ID ATPI_ADICA Reviewed; 248 AA. AC Q85FN1; DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2004, sequence version 2. DT 22-FEB-2023, entry version 80. 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 Adiantum capillus-veneris (Maidenhair fern). OG Plastid; Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Polypodiopsida; Polypodiidae; Polypodiales; Pteridineae; Pteridaceae; OC Vittarioideae; Adiantum. OX NCBI_TaxID=13818; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12755170; DOI=10.1093/dnares/10.2.59; RA Wolf P.G., Rowe C.A., Sinclair R.B., Hasebe M.; RT "Complete nucleotide sequence of the chloroplast genome from a RT leptosporangiate fern, Adiantum capillus-veneris L."; RL DNA Res. 10:59-65(2003). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND RNA EDITING. RC TISSUE=Frond; RX PubMed=15363849; DOI=10.1016/j.gene.2004.06.018; RA Wolf P.G., Rowe C.A., Hasebe M.; RT "High levels of RNA editing in a vascular plant chloroplast genome: RT analysis of transcripts from the fern Adiantum capillus-veneris."; RL Gene 339:89-97(2004). 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 -!- RNA EDITING: Modified_positions=14 {ECO:0000269|PubMed:15363849}, 24 CC {ECO:0000269|PubMed:15363849}, 78 {ECO:0000269|PubMed:15363849}, 82 CC {ECO:0000269|PubMed:15363849}, 104 {ECO:0000269|PubMed:15363849}, 149 CC {ECO:0000269|PubMed:15363849}, 162 {ECO:0000269|PubMed:15363849}, 181 CC {ECO:0000269|PubMed:15363849}, 205 {ECO:0000269|PubMed:15363849}, 217 CC {ECO:0000269|PubMed:15363849}; Note=The nonsense codon at position 24 CC is modified to a sense codon.; CC -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000255|HAMAP- CC Rule:MF_01393}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY178864; AAP29380.2; -; Genomic_DNA. DR RefSeq; NP_848048.1; NC_004766.1. DR AlphaFoldDB; Q85FN1; -. DR SMR; Q85FN1; -. DR GeneID; 807428; -. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. 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 CDD; cd00310; ATP-synt_Fo_a_6; 1. DR Gene3D; 1.20.120.220; ATP synthase, F0 complex, subunit A; 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; ATP SYNTHASE SUBUNIT A, CHLOROPLASTIC; 1. DR PANTHER; PTHR42823:SF3; ATP SYNTHASE SUBUNIT A, CHLOROPLASTIC; 1. DR Pfam; PF00119; ATP-synt_A; 1. DR PRINTS; PR00123; ATPASEA. DR SUPFAM; SSF81336; F1F0 ATP synthase subunit A; 1. DR TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 1. DR PROSITE; PS00449; ATPASE_A; 1. PE 2: Evidence at transcript level; KW ATP synthesis; CF(0); Chloroplast; Hydrogen ion transport; Ion transport; KW Membrane; Plastid; RNA editing; Thylakoid; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..248 FT /note="ATP synthase subunit a, chloroplastic" FT /id="PRO_0000002575" 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; 27566 MW; 1E901EB7E4078F53 CRC64; MQIEQLQINE IDNLHQVSSV EVGQHLYWQI GNFQVHAQVL ITSWVVVAIL VALPATTTGN LQSIPTGTQN FIEYVLEFIR DLTRTQMGEE GYRPWVPFIG TMFLFIFASN WSGALLPWRV IQLPHGELAA PTNDINTTVA LALLTSVAYF YAGLYKRGFS YFGKYIQPTP ILLPINILED FTKPLSLSFR LFGNILADEL VVAVLVSLVP LIVPVPMMLL GLFTSGIQAL IFATLAAAYI GESMEGHH //