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Database: UniProt
Entry: Q9MRD7_9ASTE
LinkDB: Q9MRD7_9ASTE
Original site: Q9MRD7_9ASTE 
ID   Q9MRD7_9ASTE            Unreviewed;       486 AA.
AC   Q9MRD7;
DT   01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 2.
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:CAB89914.2};
OS   Ipomoea mauritiana.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:CAB89914.2}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Convolvulaceae; Ipomoeeae; Ipomoea.
OX   NCBI_TaxID=85214 {ECO:0000313|EMBL:CAB89914.2};
RN   [1] {ECO:0000313|EMBL:CAB89914.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Chase 2525 K {ECO:0000313|EMBL:CAB89914.2};
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000256|ARBA:ARBA00008936}.
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DR   EMBL; AJ235505; CAB89914.2; -; Genomic_DNA.
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:0000256|ARBA:ARBA00022528, ECO:0000313|EMBL:CAB89914.2};
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:CAB89914.2};
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:CAB89914.2"
FT   NON_TER         486
FT                   /evidence="ECO:0000313|EMBL:CAB89914.2"
SQ   SEQUENCE   486 AA;  52473 MW;  1F12BC52BFBEB051 CRC64;
     XXSGFEVSAV EKKNXGRXVQ IIGPVIDVAF PPGKMPNIYN ALVVQGRDXX XEQTNVXCEV
     QQLLGNNRVR AVAMSDTDGL MRGMEVIDTG APISVPVGGS TLGRIFNVLG QPVDNLGPVD
     TNTTSPIHRS APAFIQLDTK LSIFETGIKV VDLLAPYRRG GKIGLFGGAG VGKTVLIMEL
     INNIAKAHGG VSVFGGVGER TREGNDLYLE MKESGVINEE NIPESKVALV YGQMNEPPGA
     RMRVGLTALT MAEYFRDVNE QDVLLFIDNI FRFVQAGSEV SALLGRMPSA VGYQPTLSTE
     MGSLQERITS TKEGSITSIQ AVYVPADDLT DPAPATTFAH LDATTVLSRG LAAKGIYPAV
     DPLDSTSTML QPRIVGEEHY ETAQRVKQTL QRYKELQDII AILGLDELSE EDRLXVARAR
     KIERFLSQPF FVAEVFTGSP GKYVGLAETI RGFQLILSGE LDGLPEQAFY LVGNIDEATA
     KAMNLX
//
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