ID Q9MTQ2_AMPOP Unreviewed; 548 AA.
AC Q9MTQ2;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 119.
DE RecName: Full=ATP synthase subunit beta {ECO:0000256|RuleBase:RU003553};
DE EC=7.1.2.2 {ECO:0000256|RuleBase:RU003553};
GN Name=atpB {ECO:0000313|EMBL:CAB75846.1};
OS Amphidinium operculatum (Dinoflagellate).
OG Plastid; Chloroplast {ECO:0000313|EMBL:CAB75846.1}.
OC Eukaryota; Sar; Alveolata; Dinophyceae; Amphidiniales; Amphidiniaceae;
OC Amphidinium.
OX NCBI_TaxID=107036 {ECO:0000313|EMBL:CAB75846.1};
RN [1] {ECO:0000313|EMBL:CAB75846.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=10732684; DOI=10.1007/s004380050042;
RA Barbrook A.C., Howe C.J.;
RT "Minicircular plastid DNA in the dinoflagellate Amphidinium operculatum.";
RL Mol. Gen. Genet. 263:152-158(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|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; AJ250266; CAB75846.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9MTQ2; -.
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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR005722; ATP_synth_F1_bsu.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
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; 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:CAB75846.1};
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:ARBA00022528, ECO:0000313|EMBL:CAB75846.1};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 223..422
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 548 AA; 59149 MW; DA48952E976D284A CRC64;
MRDGSVLASE CEAFVWDLFY MESFVSMLHS VFKGIAPTPN KEALDLISLE LEYCASNELS
LALASSGLFI KSYANALIAE VQQIAYGGIL RAVALAGTDG LDLVSTYGHL TYQPLVVPVG
RVCQGRILNC VGAPMDAYDD IVISAAYSSV ESPASVVLNA LWYGGTASSS PSKLTTPLSH
YDQSFANAAP IHKDQVGVLD IDITAPLFET GIKVVDVLTP YKKGGKVGLF GGAGVGKTVL
IMELIRNLAY SHNGLSLFSG IGERSREAND LYVEMQESGI ILLAEDSSNP YFSAESKVAL
VFGQMNDTPG ARFRVANAAL TMAEYFRDVN GQDLLVFMDN IFRFVQAGSE LSTLLGRMPS
AVGYQPTLAT EMGTLQERIV PTLFGSITSI QAVYVPADDI TDPAPVAIFT HLDAITVLSR
GLAAKGIYPA VDPLASTSKA LTASFVGERH YNVAQSIIQC LNRYKELQDL IAILGLDELS
ESDRLSVLRG RKIERFLSQP FFVAEVFSRT PGKYVKVEEA LDGFDGILTG RYDDRAEADF
YLQGAMSD
//
