ID   ATPB_PROWI              Reviewed;         481 AA.
AC   Q9TJR9;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, 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   Prototheca wickerhamii.
OG   Plastid; Non-photosynthetic plastid.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Prototheca.
OX   NCBI_TaxID=3111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TRANSCRIPT DETECTION.
RC   STRAIN=263-11;
RX   PubMed=12111556; DOI=10.1007/s00438-002-0681-6;
RA   Knauf U., Hachtel W.;
RT   "The genes encoding subunits of ATP synthase are conserved in the reduced
RT   plastid genome of the heterotrophic alga Prototheca wickerhamii.";
RL   Mol. Genet. Genomics 267:492-497(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:0000250}; Peripheral
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
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DR   EMBL; AJ245645; CAB53102.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9TJR9; -.
DR   SMR; Q9TJR9; -.
DR   PRIDE; Q9TJR9; -.
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..481
FT                   /note="ATP synthase subunit beta, plastid"
FT                   /id="PRO_0000254516"
FT   BINDING         162..169
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   481 AA;  52331 MW;  55B7D78F2E4DAAD6 CRC64;
     MTVFIETQNF GTITRIIGPV LDITFTGNKM PKIYHALSII DKNSEGLDIF IVCEVQQLLG
     DHCVRAISMN ATDGLKRGMT VFDTGDVLKV PVGRSTLGRI FNVLGETIDN LGPADTSNQL
     PIHRSAPKFI DLDTKLSIFE TGIKVVDLLA PYRRGGKIGL FGGAGVGKTV LIMELINNIA
     KTHGGVSVFG GVGERTREGN DLYMEMKESG IINEALISES KVALVYGQMN EPPGARMRVG
     LTALTMAEYF RDVSSQDVLL FIDNIFRFLQ AGSEVSALLG RLPSAVGYQP TLASEMGALQ
     ERITSTKDGS ITSIQAVYIP ADDLTDPAPA TTFAHLDATT VLSRGLASKG IYPAVDPLES
     TSTMLQPWIV GEEHYKCSQN VKQTLQRYKE LQDIIAILGL DELSPDDRLI VARARKIERF
     LSQPFFVAEL FTGLPGKYVS LAKTIQGFNL ILSGDLDALS EQAFYLVGDI EEAISKGFLK
     K