ID   ATPB_ANEMR              Reviewed;         492 AA.
AC   B0YPN7;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=ATP synthase subunit beta, plastid {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   Aneura mirabilis (Parasitic liverwort) (Cryptothallus mirabilis).
OG   Plastid; Non-photosynthetic plastid.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Jungermanniopsida; Metzgeriidae; Metzgeriales; Aneuraceae; Aneura.
OX   NCBI_TaxID=280810;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18056074; DOI=10.1093/molbev/msm267;
RA   Wickett N.J., Zhang Y., Hansen S.K., Roper J.M., Kuehl J.V., Plock S.A.,
RA   Wolf P.G., dePamphilis C.W., Boore J.L., Goffinet B.;
RT   "Functional gene losses occur with minimal size reduction in the plastid
RT   genome of the parasitic liverwort Aneura mirabilis.";
RL   Mol. Biol. Evol. 25:393-401(2008).
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 membrane {ECO:0000250}; Peripheral
CC       membrane protein {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; EU043314; ABS54484.1; -; Genomic_DNA.
DR   RefSeq; YP_001687223.1; NC_010359.1.
DR   AlphaFoldDB; B0YPN7; -.
DR   SMR; B0YPN7; -.
DR   PRIDE; B0YPN7; -.
DR   GeneID; 5952226; -.
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..492
FT                   /note="ATP synthase subunit beta, plastid"
FT                   /id="PRO_0000339604"
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;  52849 MW;  48364453B85A4D2C CRC64;
     MINNPSLLGT SIPVTKNVGS ITQIIGPVLD IVFSPGKMPN IYNSLIVRGQ NSAGQEINVT
     CEVQQLLGNN EVRAVATSAT DGLMREMEVL DTGAPSSVPV GEATLGRIFN VLGEAVDNLG
     PVDAGLTSPI HRAAPSFIQL DTKLSIFETG IKVVDLLVPY RRGGKIGLFG GAGVGKTVLI
     MELINNIAKA HGGVSVFGGV GERTREGNDL YMEMKESKVI NEQNIAESKV ALVYGQMNEP
     PGARMRVGST ALTMAEYFRD VNKQDVLLFI DNIFRFVQAG SEVSALLGRM PSAVGYQPTL
     GTEMGTLQER ITSTKEGSIT SIQAVYVPAD DLTDPAPATT FAHLDATTVL SRGLAAKGIY
     PAVDPLDSTS TMLQPWIVGE EHYETAQGVK QTLQRYKELQ DIIAIPGLDE LSEEDRLTVA
     RARRIERFLS QPFFVAEVFT GSPGKYVSLR ETIKGFQMIL AGELDNLPEQ AFYLVGNIDE
     VAAKAVVSQS GD