ATPE_SPIOL
ID ATPE_SPIOL Reviewed; 134 AA.
AC P00833;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=ATP synthase epsilon chain, chloroplastic {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 Spinacia oleracea (Spinach).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16593238; DOI=10.1073/pnas.79.20.6260;
RA Zurawski G., Bottomley W., Whitfeld P.R.;
RT "Structures of the genes for the beta and epsilon subunits of spinach
RT chloroplast ATPase indicate a dicistronic mRNA and an overlapping
RT translation stop/start signal.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:6260-6264(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Geant d'hiver, and cv. Monatol;
RX PubMed=11292076; DOI=10.1023/a:1006478403810;
RA Schmitz-Linneweber C., Maier R.M., Alcaraz J.-P., Cottet A., Herrmann R.G.,
RA Mache R.;
RT "The plastid chromosome of spinach (Spinacia oleracea): complete nucleotide
RT sequence and gene organization.";
RL Plant Mol. Biol. 45:307-315(2001).
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, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_00530}; Peripheral membrane protein
CC {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; J01441; AAA84627.1; -; Genomic_DNA.
DR EMBL; AJ400848; CAB88735.1; -; Genomic_DNA.
DR PIR; A01034; PWSPE.
DR RefSeq; NP_054942.1; NC_002202.1.
DR PDB; 2RQ7; NMR; -; A=89-134.
DR PDB; 6FKF; EM; 3.10 A; e=1-134.
DR PDB; 6FKH; EM; 4.20 A; e=1-134.
DR PDB; 6FKI; EM; 4.30 A; e=1-134.
DR PDB; 6VM1; EM; 7.90 A; e=1-134.
DR PDB; 6VM4; EM; 7.08 A; e=1-134.
DR PDB; 6VMB; EM; 5.23 A; e=1-134.
DR PDB; 6VMD; EM; 4.53 A; e=1-134.
DR PDB; 6VMG; EM; 6.46 A; e=1-134.
DR PDB; 6VOF; EM; 4.51 A; e=1-134.
DR PDB; 6VOG; EM; 4.35 A; e=1-134.
DR PDB; 6VOH; EM; 4.16 A; e=1-134.
DR PDB; 6VOI; EM; 4.03 A; e=1-134.
DR PDB; 6VOJ; EM; 4.34 A; e=1-134.
DR PDB; 6VOK; EM; 3.85 A; e=1-134.
DR PDB; 6VOL; EM; 4.06 A; e=1-134.
DR PDB; 6VOM; EM; 3.60 A; e=1-134.
DR PDB; 6VON; EM; 3.35 A; e=1-134.
DR PDB; 6VOO; EM; 3.05 A; e=1-134.
DR PDBsum; 2RQ7; -.
DR PDBsum; 6FKF; -.
DR PDBsum; 6FKH; -.
DR PDBsum; 6FKI; -.
DR PDBsum; 6VM1; -.
DR PDBsum; 6VM4; -.
DR PDBsum; 6VMB; -.
DR PDBsum; 6VMD; -.
DR PDBsum; 6VMG; -.
DR PDBsum; 6VOF; -.
DR PDBsum; 6VOG; -.
DR PDBsum; 6VOH; -.
DR PDBsum; 6VOI; -.
DR PDBsum; 6VOJ; -.
DR PDBsum; 6VOK; -.
DR PDBsum; 6VOL; -.
DR PDBsum; 6VOM; -.
DR PDBsum; 6VON; -.
DR PDBsum; 6VOO; -.
DR AlphaFoldDB; P00833; -.
DR SMR; P00833; -.
DR IntAct; P00833; 1.
DR STRING; 3562.P00833; -.
DR ChEMBL; CHEMBL2366567; -.
DR GeneID; 2715577; -.
DR KEGG; soe:2715577; -.
DR OrthoDB; 1438051at2759; -.
DR EvolutionaryTrace; P00833; -.
DR PRO; PR:P00833; -.
DR Proteomes; UP000054095; 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 3D-structure; ATP synthesis; CF(1); Chloroplast; Hydrogen ion transport;
KW Ion transport; Membrane; Plastid; Reference proteome; Thylakoid; Transport.
FT CHAIN 1..134
FT /note="ATP synthase epsilon chain, chloroplastic"
FT /id="PRO_0000188294"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 19..24
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 71..79
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:6FKF"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 91..104
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 109..130
FT /evidence="ECO:0007829|PDB:6FKF"
SQ SEQUENCE 134 AA; 14700 MW; 2C3F0E3E5E60B4C1 CRC64;
MTLNLCVLTP NRSIWNSEVK EIILSTNSGQ IGVLPNHAPT ATAVDIGILR IRLNDQWLTL
ALMGGFARIG NNEITILVND AERGSDIDPQ EAQQTLEIAE ANLRKAEGKR QKIEANLALR
RARTRVEASN TISS
