ID   ATPB_MANES              Reviewed;         500 AA.
AC   B1NWF7;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 68.
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   Manihot esculenta (Cassava) (Jatropha manihot).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC   Manihot.
OX   NCBI_TaxID=3983;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. TME3;
RX   PubMed=18214421; DOI=10.1007/s00122-007-0706-y;
RA   Daniell H., Wurdack K.J., Kanagaraj A., Lee S.-B., Saski C., Jansen R.K.;
RT   "The complete nucleotide sequence of the cassava (Manihot esculenta)
RT   chloroplast genome and the evolution of atpF in Malpighiales: RNA editing
RT   and multiple losses of a group II intron.";
RL   Theor. Appl. Genet. 116:723-737(2008).
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; EU117376; ABV66161.1; -; Genomic_DNA.
DR   RefSeq; YP_001718444.1; NC_010433.1.
DR   AlphaFoldDB; B1NWF7; -.
DR   SMR; B1NWF7; -.
DR   GeneID; 5999989; -.
DR   KEGG; mesc:5999989; -.
DR   OrthoDB; 495235at2759; -.
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..500
FT                   /note="ATP synthase subunit beta, chloroplastic"
FT                   /id="PRO_0000339628"
FT   BINDING         174..181
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ   SEQUENCE   500 AA;  53771 MW;  F1DADD877E0FFE17 CRC64;
     MRINPTTSTS GPGVSALEKK NLGRIAQIIG PVLDVAFPPG KMPNIYNALV VKGRDTAGQE
     INVTCEVQQL LGNNRVRAVA MSATDGLTRG MEVIDTGAPL SVPVGGATLG RIFNVLGEPV
     DDLGPVDTRA TSPIHRSAPA FIQLDTKLSI FETGIKVVDL LAPYRRGGKI GLFGGAGVGK
     TVLIMELINN IAKAHGGVSV FGGVGERTRE GNDLYMEMKE SGVINEENIA ESKVALVYGQ
     MNEPPGARMR VGLTALTMAE YFRDVNEQDV LLFIDNIFRF VQAGSEVSAL LGRMPSAVGY
     QPTLSTEMGS LQERITSTKE GSITSIQAVY VPADDLTDPA PATTFAHLDA TTVLSRGLAA
     KGIYPAVDPL DSTSTMLQPQ IVGEEHYETA QRVKQTLQRY KELQDIIAIL GLDELSEEDR
     LTVARARKIE RFLSQPFFVA EVFTGSPGKY VGLAETIRGF KLILSGELDS LPEQAFYLVG
     NIDEATAKAT NLEMENNLKK