ID   ATPB_CUSSA              Reviewed;         494 AA.
AC   Q8MBG4;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 100.
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 sandwichiana (Kauna'oa).
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. Cleistogrammica.
OX   NCBI_TaxID=197374;
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 [GENOMIC DNA].
RX   PubMed=15999247; DOI=10.1007/s00239-004-0267-5;
RA   Stefanovic S., Olmstead R.G.;
RT   "Down the slippery slope: plastid genome evolution in Convolvulaceae.";
RL   J. Mol. Evol. 61:292-305(2005).
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 probably non-photosynthetic, the role of
CC       this protein is uncertain. {ECO:0000305}.
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DR   EMBL; AY100845; AAM52199.1; -; Genomic_DNA.
DR   EMBL; AY936346; AAY58014.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8MBG4; -.
DR   SMR; Q8MBG4; -.
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..494
FT                   /note="ATP synthase subunit beta, plastid"
FT                   /id="PRO_0000254469"
FT   BINDING         169..176
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   494 AA;  54038 MW;  88ED1686F8C6A1DF CRC64;
     MRLTPNYDYE VSSIDKKKRG YIVQIIGPVL DVAFSPGMMP SIYNALVVQG RHKQEPNVTC
     EVQQLLGNNR VRAVAMSDTD GLMRGMEVID TGTPISVPVG GSTLGRIFNV LGEPVDQLGP
     VETNQLSPIH RSAPPFLKLD TRLSIFETGI KVVDLLAPYR RGGKVGLFGG AGVGKTVLIM
     ELINNIAKAY GGVSVFGGVG ERTREGNDLY MEMKESGVIN QQKLAESKVA LVYGQMNEPP
     GARMRVGLTA LTMAEYFRDV NRQDVLLFID NIFRFVQAGS EVSALLGRMP SAVGYQPTLS
     TEMGSLQERI TSTKEGSITS IQAVYVPADD LTDPAPATTF AHLDATTVLS RSLAAKGIYP
     AVDPLDSTSM MLQPQIVGEQ HYKTAQRVKQ TLQRYKELQD IIAILGLDEL SDDDRLTVAR
     ARKIERFLSQ PFFVAEIFTG SPGKYVSLAE TIRGCTLILS GEFDDLPEQT FYLVGTIDEV
     NAKAILEEEK NFTK