ID   ATPB_CUSJA              Reviewed;         490 AA.
AC   Q8MBG0;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=ATP synthase subunit beta, plastid;
DE            EC=7.1.2.2;
DE   AltName: Full=ATP synthase F1 sector subunit beta;
DE   AltName: Full=F-ATPase subunit beta;
GN   Name=atpB;
OS   Cuscuta japonica (Japanese dodder).
OG   Plastid.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Convolvulaceae; Cuscuteae; Cuscuta;
OC   Cuscuta subgen. Monogynella.
OX   NCBI_TaxID=81913;
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 (By similarity). {ECO:0000250}.
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   -!- 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) (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid membrane {ECO:0000305}; Peripheral
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
CC   -!- CAUTION: This organism being non-photosynthetic, the role of this
CC       protein is uncertain. {ECO:0000305}.
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DR   EMBL; AY100849; AAM52203.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8MBG0; -.
DR   SMR; Q8MBG0; -.
DR   PRIDE; Q8MBG0; -.
DR   GO; GO:0042170; C:plastid 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); Hydrogen ion transport; Ion transport;
KW   Membrane; Nucleotide-binding; Plastid; Translocase; Transport.
FT   CHAIN           1..490
FT                   /note="ATP synthase subunit beta, plastid"
FT                   /id="PRO_0000254467"
FT   BINDING         170..177
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   490 AA;  53236 MW;  BC3215DAC6359EE8 CRC64;
     MRINPPTYGS EISSIEKKNR GCIVQIIGPV LDVAFPPGKM PNIYNALVVK GRDTEQMNVT
     CEVQQLLGNN RVRAVAMNDT DGLMRGMEVI DTGTPITVPV GGSTLGRIFN VLGEPVDNFG
     PVDTNTTSTI HRSAPAFIQL DTKLSIFETG IKVVDFLAPY RRGGKIGLFG GAGVGKTVLI
     MELINNIAKA HGGVSVFGGV GERTREGNDL YMEMKESGVI NENNITESKV ALVYGQMNEP
     PGARMRVGLT ALTMAEYFRD VNEQDVLLFI DNIFRFVQAG SEVSALLGRM PSAVGYQPTL
     STEMGSLQER ITSTKEGSIT SIQAVYVPAD DLTDPAPATT FAHLDATTVL SRGLAAKGIY
     PAVDPLDSTS MMLQPRIVGE EHYETAQKVK QTLQRYKELQ DIIAILGLDE LSEEDRLTVA
     RARKIERFLS QPFFVAEVFT GSPGKYVGLA ETIRGFNLIL SGELDSLPEQ AFYLVGNIDE
     ATEKAMNLKT