ID C6ZQ17_9ERIC Unreviewed; 465 AA.
AC C6ZQ17;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=ATP synthase subunit beta {ECO:0000256|RuleBase:RU003553};
DE EC=7.1.2.2 {ECO:0000256|RuleBase:RU003553};
DE Flags: Fragment;
GN Name=atpB {ECO:0000313|EMBL:ACL99423.1};
OS Diospyros cherrieri.
OG Plastid {ECO:0000313|EMBL:ACL99423.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; Ericales; Ebenaceae; Diospyros.
OX NCBI_TaxID=589114 {ECO:0000313|EMBL:ACL99423.1};
RN [1] {ECO:0000313|EMBL:ACL99423.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=19427384; DOI=10.1016/j.ympev.2009.04.021;
RA Duangjai S., Samuel R., Munzinger J., Forest F., Wallnofer B.,
RA Barfuss M.H., Fischer G., Chase M.W.;
RT "A multi-locus plastid phylogenetic analysis of the pantropical genus
RT Diospyros (Ebenaceae), with an emphasis on the radiation and biogeographic
RT origins of the New Caledonian endemic species.";
RL Mol. Phylogenet. Evol. 52:602-620(2009).
RN [2] {ECO:0000313|EMBL:AGR87999.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BT262 {ECO:0000313|EMBL:AGR87999.1}, and BT297
RC {ECO:0000313|EMBL:AGR88000.1};
RX PubMed=23850609; DOI=10.1016/j.ympev.2013.07.002;
RA Turner B., Munzinger J., Duangjai S., Temsch E.M., Stockenhuber R.,
RA Barfuss M.H., Chase M.W., Samuel R.;
RT "Molecular phylogenetics of New Caledonian Diospyros (Ebenaceae) using
RT plastid and nuclear markers.";
RL Mol. Phylogenet. Evol. 69:740-763(2013).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. {ECO:0000256|RuleBase:RU003553}.
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:0000256|ARBA:ARBA00001741,
CC ECO:0000256|RuleBase:RU003553};
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).
CC {ECO:0000256|RuleBase:RU003553}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000256|ARBA:ARBA00008936}.
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DR EMBL; EU980818; ACL99423.1; -; Genomic_DNA.
DR EMBL; EU980819; ACL99424.1; -; Genomic_DNA.
DR EMBL; KF291803; AGR87999.1; -; Genomic_DNA.
DR EMBL; KF291804; AGR88000.1; -; Genomic_DNA.
DR AlphaFoldDB; C6ZQ17; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
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-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR CDD; cd18110; ATP-synt_F1_beta_C; 1.
DR CDD; cd18115; ATP-synt_F1_beta_N; 1.
DR CDD; cd01133; F1-ATPase_beta_CD; 1.
DR Gene3D; 2.40.10.170; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR01039; atpD; 1.
DR PANTHER; PTHR15184; ATP SYNTHASE; 1.
DR PANTHER; PTHR15184:SF71; ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF50615; N-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310,
KW ECO:0000256|RuleBase:RU003553};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003553};
KW CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|RuleBase:RU003553};
KW Chloroplast {ECO:0000313|EMBL:AGR87999.1};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003553}; Plastid {ECO:0000313|EMBL:ACL99423.1};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 144..336
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACL99423.1"
FT NON_TER 465
FT /evidence="ECO:0000313|EMBL:ACL99423.1"
SQ SEQUENCE 465 AA; 50098 MW; D649B7FBAECDB044 CRC64;
GRIVQIIGPV LDVAFPPGKM PNIYNALVIK GRDTVGQPIN VTCEVQQLLG NNRVRAVAMS
ATDGLTRGME VIDTGAPLSV PVGGVTLGRI FNVLGEPVDN LGPVDTRTTS PIHRSAPAFI
QLDTKLSIFE TGIKVVDLLA PYRRGGKIGL FGGAGVGKTV LIMELINNIA KAHGGVSVFG
GVGERTREGN DLYMEMKESG VINEQNIAES KVALVYGQMN EPPGARMRVG LTALTMAEYF
RDVNEQDVLL FIDNIFRFVQ AGSEVSALLG RMPSAVGYQP TLSTEMGSLQ ERITSTKEGS
ITSIQAVYVP ADDLTDPAPA TTFAHLDATT VLSRGLAAKG IYPAVDPLDS TSTMLQPRIV
GEEHYETAQR VKQTLQRYKE LQDIIAILGL DELSEEDRLT VARARKIERF LSQPFFVAEV
FTGSPGKYVG LAETIRGFQL IFSGELDGLP EQAFYLVGNI DEATA
//
