ATPE_BIGNA
ID ATPE_BIGNA Reviewed; 137 AA.
AC Q06J28;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 61.
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 Bigelowiella natans (Pedinomonas minutissima) (Chlorarachnion sp. (strain
OS CCMP621)).
OG Plastid; Chloroplast.
OC Eukaryota; Sar; Rhizaria; Cercozoa; Chlorarachniophyceae; Bigelowiella.
OX NCBI_TaxID=227086;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16990439; DOI=10.1093/molbev/msl129;
RA Rogers M.B., Gilson P.R., Su V., McFadden G.I., Keeling P.J.;
RT "The complete chloroplast genome of the chlorarachniophyte Bigelowiella
RT natans: evidence for independent origins of chlorarachniophyte and euglenid
RT secondary endosymbionts.";
RL Mol. Biol. Evol. 24:54-62(2007).
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; DQ851108; ABG91431.1; -; Genomic_DNA.
DR RefSeq; YP_778599.1; NC_008408.1.
DR AlphaFoldDB; Q06J28; -.
DR SMR; Q06J28; -.
DR GeneID; 4353016; -.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
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 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); Chloroplast; Hydrogen ion transport; Ion transport;
KW Membrane; Plastid; Thylakoid; Transport.
FT CHAIN 1..137
FT /note="ATP synthase epsilon chain, chloroplastic"
FT /id="PRO_0000295908"
SQ SEQUENCE 137 AA; 15472 MW; D346082552871D1A CRC64;
MKLKVKIAIP GKVVWENEVD EVNIQTTTGK IGILPNHAPI IATVETSVLR MKSDESQNPI
LMVISDGYLS LEKNSIFIAT DRCILEDNIN ASKLEEDYKT ALERYNNAEK PGKKYIANKA
LKRINACYEI LSYRNND