ID   ATPB_PTEAQ              Reviewed;         495 AA.
AC   O03079;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 2.
DT   03-AUG-2022, entry version 117.
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   Pteridium aquilinum (Bracken fern) (Pteris aquilina).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Polypodiopsida; Polypodiidae; Polypodiales; Dennstaedtiineae;
OC   Dennstaedtiaceae; Pteridium.
OX   NCBI_TaxID=32101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
RA   Wolf P.G., Su P.-H.;
RL   Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-473.
RC   TISSUE=Frond;
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; U93835; AAB51743.3; -; Genomic_DNA.
DR   AlphaFoldDB; O03079; -.
DR   SMR; O03079; -.
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..495
FT                   /note="ATP synthase subunit beta, chloroplastic"
FT                   /id="PRO_0000144544"
FT   BINDING         172..179
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ   SEQUENCE   495 AA;  52835 MW;  ED40BD8939317068 CRC64;
     MVTKTSFLSF EISELVKKNV GYITQIIGPV LDVASSPGKM PNIYNSLIIK GQNPAGQEIN
     VTCEVQQLLG NNEVRAVAMS ATDGLTRGMG AVDTGAPLSV PVGETTLGRI SNVLGEPVDN
     LGPVQSSTTF PIHRSAPAFI QLDTKLSIFE TGIKVVDLLA PYRRGGKIGL FGGAGVGKTV
     LIMELINNIA KAHGGVSVSG GVGERTREGN DPYMEMKESK VINEENISES KVALVYGQMN
     EPPGARMRVG STASTMAEYF RDVNKQDVLP FIDNILRFVQ AGSEVSALLG RMPSAVGYQP
     TLGTEMGSSQ ERITSTKDGS ITSIQAVYVP ADDLTDPAPA TTSAHLDATT VLSRGLAAKG
     IYPAVDPLDS TSTMSQPWIV GEEHYETAQG VKQTSQRYKE LQDIIAILGL DELSEEDRQT
     VARARKIERF SSQPSFVAEV FTGSPGKYVS LSETIKGFQM ILPGELDNLP EQAFYLVGNI
     DEATAKAAAL QVEGQ