ID   A0A290DR72_9ASPA        Unreviewed;       495 AA.
AC   A0A290DR72;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   05-DEC-2018, entry version 6.
DE   RecName: Full=ATP synthase subunit beta, chloroplastic {ECO:0000256|HAMAP-Rule:MF_01347};
DE            EC=7.1.2.2 {ECO:0000256|HAMAP-Rule:MF_01347};
DE   AltName: Full=ATP synthase F1 sector subunit beta {ECO:0000256|HAMAP-Rule:MF_01347};
DE   AltName: Full=F-ATPase subunit beta {ECO:0000256|HAMAP-Rule:MF_01347};
GN   Name=atpB {ECO:0000256|HAMAP-Rule:MF_01347,
GN   ECO:0000313|EMBL:ATB18925.1};
OS   Hosta minor.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:ATB18925.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Asparagales; Asparagaceae;
OC   Agavoideae; Hosta.
OX   NCBI_TaxID=1035810 {ECO:0000313|EMBL:ATB18925.1};
RN   [1] {ECO:0000313|EMBL:ATB18925.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Park H., Kim C., Kim J.-H.;
RT   "The comparative plastid genome analysis and its phylogenetic
RT   implication on Asparagaceae s.l.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton
CC       gradient across the membrane. The catalytic sites are hosted
CC       primarily by the beta subunits. {ECO:0000256|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;
CC         EC=7.1.2.2; Evidence={ECO:0000256|HAMAP-Rule:MF_01347,
CC         ECO:0000256|RuleBase:RU003553};
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
CC       core - and CF(0) - the membrane proton channel. CF(1) has five
CC       subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0)
CC       has four main subunits: a(1), b(1), b'(1) and c(9-12).
CC       {ECO:0000256|HAMAP-Rule:MF_01347, ECO:0000256|RuleBase:RU004289}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000256|HAMAP-Rule:MF_01347}; Peripheral membrane protein
CC       {ECO:0000256|HAMAP-Rule:MF_01347}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000256|HAMAP-Rule:MF_01347}.
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DR   EMBL; KX822777; ATB18925.1; -; Genomic_DNA.
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:0015986; P:ATP synthesis coupled proton transport; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.1140.10; -; 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 {ECO:0000256|HAMAP-Rule:MF_01347,
KW   ECO:0000256|RuleBase:RU003553};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01347,
KW   ECO:0000256|RuleBase:RU003553};
KW   CF(1) {ECO:0000256|HAMAP-Rule:MF_01347,
KW   ECO:0000256|RuleBase:RU003553};
KW   Chloroplast {ECO:0000313|EMBL:ATB18925.1};
KW   Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01347};
KW   Ion transport {ECO:0000256|HAMAP-Rule:MF_01347};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01347};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01347,
KW   ECO:0000256|RuleBase:RU003553};
KW   Plastid {ECO:0000313|EMBL:ATB18925.1};
KW   Thylakoid {ECO:0000256|HAMAP-Rule:MF_01347};
KW   Translocase {ECO:0000256|HAMAP-Rule:MF_01347};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01347}.
FT   DOMAIN      164    356       AAA. {ECO:0000259|SMART:SM00382}.
FT   NP_BIND     172    179       ATP. {ECO:0000256|HAMAP-Rule:MF_01347}.
SQ   SEQUENCE   495 AA;  53299 MW;  727EB9E2E462AE50 CRC64;
     MKINPTTSGP AVSTLEEKNL GRIAQIIGPV LDVVFPPGKM PNIYNALVVK GRDTVGQQIN
     VTCEVQQLLG NNRVRAVAMS ATDGLTRGME VIDTGAALSV PVGGATLGRI FNVLGEPVDN
     LGPVDTRTTS PIHRSAPAFI QLDTKLSIFE TGIKVVDLLA PYRRGGKIGL FGGAGVGKTV
     LIMELINNIA KAHGGVSVFG GVGERTREGN DLYMEMKESG VINEKNIAES KVALVYGQMN
     EPPGARMRVG LTALTMAEYF RDVNEQDVLL FIDNIFRFVQ AGSEVSALLG RMPSAVGYQP
     TLSTEMGSLQ ERITSTKEGS ITSIQAVYVP ADDLTDPAPA TTFAHLDATT VLSRGLAAKG
     IYPAVDPLDS TSTMLQPRIV GEEHYETAQR VKQTLQRYKE LQDIIAILGL DELSEEDRLT
     VARARKIERF LSQPFFVAEV FTGSPGKYVG LAETIRGFQL ILSGELDSLP EQAFYLVGNI
     DEATAKAMNL EGEKK
//