ATPB_CHAGL
ID ATPB_CHAGL Reviewed; 493 AA.
AC Q8SLY2;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 104.
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 Chaetosphaeridium globosum (Charophycean green alga) (Herposteiron
OS globosum).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Coleochaetophyceae; Coleochaetales;
OC Chaetosphaeridiaceae; Chaetosphaeridium.
OX NCBI_TaxID=96477;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1311;
RX PubMed=12161560; DOI=10.1073/pnas.162203299;
RA Turmel M., Otis C., Lemieux C.;
RT "The chloroplast and mitochondrial genome sequences of the charophyte
RT Chaetosphaeridium globosum: insights into the timing of the events that
RT restructured organelle DNAs within the green algal lineage that led to land
RT plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:11275-11280(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 69-467.
RC STRAIN=SAG 26.98;
RX PubMed=11743201; DOI=10.1126/science.1065156;
RA Karol K.G., McCourt R.M., Cimino M.T., Delwiche C.F.;
RT "The closest living relatives of land plants.";
RL Science 294:2351-2353(2001).
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; AF494278; AAM96500.1; -; Genomic_DNA.
DR EMBL; AF408792; AAL83520.1; -; Genomic_DNA.
DR RefSeq; NP_683810.1; NC_004115.1.
DR AlphaFoldDB; Q8SLY2; -.
DR SMR; Q8SLY2; -.
DR PRIDE; Q8SLY2; -.
DR GeneID; 860669; -.
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_0000144503"
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; 52945 MW; 14D246163AEA638C CRC64;
MINSSFILLA STVTSKKVGR ITQIIGPVMD VAFPSGNMPN IYNALVVKGK NAAGQDIDVT
CEVQQLLGDN KVRAVAMSAT DGLMRGMDVI DTGSALSVPV GEVTLGRIFN VLGEPVDNMG
PVNATVTSPI HRSAPAFTQL DTKLSIFETG IKVVDLLAPY RRGGKIGLFG GAGVGKTVLI
MELINNIAKA HGGVSVFGGV GERTREGNDL YMEMKESKVI NEENLGESKV ALVYGQMNEP
PGARMRVGLT ALTMAEYFRD VNKQDVLLFI DNIFRFVQAG SEVSALLGRM PSAVGYQPTL
STEMGGLQER ITSTKEGSIT SIQAVYVPAD DLTDPAPATT FAHLDATTVL SRGLAAKGIY
PAVDPLDSTS TMLQPWIVGE EHYETAQGVK KTLQRYKELQ DIIAILGLDE LSEEDRLLVA
RARKIERFLS QPFFVAEVFT GSPGKYVSLV ETIKGFQMIL SGDLDSLPEQ AFYLVGNIDE
ATAKAATLQV ENS