ID   ATPI_PAUCH              Reviewed;         242 AA.
AC   B1X3Y1;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=ATP synthase subunit a, organellar chromatophore {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}; OrderedLocusNames=PCC_0200;
OS   Paulinella chromatophora.
OG   Plastid; Organellar chromatophore.
OC   Eukaryota; Sar; Rhizaria; Imbricatea; Silicofilosea; Euglyphida;
OC   Paulinellidae; Paulinella.
OX   NCBI_TaxID=39717;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18356055; DOI=10.1016/j.cub.2008.02.051;
RA   Nowack E.C.M., Melkonian M., Gloeckner G.;
RT   "Chromatophore genome sequence of Paulinella sheds light on acquisition of
RT   photosynthesis by eukaryotes.";
RL   Curr. Biol. 18:410-418(2008).
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, organellar chromatophore thylakoid
CC       membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       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; CP000815; ACB42650.1; -; Genomic_DNA.
DR   RefSeq; YP_002048860.1; NC_011087.1.
DR   AlphaFoldDB; B1X3Y1; -.
DR   SMR; B1X3Y1; -.
DR   GeneID; 6481240; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0070118; C:organellar chromatophore thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
DR   GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR   GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEA:InterPro.
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); Hydrogen ion transport; Ion transport; Membrane;
KW   Organellar chromatophore; Plastid; Thylakoid; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..242
FT                   /note="ATP synthase subunit a, organellar chromatophore"
FT                   /id="PRO_0000362606"
FT   TRANSMEM        28..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        128..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        193..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        214..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
SQ   SEQUENCE   242 AA;  27245 MW;  18485505B40F870A CRC64;
     MVPLSFPFHV AELEVGQHLY WQIGNLNLHG QVFISSWVVI SALLVLVITG TRKMERDPQG
     VQNLLEFLWD YLRDLAREQI GEKAYRDWLP FIGTLFLFIF GCNWGGALVP WKLIELPNGE
     LGAPTADINT TVAMALLVSL SYFYAGLSRK GLRYFEYYVE PTPIMLPFKI IEDFTKPLSL
     SFRLFGNILA DELVVGVLAF LVPILVPLPA MFLGLFTSAI QALIFATLAA NYIGEAVHEE
     HH