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ATPB_DENPU
ID   ATPB_DENPU              Reviewed;         486 AA.
AC   O03068;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 2.
DT   03-AUG-2022, entry version 108.
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};
DE   Flags: Fragment;
GN   Name=atpB {ECO:0000255|HAMAP-Rule:MF_01347};
OS   Dennstaedtia punctilobula (Hay-scented fern) (Nephrodium punctilobum).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Polypodiopsida; Polypodiidae; Polypodiales; Dennstaedtiineae;
OC   Dennstaedtiaceae; Dennstaedtia.
OX   NCBI_TaxID=32088;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
RA   Wolf P.G., Su P.-H.;
RL   Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 240-454.
RC   TISSUE=Frond;
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).
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; U93836; AAB51744.2; -; Genomic_DNA.
DR   AlphaFoldDB; O03068; -.
DR   SMR; O03068; -.
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-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); Chloroplast; Hydrogen ion transport;
KW   Ion transport; Membrane; Nucleotide-binding; Plastid; Thylakoid;
KW   Translocase; Transport.
FT   CHAIN           <1..486
FT                   /note="ATP synthase subunit beta, chloroplastic"
FT                   /id="PRO_0000144509"
FT   BINDING         154..161
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
FT   NON_TER         1
SQ   SEQUENCE   486 AA;  51878 MW;  321B1528A103197F CRC64;
     NVGYITQIIG PVLDVAFSPG EMPNIYNSLV VKGQNPAGQD INVTCEVQQL LGNNEVRAVA
     TSATDGLMRG MGAVDTGAPL SVPVGETTLG RISNVLGEPV DNPGPVQSNT TFPIHRSAPA
     FTQLDTKLST FETGIKVVDL LAPYRRGGKI GLFGGAGVGK TVPITELINN IAKAHGGVSV
     SGGVGERTRE GNDLYMEMKE SKVINEQNIS ESKVALVYGQ MNEPPGARMR VGSTASTMAE
     YFRDVNKQDV PLFIDNILRF VQAGSEVSAL LGRMPSAVGY QPTLGTEMGS LQERITSTKE
     GSITSIQAVY VPADDLTDPA PATTSAHLDA TTVLSRGLAA KGIYPAVDPL DSTSTMSQPW
     IVGEEHYETA QGVKQTSQRY KELQDIIAIL GLDELSEEDR LTVARARKIE RFSSQPFLVA
     EVFTGSPGKY VSLPETIKGF QMILPGELDN LPEQASYLAG NVDEATAKAA ALQVEGQRKG
     WYRIFA
 
 
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