ID A0A182YSV3_ANOST Unreviewed; 437 AA.
AC A0A182YSV3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=ATP synthase subunit beta {ECO:0000256|RuleBase:RU003553};
DE EC=7.1.2.2 {ECO:0000256|RuleBase:RU003553};
OS Anopheles stephensi (Indo-Pakistan malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=30069 {ECO:0000313|EnsemblMetazoa:ASTEI11539-PA, ECO:0000313|Proteomes:UP000076408};
RN [1] {ECO:0000313|Proteomes:UP000076408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Indian {ECO:0000313|Proteomes:UP000076408};
RX PubMed=25244985; DOI=10.1186/preaccept-1262842421127991;
RA Jiang X., Peery A., Hall A.B., Sharma A., Chen X.G., Waterhouse R.M.,
RA Komissarov A., Riehle M.M., Shouche Y., Sharakhova M.V., Lawson D.,
RA Pakpour N., Arensburger P., Davidson V.L., Eiglmeier K., Emrich S.,
RA George P., Kennedy R.C., Mane S.P., Maslen G., Oringanje C., Qi Y.,
RA Settlage R., Tojo M., Tubio J.M., Unger M.F., Wang B., Vernick K.D.,
RA Ribeiro J.M., James A.A., Michel K., Riehle M.A., Luckhart S.,
RA Sharakhov I.V., Tu Z.;
RT "Genome analysis of a major urban malaria vector mosquito, Anopheles
RT stephensi.";
RL Genome Biol. 15:459-459(2014).
RN [2] {ECO:0000313|EnsemblMetazoa:ASTEI11539-PA}
RP IDENTIFICATION.
RC STRAIN=Indian {ECO:0000313|EnsemblMetazoa:ASTEI11539-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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 three main
CC subunits: a, b and c. {ECO:0000256|RuleBase:RU003553}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000256|ARBA:ARBA00008936}.
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DR AlphaFoldDB; A0A182YSV3; -.
DR STRING; 30069.A0A182YSV3; -.
DR EnsemblMetazoa; ASTEI11539-RA; ASTEI11539-PA; ASTEI11539.
DR VEuPathDB; VectorBase:ASTE002107; -.
DR VEuPathDB; VectorBase:ASTEI11539; -.
DR VEuPathDB; VectorBase:ASTEI20_040243; -.
DR OMA; GFNMIMD; -.
DR Proteomes; UP000076408; Unassembled WGS sequence.
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 PIRSF; PIRSF039072; ATPase_subunit_beta; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000076408};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 120..304
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 437 AA; 47035 MW; 9A17383CFFCB51DE CRC64;
LPPILNALEV QGRSARLVLE VAQHLGENTV RTIAMDGTEG LVRGQRVLDT GSPIRIPVGA
ETLGRIINVI GEPIDERGPI NTNLSAPIHA EAPEFIEMSV EQEILVTGIK VVDLLAPYAK
GGKIGLFGGA GVGKTVLIME LINNVAKAHG GYSVFAGVGE RTREGNDLYN EMIEGGVISL
KDKSSKVALV YGQMNEPPGA RARVALTGLT VAEYFRDQEG QDVLLFIDNI FRFTQAGSEV
SALLGRIPSA VGYQPTLATD MGSMQERITT TKKGSITSVQ AIYVPADDLT DPAPATTFAH
LDATTVLSRA IAELGIYPAV DPLDSTSRIM DPNIIGAEHY NIARGVQKIL QDYKSLQDII
AILGMDELSE EDKLTVARAR KIQRFLSQPF QVAEVFTGHA GKLVPLEETI KGFTKILNGE
LDHLPEVAFY MVGPIEE
//
