ID   ATPB_ANGEV              Reviewed;         492 AA.
AC   A2T340;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 75.
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   Angiopteris evecta (Mule's foot fern) (Polypodium evectum).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Polypodiopsida; Marattiidae; Marattiales; Marattiaceae; Angiopteris.
OX   NCBI_TaxID=13825;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Roper J.M., Hansen S.K., Wolf P.G., Karol K.G., Mandoli D.F.,
RA   Everett K.D.E., Kuehl J.V., Boore J.L.;
RT   "The complete plastid genome sequence of Angiopteris evecta (G. Forst.)
RT   Hoffm. (Marattiaceae).";
RL   Am. Fern J. 97:95-106(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. {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; DQ821119; ABG79607.1; -; Genomic_DNA.
DR   RefSeq; YP_001023708.1; NC_008829.1.
DR   AlphaFoldDB; A2T340; -.
DR   SMR; A2T340; -.
DR   GeneID; 4788193; -.
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..492
FT                   /note="ATP synthase subunit beta, chloroplastic"
FT                   /id="PRO_0000339605"
FT   BINDING         170..177
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ   SEQUENCE   492 AA;  52812 MW;  C45A0788DB03F5D4 CRC64;
     MKTNPLVFVV STAVEKNAGY ITQIIGPVLD VAFSPGKLPN IYNSLIVKGQ NPAGQEINVT
     CEVQQLLGND RVRAVAMSAT DGLMRGMKVI DTGAPLSVPV GEVTLGRIFN VLGEPVDNLG
     PVDAGTTSPI HKSAPAFTQL DTKLSIFETG IKVVDLSAPY RRGGKIGLFG GAGVGKTVLI
     MELINNIAKA HGGVSVFGGV GERTREGNDL YMEMKESKVI NQENISESKV ALVYGQMNEP
     PGARMRVGLT ALTMAEYFRD VNKQDVLLFI DNIFRFVQAG SEVSASSGRM PSAVGYQPTL
     ATEMGSLQER ITSTKEGSIT SIQAVYVPAD DLTDPAPATT FAHSDATTVL SRGLAAKGIY
     PAVDPLDSTS TMLQPWIVGE EHYETAQGVK QTLQRYKELQ DIIAILGLDE LSEEDRLTVA
     RARKIERFLS QPFFVAEVFT GSPGKYVSLI ETIKGFQMIL SGELDSLPEQ AFYLVGNIDE
     ATAKAATLQV ES