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Database: UniProt
Entry: Q9MRW2_AMAHP
LinkDB: Q9MRW2_AMAHP
Original site: Q9MRW2_AMAHP 
ID   Q9MRW2_AMAHP            Unreviewed;       456 AA.
AC   Q9MRW2;
DT   01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 106.
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:CAB90075.1};
OS   Amaranthus hypochondriacus (Prince-of-Wales feather) (Amaranthus hybridus
OS   var. hypochondriacus).
OG   Plastid; Chloroplast {ECO:0000313|EMBL:CAB90075.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Amaranthaceae; Amaranthus.
OX   NCBI_TaxID=28502 {ECO:0000313|EMBL:CAB90075.1};
RN   [1] {ECO:0000313|EMBL:CAB90075.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Unknown {ECO:0000313|EMBL:CAB90075.1};
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; AJ235388; CAB90075.1; -; 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:0000313|EMBL:CAB90075.1};
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:CAB90075.1};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          140..332
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CAB90075.1"
FT   NON_TER         456
FT                   /evidence="ECO:0000313|EMBL:CAB90075.1"
SQ   SEQUENCE   456 AA;  49059 MW;  9860AD660E6C4368 CRC64;
     QIXGPVLDVA FPPGXMPNIY NALVVXGRDS VXQPINVTCE VQQLLGNNRV RAVAMSATDG
     LTRGMEVIDT GAPLSVPVGG TTLGRIFNVL GEPVDNLGPV DTSTTSPIHR SAPAFTQLDT
     KLSIFETGIK VVDLLAPYRR GGKIGLFGGA GVGKTVLIME LINNIAKAHG GVSVFGGVGE
     RTREGNDLYM EMKESGVINE QNIAESKVAL VYGQMNEPPG ARMRVGXTAL TMAEYFRDVN
     EQDVLLFIDN IFRFVQAGSE VSALLGRMPS AVGYQPTLST EMGSLQERIT STKEGSITSI
     QAVYVPADDL TDPAPATTFA HLDATTVLSR GLAAKGIYPA VDPLDSTSTM LQPRIVGEEH
     YETAQRVKQT LQRYKELQDI IAILGLDELS EEDRLTVARA RKIERFLSQP FFVAEVFTGS
     PGKYVGLAET IRGFQLXLSG ELDGLPEQAF YLVGNI
//
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