ID   ATPB_CALSE              Reviewed;         490 AA.
AC   Q8MBM4;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 97.
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   Calystegia sepium (Hedge bindweed) (Convolvulus sepium).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Convolvulaceae; Convolvuleae; Calystegia.
OX   NCBI_TaxID=47519;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   AGRICOLA=IND23320510;
RA   Stefanovic S., Krueger L., Olmstead R.G.;
RT   "Monophyly of the Convolvulaceae and circumscription of their major
RT   lineages based on DNA sequences of multiple chloroplast loci.";
RL   Am. J. Bot. 89:1510-1522(2002).
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; AY100783; AAM52137.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8MBM4; -.
DR   SMR; Q8MBM4; -.
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..490
FT                   /note="ATP synthase subunit beta, chloroplastic"
FT                   /id="PRO_0000254453"
FT   BINDING         170..177
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ   SEQUENCE   490 AA;  52863 MW;  ABCD73451A62A4C4 CRC64;
     MRSNPTTSGS EVSAVEKKNL GRIVKIIGPV LDVAFPPGKM PNIYNALVVQ GRDNEQTNVT
     CEVQQLLGNN RVRAVAMSDT NGLMRGMEVI NTGAPISVPV GGSTLGRIFN VLGQPVDNLG
     PVDTNTTSPI HRSAPAFIQL DTKLSIFETG IKVVDLLAPY RRGGKIGLFG GAGVGKTVLI
     MELINNIAKA HGGVSVFGGV GERTREGNDL YMEMKESGVI NEENIAESKV ALVYGQMNEP
     PGARMRVGLT ALTMAEYFRD VNEQDVLLFI DNIFRFVQAG SEVSALLGRM PSAVGYQPTL
     STEMGTLQER ITSTKEGSIT SIQAVYVPAD DLTDPAPATT FAHLDATTVL SRGLAAKGIY
     PAVDPLDSTS TMLQPRIVGE EHYETAQRVK QTLQRYKELQ DIIAILGLDE LSEEDRLTVA
     RARKIERFLS QPFFVAEVFT GSPGKYVGLA ETIRGFQLIL SGELDGLPEQ AFYLVGNIDE
     ATAKAMNLKT