ATPB_SPIOL
ID ATPB_SPIOL Reviewed; 498 AA.
AC P00825; Q6EYW8;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 160.
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 Spinacia oleracea (Spinach).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16593238; DOI=10.1073/pnas.79.20.6260;
RA Zurawski G., Bottomley W., Whitfeld P.R.;
RT "Structures of the genes for the beta and epsilon subunits of spinach
RT chloroplast ATPase indicate a dicistronic mRNA and an overlapping
RT translation stop/start signal.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:6260-6264(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1531962; DOI=10.1016/0014-5793(92)80024-b;
RA Chen Z., Wu I., Richter M.L., Gegenheimer P.;
RT "Over-expression and refolding of beta-subunit from the chloroplast ATP
RT synthase.";
RL FEBS Lett. 298:69-73(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Graham S.W., Rai H.S., Ikegami K., Reeves P.A., Olmstead R.G.;
RT "Parsing out signal and noise for seed-plant phylogenetic inference.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Geant d'hiver, and cv. Monatol;
RX PubMed=11292076; DOI=10.1023/a:1006478403810;
RA Schmitz-Linneweber C., Maier R.M., Alcaraz J.-P., Cottet A., Herrmann R.G.,
RA Mache R.;
RT "The plastid chromosome of spinach (Spinacia oleracea): complete nucleotide
RT sequence and gene organization.";
RL Plant Mol. Biol. 45:307-315(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 313-354.
RX PubMed=1426274; DOI=10.1016/0014-5793(92)81191-n;
RA Michel L., Garin J., Girault G., Vignais P.V.;
RT "Photolabeling of the phosphate binding site of chloroplast coupling factor
RT 1 with [32P]azidonitrophenyl phosphate.";
RL FEBS Lett. 313:90-93(1992).
RN [6]
RP CHARACTERIZATION.
RX PubMed=1832378; DOI=10.1111/j.1432-1033.1991.tb16203.x;
RA Horbach M., Meyer H.E., Bickel-Sandkoetter S.;
RT "Inactivation of chloroplast H(+)-ATPase by modification of Lys beta 359,
RT Lys alpha 176 and Lys alpha 266.";
RL Eur. J. Biochem. 200:449-456(1991).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 19-485 IN COMPLEX WITH ALPHA
RP CHAIN.
RX PubMed=11032839; DOI=10.1074/jbc.m008015200;
RA Groth G., Pohl E.;
RT "The structure of the chloroplast F1-ATPase at 3.2 A resolution.";
RL J. Biol. Chem. 276:1345-1352(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.
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; J01441; AAA84626.1; -; Genomic_DNA.
DR EMBL; U23082; AAB60294.1; -; Genomic_DNA.
DR EMBL; AF528861; AAQ09249.1; -; Genomic_DNA.
DR EMBL; AJ400848; CAB88736.1; -; Genomic_DNA.
DR PIR; A01028; PWSPB.
DR RefSeq; NP_054943.1; NC_002202.1.
DR PDB; 1FX0; X-ray; 3.20 A; B=1-498.
DR PDB; 1KMH; X-ray; 3.40 A; B=1-498.
DR PDB; 6FKF; EM; 3.10 A; B/D/F=1-498.
DR PDB; 6FKH; EM; 4.20 A; B/D/F=1-498.
DR PDB; 6FKI; EM; 4.30 A; B/D/F=1-498.
DR PDB; 6VM1; EM; 7.90 A; D/E/F=1-498.
DR PDB; 6VM4; EM; 7.08 A; D/E/F=1-498.
DR PDB; 6VMB; EM; 5.23 A; D/E/F=1-498.
DR PDB; 6VMD; EM; 4.53 A; D/E/F=1-498.
DR PDB; 6VMG; EM; 6.46 A; D/E/F=1-498.
DR PDB; 6VOF; EM; 4.51 A; D/E/F=1-498.
DR PDB; 6VOG; EM; 4.35 A; D/E/F=1-498.
DR PDB; 6VOH; EM; 4.16 A; D/E/F=1-498.
DR PDB; 6VOI; EM; 4.03 A; D/E/F=1-498.
DR PDB; 6VOJ; EM; 4.34 A; D/E/F=1-498.
DR PDB; 6VOK; EM; 3.85 A; D/E/F=1-498.
DR PDB; 6VOL; EM; 4.06 A; D/E/F=1-498.
DR PDB; 6VOM; EM; 3.60 A; D/E/F=1-498.
DR PDB; 6VON; EM; 3.35 A; D/E/F=1-498.
DR PDB; 6VOO; EM; 3.05 A; D/E/F=1-498.
DR PDBsum; 1FX0; -.
