ID   ATPB_AETCO              Reviewed;         490 AA.
AC   A4QJC2;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=ATP synthase subunit beta, chloroplastic {ECO:0000255|HAMAP-Rule:MF_01347};
DE            EC=7.1.2.2 {ECO:0000255|HAMAP-Rule:MF_01347};
DE   AltName: Full=ATP synthase F1 sector subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
DE   AltName: Full=F-ATPase subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
GN   Name=atpB {ECO:0000255|HAMAP-Rule:MF_01347};
OS   Aethionema cordifolium (Lebanon stonecress).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Aethionemeae; Aethionema.
OX   NCBI_TaxID=434059;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Hosouchi T., Tsuruoka H., Kotani H.;
RT   "Sequencing analysis of Aethionema coridifolium chloroplast DNA.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. The catalytic sites are hosted primarily by the
CC       beta subunits. {ECO:0000255|HAMAP-Rule:MF_01347}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC         Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01347};
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(1), b(1), b'(1) and c(9-12). {ECO:0000255|HAMAP-
CC       Rule:MF_01347}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000255|HAMAP-Rule:MF_01347}; Peripheral membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_01347}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000255|HAMAP-Rule:MF_01347}.
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DR   EMBL; AP009366; BAF49777.1; -; Genomic_DNA.
DR   RefSeq; YP_001122953.1; NC_009265.1.
DR   AlphaFoldDB; A4QJC2; -.
DR   SMR; A4QJC2; -.
DR   PRIDE; A4QJC2; -.
DR   GeneID; 4968666; -.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.1140.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_01347; ATP_synth_beta_bact; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR005722; ATP_synth_F1_bsu.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR   InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR024034; ATPase_F1/V1_b/a_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF50615; SSF50615; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01039; atpD; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; ATP-binding; CF(1); Chloroplast; Hydrogen ion transport;
KW   Ion transport; Membrane; Nucleotide-binding; Phosphoprotein; Plastid;
KW   Thylakoid; Translocase; Transport.
FT   CHAIN           1..490
FT                   /note="ATP synthase subunit beta, chloroplastic"
FT                   /id="PRO_0000339602"
FT   BINDING         172..179
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
FT   MOD_RES         6
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P19366"
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P19366"
SQ   SEQUENCE   490 AA;  52796 MW;  BD868F51796B0BB8 CRC64;
     MRINPTTSDP GVSILENKNL GRIAQIIGPV LDVAFPPGKM PNIYNALVVK GRDTLGQEIN
     VTCEVQQLLG NNRVRAVAMS ATEGLKRGMD VVDMGTPLSV PVGGATLGRI FNVLGEPVDN
     LGPVDTRTTS PIHKSAPAFI QLDTKLSIFE TGIKVVDLLA PYRRGGKIGL FGGAGVGKTV
     LIMELINNIA KAHGGVSVFG GVGERTREGN DLYMEMKESG VINEQNLAES KVALVYGQMN
     EPPGARMRVG LTALTMAEYF RDVNEQDVLL FIDNIFRFVQ AGSEVSALLG RMPSAVGYQP
     TLSTEMGSLQ ERITSTKKGS ITSIQAVYVP ADDLTDPAPA TTFAHLDATT VLSRGLAAKG
     IYPAVDPLDS TSTMLQPRIV GEEHYETAQQ VKQTLQRYKE LQDIIAILGL DELSEEDRLT
     VARARKIERF LSQPFFVAEV FTGSPGKYVG LAETIRGFKL ILSGELDSLP EQAFYLVGNI
     DEATAKATNL