ID Q9XQP8_9ROSI Unreviewed; 485 AA.
AC Q9XQP8;
DT 01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT 01-FEB-2005, sequence version 2.
DT 27-MAR-2024, entry version 112.
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:CAB44028.2};
OS Fremontodendron californicum x Fremontodendron mexicanum.
OG Plastid; Chloroplast {ECO:0000313|EMBL:CAB44028.2}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Bombacoideae; Fremontodendron.
OX NCBI_TaxID=82396 {ECO:0000313|EMBL:CAB44028.2};
RN [1] {ECO:0000313|EMBL:CAB44028.2}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:CAB44028.2};
RA Bayer C., Fay M.F., de Bruin A.Y., Savolainen V., Morton C.M., Kubitzki K.,
RA Alverson W.S., Chase M.W.;
RT "Support for an expanded family concept of Malvaceae withih a
RT recircumscribed oder Malvales: a combined analysis of plastid atpB and rbcL
RT DNA sequences.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
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; AJ233077; CAB44028.2; -; 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:0000313|EMBL:CAB44028.2};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781};
KW Hydrolase {ECO:0000313|EMBL:CAB44028.2};
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:CAB44028.2};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 155..347
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAB44028.2"
FT NON_TER 485
FT /evidence="ECO:0000313|EMBL:CAB44028.2"
SQ SEQUENCE 485 AA; 52249 MW; 93AEDE09A99AA0FA CRC64;
SGISTLEKEX LGRISQIIGP VLDVAFPPGK MPNIYNALVV KGRDTAGQQI NVTCEVQQLL
GNNRVRAVAM SATDGLMRGM EVIDTGAPLS VPVGGATLGR IFNVLGEPVD NLGPVDTRTT
SPIHKPAPAF IQLDTKLSIF ETGIKVVDLL APYRRGGKIG LFGGAGVGKT VLIMELINNI
AKAHGGVSVF GGVGERTREG NDLYMEMKES GVINEQNLAE SKVALVYGQM NEPPGARMRV
GLTALTMAEY FRDVNEQDVL LFIDNIFRFV QAGSEVSALL GRMPSAVGYQ PTLSTEMGTL
QERITSTKEG SIISIQAVYV PADDLTDPAP ATTFAHLDAT TVLSRGLAAK GIYPAVDPLD
STSTMLQPRI VGEEHYETAQ RVKQTLQRYK ELQDIIAILG LDELSEEDRL TVARARKIER
FLSQPFFVAE VFTGSPGKYV GLAETIRGFK LILSGELDGL PEQAFYLVGN IDEATAKATN
LEMEX
//
