ID   ATPB_PTEES              Reviewed;         473 AA.
AC   O03080;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 109.
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};
DE   Flags: Fragment;
GN   Name=atpB {ECO:0000255|HAMAP-Rule:MF_01347};
OS   Pteridium esculentum (Bracken fern).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Polypodiopsida; Polypodiidae; Polypodiales; Dennstaedtiineae;
OC   Dennstaedtiaceae; Pteridium.
OX   NCBI_TaxID=32102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Wolf P.G.;
RT   "Evaluation of atpB nucleotide sequences for phylogenetic studies of ferns
RT   and other pteridophytes.";
RL   Am. J. Bot. 84:1429-1440(1997).
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; U93834; AAB51742.1; -; Genomic_DNA.
DR   AlphaFoldDB; O03080; -.
DR   SMR; O03080; -.
DR   PRIDE; O03080; -.
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-KW.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC.
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..>473
FT                   /note="ATP synthase subunit beta, chloroplastic"
FT                   /id="PRO_0000144545"
FT   BINDING         172..179
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
FT   NON_TER         1
FT   NON_TER         473
SQ   SEQUENCE   473 AA;  50434 MW;  5F30596E88E90029 CRC64;
     IVTKTSFLSF EISELVKKNV GYITQIIGPV LDVASSPGKM PNIYNSLIIK GQNSAGQELN
     VTCEVQQLLG NNEVRAVAMS ATDGLTRGMG AVDTGAPLSV PVGETTLGRI SNVLGEPVDN
     LGPVQSSTTF PIHRSAPAFI QLDTKLSIFE TGIKVVDLSA PYRRGGKIGL FGGAGVGKTV
     LITELINNIA KAHGGVSVSG GVGERTREGN DPYMEMKESK VINEQNISES KVALVYGQMN
     EPPGASMRVG STASTMAEYF RDVNKQDVLP FIDYILRFVQ AGSEVSALLG RMPSAVGYQP
     TLGTEMGSSQ ERITSTKDGS ITSIQAVYVP ADDLTDPAPA TTSAHLDATT VLSRGLAAKG
     IYPAVDPLDS TSTMSQPWIV GEEHYETAQG VKQTSQRYKE LQDIIAILGL DELSEEDRLT
     VARARKIERF SSQPSFVAEV FTGSPGKYVS LPETIKGFQM ILPGELDNLP EQA