ID Q9MRA8_9LAMI Unreviewed; 483 AA.
AC Q9MRA8;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 110.
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:CAB89923.1};
OS Lavandula bipinnata.
OG Plastid; Chloroplast {ECO:0000313|EMBL:CAB89923.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Ocimeae; Lavandulinae;
OC Lavandula.
OX NCBI_TaxID=85224 {ECO:0000313|EMBL:CAB89923.1};
RN [1] {ECO:0000313|EMBL:CAB89923.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Upson sn RNG {ECO:0000313|EMBL:CAB89923.1};
RX PubMed=12118410; DOI=10.1080/10635159950173861;
RA Savolainen V., Chase M.W., Morton C.M., Hoot S.B., Soltis D.E., Bayer C.,
RA Fay M.F., de Bruijn A., Sullivan S., Qiu Y.-L.;
RT "Phylogenetics of flowering plants based upon a combined analysis of
RT plastid atpB and rbcL gene sequences.";
RL Syst. Biol. 49:306-362(2000).
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; AJ235519; CAB89923.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9MRA8; -.
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:CAB89923.1};
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:CAB89923.1};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 159..351
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAB89923.1"
FT NON_TER 483
FT /evidence="ECO:0000313|EMBL:CAB89923.1"
SQ SEQUENCE 483 AA; 51951 MW; C57C115F16250BED CRC64;
TTSGSGVSTL EKKNLGRIIQ IIGPVLDVAF PPGQMPNIYN ALVVKGRDTV GQPINVTCEV
QQLLGNNRVR AVAMSATDGL MRGMEVIDTG APLSVPVGGA TLGRIFNVLG EPVDNLGPVD
TRTTFPIHRS APAFIQLDTK LSIFETGIKV VDLLAPYRRG GKIGLFGGAG VGKTVLIMEL
INNIAKAHGG VSVFGGVGER TREGNDLYME MKESGVINEE NIAESKVALV YGQMNEPPGA
RMRVGLTALT MAEYFRDVNE QDVLLFIDNI FRFVQAGSEV SALLGRMPSA VGYQPTLSTE
MGSLQERITS TKEGSITSIQ AVYVPADDLT DPAPATTFAH LDATTVLSRG LAAKGIYPAV
DPLDSTSTML QPRIVGEEHY ETAQRVKQTL QRYKELQDII AILGLDELSE EDRLTVARAR
KIERFLSQPF FVAEVFTGSP GKYVGLAETI KGFQLILSGE LDGLPEQAFY LVGNIDEATA
KGY
//
