ATPI_MESVI
ID ATPI_MESVI Reviewed; 247 AA.
AC Q9MUS9;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 92.
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 Mesostigma viride (Green alga).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Mesostigmatophyceae;
OC Mesostigmatales; Mesostigmataceae; Mesostigma.
OX NCBI_TaxID=41882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-296 / KY-14 / CCMP 2046;
RX PubMed=10688199; DOI=10.1038/35001059;
RA Lemieux C., Otis C., Turmel M.;
RT "Ancestral chloroplast genome in Mesostigma viride reveals an early branch
RT of green plant evolution.";
RL Nature 403:649-652(2000).
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; AF166114; AAF43822.1; -; Genomic_DNA.
DR RefSeq; NP_038381.1; NC_002186.1.
DR AlphaFoldDB; Q9MUS9; -.
DR SMR; Q9MUS9; -.
DR GeneID; 800972; -.
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..247
FT /note="ATP synthase subunit a, chloroplastic"
FT /id="PRO_0000002589"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
SQ SEQUENCE 247 AA; 27748 MW; 5B99D9287931BB50 CRC64;
MINPSSMENF NMLYQLSKVE VGQHFYWQIG DFEVHGQVLL VSWFVMTIII SLSIFGTRNL
QTIPTGTQNF VEYVLEFIRD LAKTQIGEED YRSWVPFIGT IFLFIFVSNW SGALVPWKLI
EIPNGELAAP TNDINTTAAL ALLTSISYFY AGFSKKGLRY FKRYISPTPV LLPINLLEDF
TKPLSLSFRL FGNILADELV VGVLITLVPL VVPMPLMLLG LFTSAIQALI FATLAAAYIG
EAVEDHH