ATPB_VITVI
ID ATPB_VITVI Reviewed; 498 AA.
AC Q0ZJ13;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
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 Vitis vinifera (Grape).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Maxxa;
RX PubMed=16603088; DOI=10.1186/1471-2148-6-32;
RA Jansen R.K., Kaittanis C., Lee S.-B., Saski C., Tomkins J., Alverson A.J.,
RA Daniell H.;
RT "Phylogenetic analyses of Vitis (Vitaceae) based on complete chloroplast
RT genome sequences: effects of taxon sampling and phylogenetic methods on
RT resolving relationships among rosids.";
RL BMC Evol. Biol. 6:32-32(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ424856; ABE47541.1; -; Genomic_DNA.
DR RefSeq; YP_567083.1; NC_007957.1.
DR AlphaFoldDB; Q0ZJ13; -.
DR SMR; Q0ZJ13; -.
DR STRING; 29760.VIT_00s0332g00060.t01; -.
DR PRIDE; Q0ZJ13; -.
DR GeneID; 4025008; -.
DR KEGG; vvi:4025008; -.
DR eggNOG; KOG1350; Eukaryota.
DR InParanoid; Q0ZJ13; -.
DR OrthoDB; 495235at2759; -.
DR Proteomes; UP000009183; Chloroplast.
DR ExpressionAtlas; Q0ZJ13; baseline and differential.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IBA:GO_Central.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central.
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 GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IBA:GO_Central.
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; Reference proteome;
KW Thylakoid; Translocase; Transport.
FT CHAIN 1..498
FT /note="ATP synthase subunit beta, chloroplastic"
FT /id="PRO_0000254531"
FT BINDING 172..179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ SEQUENCE 498 AA; 53743 MW; E7E39222B7EE72B7 CRC64;
MRINPTTSGP GVSTLEKKNL GRIAQIIGPV LDVAFPPGKM PNIYNALVVK GRDTVGQQIN
VTCEVQQLLG NNRVRAVAMS ATDGLMRGME VIDTGAPLSV PVGGATLGRI FNVLGEPVDN
LGPVDTRTTS PIHRSAPAFI QLDTKLSIFE TGIKVVDLLA PYRRGGKIGL FGGAGVGKTV
LIMELINNIA KAHGGVSVFG GVGERTREGN DLYMEMKESG VINEKNISES KVALVYGQMN
EPPGARMRVG LTALTMAEYF RDVNEQDVLL FIDNIFRFVQ AGSEVSALLG RMPSAVGYQP
TLSTEMGTLQ ERITSTKEGS ITSIQAVYVP ADDLTDPAPA TTFAHLDATT VLSRGLAAKG
IYPAVDPLDS TSTMLQPRIV GEEHYETAQR VKQTLQRYKE LQDIIAILGL DELSEEDRLT
VARARKIERF LSQPFFVAEV FTGSPGKYVG LAETIRGFQL ILSGELDGLP EQAFYLVGNI
DEATAKAMNL EMESKLKK