DR PDBsum; 1KMH; -.
DR PDBsum; 6FKF; -.
DR PDBsum; 6FKH; -.
DR PDBsum; 6FKI; -.
DR PDBsum; 6VM1; -.
DR PDBsum; 6VM4; -.
DR PDBsum; 6VMB; -.
DR PDBsum; 6VMD; -.
DR PDBsum; 6VMG; -.
DR PDBsum; 6VOF; -.
DR PDBsum; 6VOG; -.
DR PDBsum; 6VOH; -.
DR PDBsum; 6VOI; -.
DR PDBsum; 6VOJ; -.
DR PDBsum; 6VOK; -.
DR PDBsum; 6VOL; -.
DR PDBsum; 6VOM; -.
DR PDBsum; 6VON; -.
DR PDBsum; 6VOO; -.
DR AlphaFoldDB; P00825; -.
DR SMR; P00825; -.
DR IntAct; P00825; 1.
DR MINT; P00825; -.
DR STRING; 3562.P00825; -.
DR ChEMBL; CHEMBL2366567; -.
DR PRIDE; P00825; -.
DR GeneID; 2715576; -.
DR KEGG; soe:2715576; -.
DR OrthoDB; 495235at2759; -.
DR EvolutionaryTrace; P00825; -.
DR PRO; PR:P00825; -.
DR Proteomes; UP000054095; Chloroplast.
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 1: Evidence at protein level;
KW 3D-structure; ATP synthesis; ATP-binding; CF(1); Chloroplast;
KW Hydrogen ion transport; Ion transport; Membrane; Nucleotide-binding;
KW Plastid; Reference proteome; Thylakoid; Translocase; Transport.
FT CHAIN 1..498
FT /note="ATP synthase subunit beta, chloroplastic"
FT /id="PRO_0000144550"
FT BINDING 172..179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
FT CONFLICT 32
FT /note="D -> N (in Ref. 1; AAA84626)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="A -> P (in Ref. 1; AAA84626)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="G -> R (in Ref. 1; AAA84626)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="D -> N (in Ref. 1; AAA84626)"
FT /evidence="ECO:0000305"
FT STRAND 19..27
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 58..70
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 73..80
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:6FKF"
FT TURN 105..108
FT /evidence="ECO:0007829|PDB:1FX0"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:1FX0"
FT HELIX 154..158
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 178..191
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 196..204
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 206..218
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 231..238
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 243..262
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 267..273
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 275..288
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 302..310
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 320..326
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:1FX0"
FT HELIX 337..345
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 347..352
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 354..359
FT /evidence="ECO:0007829|PDB:6FKF"
FT TURN 367..369
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 371..374
FT /evidence="ECO:0007829|PDB:6FKF"
FT TURN 377..379
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 382..400
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 402..405
FT /evidence="ECO:0007829|PDB:6FKF"
FT TURN 406..408
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 415..430
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 436..438
FT /evidence="ECO:0007829|PDB:6FKF"
FT TURN 439..442
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 451..462
FT /evidence="ECO:0007829|PDB:6FKF"
FT TURN 463..468
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 471..473
FT /evidence="ECO:0007829|PDB:6FKF"
FT TURN 474..476
FT /evidence="ECO:0007829|PDB:1FX0"
FT HELIX 480..494
FT /evidence="ECO:0007829|PDB:6FKF"
SQ SEQUENCE 498 AA; 53745 MW; 77C8E00EF4B667F6 CRC64;
MRINPTTSDP GVSTLEKKNL GRIAQIIGPV LDVAFPPGKM PNIYNALIVK GRDTAGQPMN
VTCEVQQLLG NNRVRAVAMS ATDGLTRGME VIDTGAPLSV PVGGATLGRI FNVLGEPVDN
LGPVDTRTTS PIHRSAPAFT QLDTKLSIFE TGIKVVDLLA PYRRGGKIGL FGGAGVGKTV
LIMELINNIA KAHGGVSVFG GVGERTREGN DLYMEMKESG VINEQNIAES KVALVYGQMN
EPPGARMRVG LTALTMAEYF RDVNEQDVLL FIDNIFRFVQ AGSEVSALLG RMPSAVGYQP
TLSTEMGSLQ ERITSTKEGS ITSIQAVYVP ADDLTDPAPA TTFAHLDATT VLSRGLAAKG
IYPAVDPLDS TSTMLQPRIV GEEHYEIAQR VKETLQRYKE LQDIIAILGL DELSEEDRLT
VARARKIERF LSQPFFVAEV FTGSPGKYVG LAETIRGFQL ILSGELDSLP EQAFYLVGNI
DEATAKAMNL EMESKLKK
