ATPB_CHAVU
ID ATPB_CHAVU Reviewed; 493 AA.
AC Q1ACK1;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 76.
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 Chara vulgaris (Common stonewort).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Charophyceae; Charales; Characeae;
OC Chara.
OX NCBI_TaxID=55564;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16611644; DOI=10.1093/molbev/msk018;
RA Turmel M., Otis C., Lemieux C.;
RT "The chloroplast genome sequence of Chara vulgaris sheds new light into the
RT closest green algal relatives of land plants.";
RL Mol. Biol. Evol. 23:1324-1338(2006).
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; DQ229107; ABA61929.1; -; Genomic_DNA.
DR RefSeq; YP_635746.1; NC_008097.1.
DR AlphaFoldDB; Q1ACK1; -.
DR SMR; Q1ACK1; -.
DR GeneID; 4100216; -.
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..493
FT /note="ATP synthase subunit beta, chloroplastic"
FT /id="PRO_0000254459"
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; 53487 MW; 15B032775232B01F CRC64;
MTTVNLDLQN SLVAEKNRGK ITQIIGPVMD ISFLPGQMPN IYNCLTVKGK NASGDFIDVT
CEVQQLLGDN KVRAVAMSAT DGLMRGMEVI DTGSPLSVPV GETTLGRIFN VLGEPVDNLG
PVDTSITFPI HRAAPAFTQL DTKLSIFETG IKVVDLLAPY RRGGKIGLFG GAGVGKTVLI
MELINNIAKA HGGVSVFGGV GERTREGNDL YMEMKESKVI NEENISESKV ALVYGQMNEP
PGARMRVGLT ALTMAEYFRD VNKQDVLLFI DNIFRFVQAG SEVSALLGRM PSAVGYQPTL
STEMGTLQER ITSTKEGSIT SIQAVYVPAD DLTDPAPATT FAHLDATTVL SRNLAAKGIY
PAVDPLDSTS TMLQPWIVGE EHYETAQGVK ETLQRYKELQ DIIAILGLDE LSEEDRLIVA
RARKIERFLS QPFFVAEVFT GSPGKYVSLI DTIKGFQMIL SGELDHLPEQ AFYLVGDIEE
ATAKAATIQV QSE
