydomonas reinhardtii are rearranged compared to higher plants:
RT   sequence of the atpE gene and location of the atpF and atpI genes.";
RL   Plant Mol. Biol. 8:151-158(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2196429; DOI=10.1007/bf00261715;
RA   Robertson D., Boynton J.E., Gillham N.W.;
RT   "Cotranscription of the wild-type chloroplast atpE gene encoding the
RT   CF1/CF0 epsilon subunit with the 3' half of the rps7 gene in Chlamydomonas
RT   reinhardtii and characterization of frameshift mutations in atpE.";
RL   Mol. Gen. Genet. 221:155-163(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC-503;
RX   PubMed=19473533; DOI=10.1186/1471-2148-9-120;
RA   Smith D.R., Lee R.W.;
RT   "Nucleotide diversity of the Chlamydomonas reinhardtii plastid genome:
RT   addressing the mutational-hazard hypothesis.";
RL   BMC Evol. Biol. 9:120-120(2009).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-26, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=cw15;
RX   PubMed=8543042; DOI=10.1016/0014-5793(95)01332-6;
RA   Fiedler H.R., Schmid R., Leu S., Shavit N., Strotmann H.;
RT   "Isolation of CF0CF1 from Chlamydomonas reinhardtii cw15 and the N-terminal
RT   amino acid sequences of the CF0CF1 subunits.";
RL   FEBS Lett. 377:163-166(1995).
RN   [5]
RP   IDENTIFICATION, AND COMPLETE PLASTID GENOME.
RX   PubMed=12417694; DOI=10.1105/tpc.006155;
RA   Maul J.E., Lilly J.W., Cui L., dePamphilis C.W., Miller W., Harris E.H.,
RA   Stern D.B.;
RT   "The Chlamydomonas reinhardtii plastid chromosome: islands of genes in a
RT   sea of repeats.";
RL   Plant Cell 14:2659-2679(2002).
CC   -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence
CC       of a proton or sodium gradient. F-type ATPases consist of two
CC       structural domains, F(1) containing the extramembraneous catalytic core
CC       and 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.
CC       {ECO:0000269|PubMed:8543042}.
CC   -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic core
CC       - and F(0) - the membrane proton channel. F(1) has five subunits:
CC       alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has four main
CC       subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains
CC       form an alternating ring which encloses part of the gamma chain. F(1)
CC       is attached to F(0) by a central stalk formed by the gamma and epsilon
CC       chains, while a peripheral stalk is formed by the delta, b and b'
CC       chains. {ECO:0000269|PubMed:8543042}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000255|HAMAP-Rule:MF_00530, ECO:0000269|PubMed:8543042};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00530}.
CC   -!- MISCELLANEOUS: In plastids the F-type ATPase is also known as
CC       CF(1)CF(0). {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ATPase epsilon chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_00530}.
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DR   EMBL; M17168; AAA84147.1; -; Genomic_DNA.
DR   EMBL; X53977; CAA37928.1; -; Genomic_DNA.
DR   EMBL; FJ423446; ACJ50112.1; -; Genomic_DNA.
DR   EMBL; FJ436948; ACK37280.1; -; Genomic_DNA.
DR   EMBL; FJ436949; ACK37281.1; -; Genomic_DNA.
DR   EMBL; BK000554; DAA00924.1; -; Genomic_DNA.
DR   PIR; S11898; PWKME.
DR   RefSeq; NP_958379.1; NC_005353.1.
DR   AlphaFoldDB; P07891; -.
DR   SMR; P07891; -.
DR   STRING; 3055.DAA00924; -.
DR   PaxDb; P07891; -.
DR   PRIDE; P07891; -.
DR   ProMEX; P07891; -.
DR   GeneID; 2716972; -.
DR   KEGG; cre:ChreCp023; -.
DR   eggNOG; KOG1758; Eukaryota.
DR   HOGENOM; CLU_084338_1_2_1; -.
DR   InParanoid; P07891; -.
DR   OrthoDB; 1438051at2759; -.
DR   Proteomes; UP000006906; Chloroplast.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1); IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
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; IPR020547; ATP_synth_F1_dsu/esu_C.
DR   InterPro; IPR020546; ATP_synth_F1_dsu/esu_N.
DR   InterPro; IPR036771; ATPsynth_dsu/esu_N.
DR   PANTHER; PTHR13822; PTHR13822; 1.
DR   Pfam; PF00401; ATP-synt_DE; 1.
DR   Pfam; PF02823; ATP-synt_DE_N; 1.
DR   SUPFAM; SSF51344; SSF51344; 1.
DR   TIGRFAMs; TIGR01216; ATP_synt_epsi; 1.
PE   1: Evidence at protein level;
KW   ATP synthesis; CF(1); Chloroplast; Direct protein sequencing;
KW   Hydrogen ion transport; Ion transport; Membrane; Plastid;
KW   Reference proteome; Thylakoid; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8543042"
FT   CHAIN           2..141
FT                   /note="ATP synthase epsilon chain, chloroplastic"
FT                   /id="PRO_0000188258"
FT   VARIANT         45
FT                   /note="N -> D (in strain: CC-2290 / S1 D2 and CC-503)"
FT   CONFLICT        120
FT                   /note="E -> V (in Ref. 1; AAA84147)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   141 AA;  15374 MW;  0CBB22F21FD622C1 CRC64;
     MSLQISILTP ERPFWNGQAD EIILPTETGE MGVLKNHAPI ITGLNVGAML IRGGQASGSK
     DEWNSYAIMG GFALVKQNQV TILANEAVSA ENINPEEAKD AFETAKANLE KAEGVKEKVE
     ANFAYKRAKA RYQVVKVLKK I