ID   ATPB_CUSGR              Reviewed;         494 AA.
AC   Q8MBG3; A7M905;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 106.
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 gronovii (Common dodder) (Epithymum gronovii).
OG   Plastid.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Convolvulaceae; Cuscuteae; Cuscuta;
OC   Cuscuta subgen. Grammica; Cuscuta sect. Oxycarpae.
OX   NCBI_TaxID=35886;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17714582; DOI=10.1186/1471-2229-7-45;
RA   Funk H.T., Berg S., Krupinska K., Maier U.-G., Krause K.;
RT   "Complete DNA sequences of the plastid genomes of two parasitic flowering
RT   plant species, Cuscuta reflexa and Cuscuta gronovii.";
RL   BMC Plant Biol. 7:45-45(2007).
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 thylakoid membrane {ECO:0000305};
CC       Peripheral membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Young tissue from this organism is photosynthetic and contains
CC       some thylakoids, although the photosynthetic activity does not exceed
CC       the light compensation point. {ECO:0000305}.
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DR   EMBL; AY100846; AAM52200.1; -; Genomic_DNA.
DR   EMBL; AM711639; CAM98333.1; -; Genomic_DNA.
DR   RefSeq; YP_001430047.1; NC_009765.1.
DR   AlphaFoldDB; Q8MBG3; -.
DR   SMR; Q8MBG3; -.
DR   GeneID; 5536750; -.
DR   GO; GO:0055035; C:plastid 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-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; Thylakoid; Translocase; Transport.
FT   CHAIN           1..494
FT                   /note="ATP synthase subunit beta, plastid"
FT                   /id="PRO_0000254466"
FT   BINDING         169..176
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   494 AA;  54055 MW;  77B31B8DF4784B80 CRC64;
     MRLTPNYDYE VSSINKKKRG YIVQIIGPVL DVAFSPGMMP SIYNALVVQG RHNQEPNVTC
     EVQQLLGNNR VRAVAMSDTD GLMRGMEVID TGTPISVPVG GSTLGRIFNV LGEPVDQLGP
     VETNQLSPIH RSAPPFLKLD TRLSIFETGI KVVDLLAPYR RGGKVGLFGG AGVGKTVLIM
     ELINNIAKAY GGVSVFGGVG ERTREGNDLY MEMKESGVIN QQKLDESKVA LVYGQMNEPP
     GARMRVGLTA LTMAEYFRDV NRQDVLLFID NIFRFVQAGS EVSALLGRMP SAVGYQPTLS
     TEMGSLQERI TSTKEGSITS IQAVYVPADD LTDPAPATTF AHLDATTVLS RSLAAKGIYP
     AVDPLDSTSM MLQPQIVGEQ HYKTAQRVKQ TLQRYKELQD IIAILGLDEL SDDDRLTVAR
     ARKIERFLSQ PFFVAEIFTG SPGKYVSLAE TIRGCTLILS GEFDDLPEQA FYLVGTIDEV
     NAKAMLEEEK NFTK