ID Q8M983_PLOBU Unreviewed; 132 AA.
AC Q8M983;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=ATP synthase epsilon chain, chloroplastic {ECO:0000256|RuleBase:RU003655};
DE Flags: Fragment;
GN Name=atpE {ECO:0000313|EMBL:CAD23933.1};
OS Plocosperma buxifolium.
OG Plastid; Chloroplast {ECO:0000313|EMBL:CAD23933.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Plocospermataceae; Plocosperma.
OX NCBI_TaxID=62094 {ECO:0000313|EMBL:CAD23933.1};
RN [1] {ECO:0000313|EMBL:CAD23933.1}
RP NUCLEOTIDE SEQUENCE.
RA Bremer B., Bremer K., Heidari N., Erixon P., Olmstead R.G., Anderberg A.A.,
RA Kallersjo M., Barkhordarian E.;
RT "Phylogenetics of asterids based on 3 coding and 3 non-coding chloroplast
RT DNA markers and the utility of non-coding DNA at higher taxonomic levels.";
RL Mol. Phylogenet. Evol. 24:273-300(2002).
RN [2] {ECO:0000313|EMBL:CAD23933.1}
RP NUCLEOTIDE SEQUENCE.
RA Lundberg J.;
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. {ECO:0000256|RuleBase:RU003655}.
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:0000256|RuleBase:RU003655}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the ATPase epsilon chain family.
CC {ECO:0000256|ARBA:ARBA00005712, ECO:0000256|RuleBase:RU003655}.
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DR EMBL; AJ429670; CAD23933.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8M983; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR GO; GO:0009579; C:thylakoid; 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; 6.10.140.480; -; 1.
DR Gene3D; 2.60.15.10; F0F1 ATP synthase delta/epsilon subunit, N-terminal; 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; IPR020547; ATP_synth_F1_esu_C.
DR InterPro; IPR036771; ATPsynth_dsu/esu_N.
DR NCBIfam; TIGR01216; ATP_synt_epsi; 1.
DR PANTHER; PTHR13822; ATP SYNTHASE DELTA/EPSILON CHAIN; 1.
DR PANTHER; PTHR13822:SF10; ATP SYNTHASE EPSILON CHAIN, CHLOROPLASTIC; 1.
DR Pfam; PF00401; ATP-synt_DE; 1.
DR Pfam; PF02823; ATP-synt_DE_N; 1.
DR SUPFAM; SSF51344; Epsilon subunit of F1F0-ATP synthase N-terminal domain; 1.
PE 3: Inferred from homology;
KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310,
KW ECO:0000256|RuleBase:RU003655};
KW CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|RuleBase:RU003655};
KW Chloroplast {ECO:0000313|EMBL:CAD23933.1};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrogen ion transport {ECO:0000256|RuleBase:RU003655};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU003655};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU003655};
KW Plastid {ECO:0000256|RuleBase:RU003655};
KW Thylakoid {ECO:0000256|ARBA:ARBA00023078, ECO:0000256|RuleBase:RU003655};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003655}.
FT DOMAIN 2..80
FT /note="ATP synthase F1 complex delta/epsilon subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02823"
FT DOMAIN 85..128
FT /note="ATP synthase epsilon subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00401"
FT COILED 88..115
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAD23933.1"
SQ SEQUENCE 132 AA; 14451 MW; 8EB08A3F0699C5B0 CRC64;
TLNLCVLTPN RIVWDSEVKE IILSTNSGQI GVLPNHAPIA TAVDIGILRI RLNDQWLTMA
LMGGFARIGN NEITVLVNDA EKGSDIDPQE AEQTLEIAEA NLRKAEGKRQ IIEANLALRR
ARTRVEAVNA IS
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