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ATPI_SPIOL
ID   ATPI_SPIOL              Reviewed;         247 AA.
AC   P06451;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   25-MAY-2022, entry version 130.
DE   RecName: Full=ATP synthase subunit a, chloroplastic;
DE   AltName: Full=ATP synthase F0 sector subunit a;
DE   AltName: Full=F-ATPase subunit IV;
GN   Name=atpI;
OS   Spinacia oleracea (Spinach).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2443718; DOI=10.1016/0022-2836(87)90690-5;
RA   Hudson G.S., Mason J.G., Holton T.A., Koller B., Cox G.B., Whitfeld P.R.,
RA   Bottomley W.;
RT   "A gene cluster in the spinach and pea chloroplast genomes encoding one CF1
RT   and three CF0 subunits of the H+-ATP synthase complex and the ribosomal
RT   protein S2.";
RL   J. Mol. Biol. 196:283-298(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Hennig J., Herrmann R.G.;
RT   "Chloroplast ATP synthase of spinach contains nine nonidentical subunit
RT   species, six of which are encoded by plastid chromosomes in two operons in
RT   a phylogenetically conserved arrangement.";
RL   Mol. Gen. Genet. 203:117-128(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Geant d'hiver, and cv. Monatol;
RX   PubMed=11292076; DOI=10.1023/a:1006478403810;
RA   Schmitz-Linneweber C., Maier R.M., Alcaraz J.-P., Cottet A., Herrmann R.G.,
RA   Mache R.;
RT   "The plastid chromosome of spinach (Spinacia oleracea): complete nucleotide
RT   sequence and gene organization.";
RL   Plant Mol. Biol. 45:307-315(2001).
RN   [4]
RP   PROTEIN SEQUENCE OF 19-34.
RA   Fromme P., Graber P., Salnikow J.;
RT   "Isolation and identification of a fourth subunit in the membrane part of
RT   the chloroplast ATP-synthase.";
RL   FEBS Lett. 218:27-30(1987).
CC   -!- FUNCTION: Key component of the proton channel; it plays a direct role
CC       in the translocation of protons across the membrane.
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.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-
CC       pass membrane protein.
CC   -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000305}.
CC   -!- CAUTION: This has been proposed to be processed from a precursor
CC       (Ref.4); however no signal is predicted by signal sequence detection
CC       programs. {ECO:0000305}.
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DR   EMBL; X03775; CAA27401.1; -; Genomic_DNA.
DR   EMBL; AJ400848; CAB88713.1; -; Genomic_DNA.
DR   PIR; S00582; PWSPA6.
DR   RefSeq; NP_054920.1; NC_002202.1.
DR   PDB; 6FKF; EM; 3.10 A; a=1-247.
DR   PDB; 6FKH; EM; 4.20 A; a=1-247.
DR   PDB; 6FKI; EM; 4.30 A; a=1-247.
DR   PDB; 6VM1; EM; 7.90 A; a=1-247.
DR   PDB; 6VM4; EM; 7.08 A; a=1-247.
DR   PDB; 6VMB; EM; 5.23 A; a=1-247.
DR   PDB; 6VMG; EM; 6.46 A; a=1-247.
DR   PDB; 6VOF; EM; 4.51 A; a=1-247.
DR   PDB; 6VOH; EM; 4.16 A; a=1-247.
DR   PDB; 6VOJ; EM; 4.34 A; a=1-247.
DR   PDB; 6VOL; EM; 4.06 A; a=1-247.
DR   PDB; 6VON; EM; 3.35 A; a=1-247.
DR   PDBsum; 6FKF; -.
DR   PDBsum; 6FKH; -.
DR   PDBsum; 6FKI; -.
DR   PDBsum; 6VM1; -.
DR   PDBsum; 6VM4; -.
DR   PDBsum; 6VMB; -.
DR   PDBsum; 6VMG; -.
DR   PDBsum; 6VOF; -.
DR   PDBsum; 6VOH; -.
DR   PDBsum; 6VOJ; -.
DR   PDBsum; 6VOL; -.
DR   PDBsum; 6VON; -.
DR   AlphaFoldDB; P06451; -.
DR   SMR; P06451; -.
DR   IntAct; P06451; 1.
DR   STRING; 3562.P06451; -.
DR   ChEMBL; CHEMBL2366567; -.
DR   GeneID; 2715580; -.
DR   KEGG; soe:2715580; -.
DR   OrthoDB; 1136313at2759; -.
DR   PRO; PR:P06451; -.
DR   Proteomes; UP000054095; 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   1: Evidence at protein level;
KW   3D-structure; ATP synthesis; CF(0); Chloroplast; Direct protein sequencing;
KW   Hydrogen ion transport; Ion transport; Membrane; Plastid;
KW   Reference proteome; Thylakoid; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..247
FT                   /note="ATP synthase subunit a, chloroplastic"
FT                   /id="PRO_0000002599"
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        134..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        220..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        37..39
FT                   /note="GQV -> DKA (in Ref. 2; CAA27401)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        144
FT                   /note="T -> A (in Ref. 2; CAA27401)"
FT                   /evidence="ECO:0000305"
FT   STRAND          28..36
FT                   /evidence="ECO:0007829|PDB:6FKF"
FT   HELIX           37..54
FT                   /evidence="ECO:0007829|PDB:6FKF"
FT   TURN            55..57
FT                   /evidence="ECO:0007829|PDB:6FKF"
FT   STRAND          58..60
FT                   /evidence="ECO:0007829|PDB:6FKF"
FT   HELIX           69..84
FT                   /evidence="ECO:0007829|PDB:6FKF"
FT   TURN            85..87
FT                   /evidence="ECO:0007829|PDB:6FKF"
FT   HELIX           95..114
FT                   /evidence="ECO:0007829|PDB:6FKF"
FT   STRAND          118..120
FT                   /evidence="ECO:0007829|PDB:6FKF"
FT   HELIX           130..132
FT                   /evidence="ECO:0007829|PDB:6FKF"
FT   HELIX           134..154
FT                   /evidence="ECO:0007829|PDB:6FKF"
FT   STRAND          158..160
FT                   /evidence="ECO:0007829|PDB:6FKF"
FT   HELIX           172..207
FT                   /evidence="ECO:0007829|PDB:6FKF"
FT   HELIX           214..243
FT                   /evidence="ECO:0007829|PDB:6FKF"
SQ   SEQUENCE   247 AA;  27087 MW;  013D875F8E409377 CRC64;
     MNVLSYSINP LKGLYAISGV EVGQHFYWQI GGFQIHGQVL ITSWVVIAIL LGSAAIAVRS
     PQTIPTGGQN FFEYVLEFIR DVSKTQIGEE YRPWVPFIGT MFLFIFVSNW SGALLPWKII
     QLPHGELAAP TNDINTTVAL ALLTSVAYFY AGLTKKGLGY FGKYIQPTPI LLPINILEDF
     TKPLSLSFRL FGNILADELV VVVLVSLVPL VVPIPVMFLG LFTSGIQALI FATLAAAYIG
     ESLEGHH
 
 
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