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ATP synthase subunit beta, chloroplastic (EC 3.6.3.14) (ATP synthase F1 sector subunit beta) (F-ATPase subunit beta)

 G8IUE9_PINRO            Unreviewed;       492 AA.
G8IUE9;
25-JAN-2012, integrated into UniProtKB/TrEMBL.
25-JAN-2012, sequence version 1.
18-JUL-2018, entry version 42.
RecName: Full=ATP synthase subunit beta, chloroplastic {ECO:0000256|HAMAP-Rule:MF_01347};
EC=3.6.3.14 {ECO:0000256|HAMAP-Rule:MF_01347};
AltName: Full=ATP synthase F1 sector subunit beta {ECO:0000256|HAMAP-Rule:MF_01347};
AltName: Full=F-ATPase subunit beta {ECO:0000256|HAMAP-Rule:MF_01347};
Name=atpB {ECO:0000256|HAMAP-Rule:MF_01347,
ECO:0000313|EMBL:AET45820.1};
ORFNames=PCL_12635 {ECO:0000313|EMBL:AET45820.1};
Pinus roxburghii (Chir pine).
Plastid; Chloroplast {ECO:0000313|EMBL:AET45820.1}.
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Pinidae; Pinales; Pinaceae; Pinus; Pinus.
NCBI_TaxID=71650 {ECO:0000313|EMBL:AET45820.1};
[1] {ECO:0000313|EMBL:AET45820.1}
NUCLEOTIDE SEQUENCE.
STRAIN=ROXB04 {ECO:0000313|EMBL:AET45820.1};
PubMed=22731878; DOI=10.1186/1471-2148-12-100;
Parks M., Cronn R., Liston A.;
"Separating the wheat from the chaff: mitigating the effects of noise
in a plastome phylogenomic data set from Pinus L. (Pinaceae).";
BMC Evol. Biol. 12:100-100(2012).
-!- FUNCTION: Produces ATP from ADP in the presence of a proton
gradient across the membrane. The catalytic sites are hosted
primarily by the beta subunits. {ECO:0000256|HAMAP-Rule:MF_01347}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate +
H(+)(Out). {ECO:0000256|HAMAP-Rule:MF_01347,
ECO:0000256|RuleBase:RU003553}.
-!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
core - and CF(0) - the membrane proton channel. CF(1) has five
subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0)
has four main subunits: a(1), b(1), b'(1) and c(9-12).
{ECO:0000256|HAMAP-Rule:MF_01347, ECO:0000256|RuleBase:RU004289}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
{ECO:0000256|HAMAP-Rule:MF_01347}; Peripheral membrane protein
{ECO:0000256|HAMAP-Rule:MF_01347}.
-!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
{ECO:0000256|HAMAP-Rule:MF_01347}.
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EMBL; JN854162; AET45820.1; -; Genomic_DNA.
GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:UniProtKB-UniRule.
Gene3D; 1.10.1140.10; -; 1.
HAMAP; MF_01347; ATP_synth_beta_bact; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR005722; ATP_synth_F1_bsu.
InterPro; IPR020003; ATPase_a/bsu_AS.
InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
InterPro; IPR024034; ATPase_F1/V1_b/a_C.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF00006; ATP-synt_ab; 1.
Pfam; PF02874; ATP-synt_ab_N; 1.
SMART; SM00382; AAA; 1.
SUPFAM; SSF50615; SSF50615; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR01039; atpD; 1.
PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
3: Inferred from homology;
ATP synthesis {ECO:0000256|HAMAP-Rule:MF_01347,
ECO:0000256|RuleBase:RU003553};
ATP-binding {ECO:0000256|HAMAP-Rule:MF_01347,
ECO:0000256|RuleBase:RU003553};
CF(1) {ECO:0000256|HAMAP-Rule:MF_01347,
ECO:0000256|RuleBase:RU003553};
Chloroplast {ECO:0000313|EMBL:AET45820.1};
Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01347};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_01347};
Ion transport {ECO:0000256|HAMAP-Rule:MF_01347};
Membrane {ECO:0000256|HAMAP-Rule:MF_01347};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01347,
ECO:0000256|RuleBase:RU003553}; Plastid {ECO:0000313|EMBL:AET45820.1};
Thylakoid {ECO:0000256|HAMAP-Rule:MF_01347};
Transport {ECO:0000256|HAMAP-Rule:MF_01347}.
DOMAIN 162 354 AAA. {ECO:0000259|SMART:SM00382}.
NP_BIND 170 177 ATP. {ECO:0000256|HAMAP-Rule:MF_01347}.
SEQUENCE 492 AA; 52917 MW; 2CD3CCEC94687DCE CRC64;
MRKNPLVLGV SARVEKNVGR IAQIIGPVLD VSFPPGNMPN IYNSLIVKGQ GTAGQEIQVT
CEVQQLLGNH KVRAVAMSAT DGLTRGMRVI DTGAPLSVPV GGATLGRIFN VLGEPVDNLG
PVDACITSPI HRPAPAFTEL DTKLSIFETG IKVVDLLAPY RRGGKIGLFG GAGVGKTVLI
MELINNIAKA HGGVSVFGGV GERTREGNDL YMEMKESGVI DEQKISESKV ALVYGQMNEP
PGARMRVGLT ALTMAEYFRD VNEQDVLLFI DNIFRFVQAG SEVSALLGRM PSAVGYQPTL
STEMGSLQER ITSTKKGSIT SIQAVYVPAD DLTDPAPATT FAHSDATTVL SRGLAAKGIY
PAVDPLDSTS TMLQPWIVGE EHYETAQGVK QTLQRYKELQ DIIAIPGLDE LSEEDRLIVA
RARKIERFLS QPFFVAEVFT GSPGKYVGLM ETIRGFQMIL SGELDGLIEQ SFYLVGNIDE
ATAKAINSNM ES


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