ID   ATPB_IDIAU              Reviewed;         498 AA.
AC   Q9MRF3;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 102.
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   Idiospermum australiense (Ribbonwood tree) (Calycanthus australiensis).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Magnoliidae; Laurales; Calycanthaceae;
OC   Idiospermoideae; Idiospermum.
OX   NCBI_TaxID=13573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12118410; DOI=10.1093/sysbio/49.2.306;
RA   Savolainen V., Chase M.W., Morton C.M., Hoot S.B., Soltis D.E., Bayer C.,
RA   Fay M.F., de Bruijn A., Sullivan S., Qiu Y.-L.;
RT   "Phylogenetics of flowering plants based upon a combined analysis of
RT   plastid atpB and rbcL gene sequences.";
RL   Syst. Biol. 49:306-362(2000).
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; AJ235500; CAB89714.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9MRF3; -.
DR   SMR; Q9MRF3; -.
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; Plastid; Thylakoid;
KW   Translocase; Transport.
FT   CHAIN           1..498
FT                   /note="ATP synthase subunit beta, chloroplastic"
FT                   /id="PRO_0000254485"
FT   BINDING         172..179
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ   SEQUENCE   498 AA;  53631 MW;  7D1D92237D05882F CRC64;
     MRINPTTSGP GVSTLEKKNL GRIAQIIGPV LDVAFPPGKM PNIYNALVVK GRDTVGQQIN
     VACEVQQLLG NNRVRAVAMS ATDGLMRGME VIDTGAPLSV PVGGATLGRI FNVLGEPVDN
     LGPVDTRTTS PIHRSAPAFI QLDTKLSIFE TGIKVVDLLA PYRRGGKIGL FGGAGVGKTV
     LIMELINNIA KAHGGVSVFG GVGERTREGN DLYMEMKESG VINEQNIAES KVALVHGQMN
     EPPGARMRVG LTALTMAEYF RDVNEQDVLL FIDNIFRFVQ AGSEVSALLG RMPSAVGYQP
     TLSTEMGSLQ ERITSTKEGS ITSIQAVYVP ADDLTDPAPA TTFAHLDATT VLSRGLAAKG
     IYPAVDPLDS TSTMLQPRIV GEEHYETAQR VKQTSQRYKE LQDIIAILGL DELSEEDRLT
     VARARKMERF LSQPFFVAEV FTGSPGKYVG LAETIRGFQL ILSGELDGLP EQAFYLVGNI
     DEATAKAMKL ELESNLKK