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ATPI_MARPO
ID   ATPI_MARPO              Reviewed;         248 AA.
AC   P06289;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   25-MAY-2022, entry version 120.
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   Marchantia polymorpha (Liverwort) (Marchantia aquatica).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=3197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   DOI=10.1038/322572a0;
RA   Ohyama K., Fukuzawa H., Kohchi T., Shirai H., Sano T., Sano S., Umesono K.,
RA   Shiki Y., Takeuchi M., Chang Z., Aota S., Inokuchi H., Ozeki H.;
RT   "Chloroplast gene organization deduced from complete sequence of liverwort
RT   Marchantia polymorpha chloroplast DNA.";
RL   Nature 322:572-574(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2974085; DOI=10.1016/0022-2836(88)90002-2;
RA   Umesono K., Inokuchi H., Shiki Y., Takeuchi M., Chang Z., Fukuzawa H.,
RA   Kohchi T., Shirai H., Ohyama K., Ozeki H.;
RT   "Structure and organization of Marchantia polymorpha chloroplast genome.
RT   II. Gene organization of the large single copy region from rps'12 to
RT   atpB.";
RL   J. Mol. Biol. 203:299-331(1988).
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; X04465; CAA28065.1; -; Genomic_DNA.
DR   PIR; A01058; LWLV6.
DR   RefSeq; NP_039279.1; NC_001319.1.
DR   AlphaFoldDB; P06289; -.
DR   SMR; P06289; -.
DR   EnsemblPlants; PTQ39617; PTQ39617; MARPO_0044s0072.
DR   GeneID; 2702537; -.
DR   Gramene; PTQ39617; PTQ39617; MARPO_0044s0072.
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; Thylakoid; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..248
FT                   /note="ATP synthase subunit a, chloroplastic"
FT                   /id="PRO_0000002588"
FT   TRANSMEM        37..57
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;  27742 MW;  566CD63FFCFD009C CRC64;
     MSHTAKMAST FNNFYEISNV EVGQHFYWQL GSFQVHAQVL ITSWIVIAIL LSLAVLATRN
     LQTIPMGGQN FVEYVLEFIR DLTRTQIGEE EYRPWVPFIG TMFLFIFVSN WSGALFPWRV
     FELPNGELAA PTNDINTTVA LALLTSVAYF YAGLHKKGLS YFGKYIQPTP VLLPINILED
     FTKPLSLSFR LFGNILADEL VVAVLISLVP LVVPIPMMFL GLFTSAIQAL IFATLAAAYI
     GESMEGHH
 
 
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