ID C8XPL7_9MONI Unreviewed; 394 AA.
AC C8XPL7;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 62.
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:ABU93538.1};
OS Dryopteris diffracta.
OG Plastid; Chloroplast {ECO:0000313|EMBL:ABU93538.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Polypodiopsida; Polypodiidae; Polypodiales; Polypodiineae; Dryopteridaceae;
OC Dryopteridoideae; Dryopteris.
OX NCBI_TaxID=385352 {ECO:0000313|EMBL:ABU93538.1};
RN [1] {ECO:0000313|EMBL:ABU93538.1}
RP NUCLEOTIDE SEQUENCE.
RX AGRICOLA=IND43981165; DOI=10.1086/521710;
RA Liu H.-M., Zhang X.-C., Wang W., Qiu Y.-L., Chen Z.-D.;
RT "Molecular phylogeny of the fern family Dryopteridaceae inferred from
RT chloroplast rbcL and atpB genes.";
RL Int. J. Plant Sci. 168:1311-1323(2007).
RN [2] {ECO:0000313|EMBL:ABU93538.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17955187; DOI=10.1007/s11427-007-0099-9;
RA Liu H., Zhang X., Chen Z., Dong S., Qiu Y.;
RT "Polyphyly of the fern family Tectariaceae sensu Ching: insights from cpDNA
RT sequence data.";
RL Sci. China, Ser. C, Life Sci. 50:789-798(2007).
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; EF450504; ABU93538.1; -; Genomic_DNA.
DR AlphaFoldDB; C8XPL7; -.
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; 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; 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 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:0000256|ARBA:ARBA00022528, ECO:0000313|EMBL:ABU93538.1};
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};
KW Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000313|EMBL:ABU93538.1};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 93..285
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABU93538.1"
FT NON_TER 394
FT /evidence="ECO:0000313|EMBL:ABU93538.1"
SQ SEQUENCE 394 AA; 42120 MW; B0AB44E691A4B9B0 CRC64;
NEVRAVAMSA TDGLMRGMGA VDTGAPLSVP VGETTLGRIS NVLGEPVDNL GPVRSSATFP
IHRPAPAFTQ LDTKLSIFET GIKVVDLLAP YRRGGKIGLL GGAGVGKTVL ITESINNIAK
AHGGVSVSGG VGERTREGND LYMEMKESKV INEQNISESK VALVYGQMNE PPGARMRVGS
TAPTMAEYFR DVNKQDVPLF IDNIFRFVQA GSEVSALLGR MPSAVGYQPT LGTEMGSLQE
RITSTKEGSI TSIQAVYVPA DDLTDPAPAT TSAHLDATTV LSRGLAAKGI YPAVDPLDST
STMSQPWIVG EEHYDTAQGV KQTLQRYKEL QDIIAILGLD ELSEEDRLTV ARARKIERFL
PQPFFVAEVF TGSPGKYVSL SETIKGFQMI LSGE
//
