ATPB_ADICA
ID ATPB_ADICA Reviewed; 493 AA.
AC O03062;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 4.
DT 03-AUG-2022, entry version 123.
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 Adiantum capillus-veneris (Maidenhair fern).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Polypodiopsida; Polypodiidae; Polypodiales; Pteridineae; Pteridaceae;
OC Vittarioideae; Adiantum.
OX NCBI_TaxID=13818;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Wolf P.G.;
RT "Evaluation of atpB nucleotide sequences for phylogenetic studies of ferns
RT and other pteridophytes.";
RL Am. J. Bot. 84:1429-1440(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
RX PubMed=12755170; DOI=10.1093/dnares/10.2.59;
RA Wolf P.G., Rowe C.A., Sinclair R.B., Hasebe M.;
RT "Complete nucleotide sequence of the chloroplast genome from a
RT leptosporangiate fern, Adiantum capillus-veneris L.";
RL DNA Res. 10:59-65(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND RNA EDITING.
RC TISSUE=Frond;
RX PubMed=15363849; DOI=10.1016/j.gene.2004.06.018;
RA Wolf P.G., Rowe C.A., Hasebe M.;
RT "High levels of RNA editing in a vascular plant chloroplast genome:
RT analysis of transcripts from the fern Adiantum capillus-veneris.";
RL Gene 339:89-97(2004).
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 -!- RNA EDITING: Modified_positions=6 {ECO:0000269|PubMed:15363849}, 77
CC {ECO:0000269|PubMed:15363849}, 181 {ECO:0000269|PubMed:15363849}, 183
CC {ECO:0000269|PubMed:15363849}, 214 {ECO:0000269|PubMed:15363849}, 249
CC {ECO:0000269|PubMed:15363849}, 461 {ECO:0000269|PubMed:15363849};
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|HAMAP-Rule:MF_01347}.
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DR EMBL; AY178864; AAB51749.3; -; Genomic_DNA.
DR RefSeq; NP_848067.2; NC_004766.1.
DR AlphaFoldDB; O03062; -.
DR SMR; O03062; -.
DR PRIDE; O03062; -.
DR GeneID; 807342; -.
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 2: Evidence at transcript level;
KW ATP synthesis; ATP-binding; CF(1); Chloroplast; Hydrogen ion transport;
KW Ion transport; Membrane; Nucleotide-binding; Plastid; RNA editing;
KW Thylakoid; Translocase; Transport.
FT CHAIN 1..493
FT /note="ATP synthase subunit beta, chloroplastic"
FT /id="PRO_0000144490"
FT BINDING 170..177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ SEQUENCE 493 AA; 53026 MW; 7B2B1FF008A0BF1B CRC64;
MKISSLLFEI SELVEKNVGY ITQIIGPVLD VAFSPGEMPS IYNSLVVKGR NSAGQEINVT
CEVQQLLGNN EVRAVAMSAT DGLMRGMGAV DTGAPLSVPV GETTLGRIFN VLGEPVDNLG
PVQNSATFPI HRSAPAFTQL DTKLSIFETG IKVVDLLAPY RRGGKIGLFG GAGVGKTVLI
MELINNIAKA HGGVSVFGGV GERTREGNDL YMEMKESKVI NEQNISESKV ALVYGQMNEP
PGARMRVGLT ALTMAEYFRD INKRDVLLFI DNIFRFVQAG SEVSALLGRM PSAVGYQPTL
GTEMGSLQER ITSTKEGSIT SIQAVYVPAD DLTDPAPATT FAHLDATTVL SRGLAAKGIY
PAVDPLDSTS TMLQPWIVGE EHYETAQGVK QTLQRYKELQ DIIAILGLDE LSEEDRLTVA
RARKIERFLS QPFFVAEVFT GSPGKYVSLP ETIKGFQMIL SGELDNLPEQ AFYLVGNIDE
AAAKAAALQA GGQ
