ATPI_AMBTC
ID ATPI_AMBTC Reviewed; 248 AA.
AC Q70XU8;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=ATP synthase subunit a, chloroplastic {ECO:0000255|HAMAP-Rule:MF_01393};
DE AltName: Full=ATP synthase F0 sector subunit a {ECO:0000255|HAMAP-Rule:MF_01393};
DE AltName: Full=F-ATPase subunit IV {ECO:0000255|HAMAP-Rule:MF_01393};
GN Name=atpI {ECO:0000255|HAMAP-Rule:MF_01393};
OS Amborella trichopoda.
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX NCBI_TaxID=13333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12832641; DOI=10.1093/molbev/msg159;
RA Goremykin V.V., Hirsch-Ernst K.I., Wolfl S., Hellwig F.H.;
RT "Analysis of the Amborella trichopoda chloroplast genome sequence suggests
RT that Amborella is not a basal angiosperm.";
RL Mol. Biol. Evol. 20:1499-1505(2003).
CC -!- FUNCTION: Key component of the proton channel; it plays a direct role
CC in the translocation of protons across the membrane.
CC {ECO:0000255|HAMAP-Rule:MF_01393}.
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 four main
CC subunits: a, b, b' and c. {ECO:0000255|HAMAP-Rule:MF_01393}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_01393}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01393}.
CC -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000255|HAMAP-
CC Rule:MF_01393}.
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DR EMBL; AJ506156; CAD56283.1; -; Genomic_DNA.
DR RefSeq; NP_904087.1; NC_005086.1.
DR AlphaFoldDB; Q70XU8; -.
DR SMR; Q70XU8; -.
DR STRING; 13333.ERN02618; -.
DR GeneID; 2546507; -.
DR KEGG; atr:2546507; -.
DR eggNOG; KOG0832; Eukaryota.
DR eggNOG; KOG4665; Eukaryota.
DR OrthoDB; 1136313at2759; -.
DR Proteomes; UP000017836; Chloroplast.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.120.220; -; 1.
DR HAMAP; MF_01393; ATP_synth_a_bact; 1.
DR InterPro; IPR045082; ATP_syn_F0_a_bact/chloroplast.
DR InterPro; IPR000568; ATP_synth_F0_asu.
DR InterPro; IPR023011; ATP_synth_F0_asu_AS.
DR InterPro; IPR035908; F0_ATP_A_sf.
DR PANTHER; PTHR42823; PTHR42823; 1.
DR Pfam; PF00119; ATP-synt_A; 1.
DR PRINTS; PR00123; ATPASEA.
DR SUPFAM; SSF81336; SSF81336; 1.
DR TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 1.
DR PROSITE; PS00449; ATPASE_A; 1.
PE 3: Inferred from homology;
KW ATP synthesis; CF(0); Chloroplast; Hydrogen ion transport; Ion transport;
KW Membrane; Plastid; Reference proteome; Thylakoid; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..248
FT /note="ATP synthase subunit a, chloroplastic"
FT /id="PRO_0000362528"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
SQ SEQUENCE 248 AA; 27197 MW; 977A16FEEBE93F1E CRC64;
MSVLPCSINT LKGIYDLSGV EVGQHFYWQI GGFQVHAQVL ITSWVVIAIL LGSATIVVRN
PQTIPTDGQN FFEYVLEFIR DLTKTQIGEE EYGPWVPFIG TMFLFIFVSN WSGALLPRKI
IELPQGELAA PTNDINTTVA LALPTSVAYF YAGISKKGLG YFGKYIQPTP ILLPINILED
FTKPLSLSFR LFGNILADEL VVVVLVSLVP SLVPIPVMFL GLFTSGIQAL IFATLAAAYI
GESMEGHH