ID   ATPB_GNEPA              Reviewed;         482 AA.
AC   A6BM09; B7ZIA6;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-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   Gnetum parvifolium (Small-leaved jointfir) (Gnetum scandens var.
OS   parvifolium).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Gnetopsida; Gnetidae; Gnetales; Gnetaceae; Gnetum.
OX   NCBI_TaxID=33153;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17383970; DOI=10.1093/molbev/msm059;
RA   Wu C.-S., Wang Y.-N., Liu S.-M., Chaw S.-M.;
RT   "Chloroplast genome (cpDNA) of Cycas taitungensis and 56 cp protein-coding
RT   genes of Gnetum parvifolium: insights into cpDNA evolution and phylogeny of
RT   extant seed plants.";
RL   Mol. Biol. Evol. 24:1366-1379(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=19166950; DOI=10.1016/j.ympev.2008.12.026;
RA   Wu C.-S., Lai Y.-T., Lin C.-P., Wang Y.-N., Chaw S.-M.;
RT   "Evolution of reduced and compact chloroplast genomes (cpDNAs) in
RT   gnetophytes: Selection toward a lower-cost strategy.";
RL   Mol. Phylogenet. Evol. 52:115-124(2009).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAH11286.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB295905; BAF64854.1; -; Genomic_DNA.
DR   EMBL; AP009569; BAH11286.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_002519775.1; NC_011942.1.
DR   AlphaFoldDB; A6BM09; -.
DR   SMR; A6BM09; -.
DR   PRIDE; A6BM09; -.
DR   GeneID; 7368119; -.
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..482
FT                   /note="ATP synthase subunit beta, chloroplastic"
FT                   /id="PRO_0000339620"
FT   BINDING         168..175
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ   SEQUENCE   482 AA;  51983 MW;  7494993DE674B6C9 CRC64;
     MKTKNTFLVS TKSETSIGQI TQIIGPVLDV SFPPGNLPNI YNSLIVKGQK DDRAFSVTCE
     VQQLLGNNTV RAVAMSATDG LTRGMKVINT GACLSVPVGK ATLGRIFNVL GEPVDNLGPV
     DTDTTFPIHR PAPAFPQLDT NLSIFETGIK VVDLLAPYRR GGKIGLFGGA GVGKTVLIME
     LINNIAKAHG GVSVFGGVGE RTREGNDLYM EMKESGVINE KNIAESKVAL VYGQMNEPPG
     ARMRVGLTAL AMAEYFRDVN EQDVLLFIDN IFRFVQAGSE VSALLGRMPS AVGYQPTLST
     EMGSLQERIT STKKGSITSI QAVYVPADDL TDPAPATTFA HLDATTVLSR GLAAKGIYPA
     VDPLDSTSTM LQPEIVGEQH YEIAQGVKQT LQRYKELQDI IAILGLDELS EEDRLTVARA
     RKIERFLSQP FFVAEVFTGS PGKYVSLIET IRGFQMILSG DLDGLPEQSF YLVGNIDEVI
     SS