ID   ATPB_NEPOL              Reviewed;         491 AA.
AC   Q9TL34;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 110.
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   Nephroselmis olivacea (Green alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Chlorophyta; Nephroselmidophyceae;
OC   Nephroselmidales; Nephroselmidaceae; Nephroselmis.
OX   NCBI_TaxID=31312;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-484 / S-N-5-8;
RX   PubMed=10468594; DOI=10.1073/pnas.96.18.10248;
RA   Turmel M., Otis C., Lemieux C.;
RT   "The complete chloroplast DNA sequence of the green alga Nephroselmis
RT   olivacea: insights into the architecture of ancestral chloroplast
RT   genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:10248-10253(1999).
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; AF137379; AAD54782.1; -; Genomic_DNA.
DR   RefSeq; NP_050811.1; NC_000927.1.
DR   AlphaFoldDB; Q9TL34; -.
DR   SMR; Q9TL34; -.
DR   PRIDE; Q9TL34; -.
DR   GeneID; 801986; -.
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..491
FT                   /note="ATP synthase subunit beta, chloroplastic"
FT                   /id="PRO_0000144529"
FT   BINDING         163..170
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ   SEQUENCE   491 AA;  52308 MW;  BBB29F3B7CF55B4D CRC64;
     MSQAGVKTKQ AGKIVQIVGP VMDVAFQPGS MPNIYNALIV KGRNGAGQEV SVVCEVQQLL
     GDGLVRAVSM SATDGLMRGM EVTDTGRALS VPVGPTTLGR IFNVLGEPVD NMGPVGNEKT
     LPIHREAPAF VDLDTKLSIF ETGIKVVDLL APYRRGGKIG LFGGAGVGKT VLIMELINNI
     AKAHGGVSVF GGVGERTREG NDLYMEMCES KVINKADVKS SKVALVYGQM NEPPGARMRV
     GLTALTMAEY FRDVNNQDVL LFIDNIFRFV QAGSEVSALL GRMPSAVGYQ PTLATEMGGL
     QERITSTKDG SITSIQAVYV PADDLTDPAP ATTFAHLDAT TVLSRNLAAK GIYPAVDPLD
     STSTMLQPWI LGDDHYGTAQ RVKQTLQRYK ELQDIIAILG LDELSEEDRM IVARARKIER
     FLSQPFFVAE VFTGAPGKYV PLAESIQGFK LILSGELDSL PESAFYLVGN IEEAIAKAAS
     IQAAAAAAAA A