ATPB_DROME
ID ATPB_DROME Reviewed; 505 AA.
AC Q05825; Q9V494;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 3.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=ATP synthase subunit beta, mitochondrial;
DE EC=7.1.2.2;
DE Flags: Precursor;
GN Name=ATPsynbeta {ECO:0000312|FlyBase:FBgn0010217};
GN Synonyms=ATPsyn-beta {ECO:0000312|FlyBase:FBgn0010217};
GN ORFNames=CG11154 {ECO:0000312|FlyBase:FBgn0010217};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-505.
RX PubMed=8373413; DOI=10.1006/bbrc.1993.2114;
RA Pena P., Garesse R.;
RT "The beta subunit of the Drosophila melanogaster ATP synthase: cDNA
RT cloning, amino acid analysis and identification of the protein in adult
RT flies.";
RL Biochem. Biophys. Res. Commun. 195:785-791(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RX PubMed=10071211; DOI=10.1007/s004380050942;
RA Caggese C., Ragone G., Perrini B., Moschetti R., de Pinto V., Caizzi R.,
RA Barsanti P.;
RT "Identification of nuclear genes encoding mitochondrial proteins: isolation
RT of a collection of D. melanogaster cDNAs homologous to sequences in the
RT Human Gene Index database.";
RL Mol. Gen. Genet. 261:64-70(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or
CC Complex V) produces ATP from ADP in the presence of a proton gradient
CC across the membrane which is generated by electron transport complexes
CC of the respiratory chain. F-type ATPases consist of two structural
CC domains, F(1) - containing the extramembraneous catalytic core, and
CC F(0) - containing the membrane proton channel, linked together by a
CC central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC the central stalk subunits to proton translocation. Subunits alpha and
CC beta form the catalytic core in F(1). Rotation of the central stalk
CC against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of
CC ATP in three separate catalytic sites on the beta subunits.
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 -!- 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.
CC -!- INTERACTION:
CC Q05825; Q9VES8: anon2A5; NbExp=3; IntAct=EBI-86574, EBI-173806;
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC Note=Peripheral membrane protein.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
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DR EMBL; X71013; CAA50332.1; -; mRNA.
DR EMBL; AE014135; AAF59391.1; -; Genomic_DNA.
DR EMBL; AY118367; AAM48396.1; -; mRNA.
DR PIR; JN0760; JN0760.
DR RefSeq; NP_001284719.1; NM_001297790.1.
DR RefSeq; NP_726631.1; NM_166808.3.
DR AlphaFoldDB; Q05825; -.
DR SMR; Q05825; -.
DR BioGRID; 68655; 69.
DR IntAct; Q05825; 31.
DR MINT; Q05825; -.
DR STRING; 7227.FBpp0305828; -.
DR PaxDb; Q05825; -.
DR PRIDE; Q05825; -.
DR DNASU; 43829; -.
DR EnsemblMetazoa; FBtr0089186; FBpp0088250; FBgn0010217.
DR EnsemblMetazoa; FBtr0344754; FBpp0311086; FBgn0010217.
DR GeneID; 43829; -.
DR KEGG; dme:Dmel_CG11154; -.
DR CTD; 43829; -.
DR FlyBase; FBgn0010217; ATPsynbeta.
DR VEuPathDB; VectorBase:FBgn0010217; -.
DR eggNOG; KOG1350; Eukaryota.
DR HOGENOM; CLU_022398_0_2_1; -.
DR InParanoid; Q05825; -.
DR OMA; GFNMIMD; -.
DR OrthoDB; 495235at2759; -.
DR PhylomeDB; Q05825; -.
DR Reactome; R-DME-1268020; Mitochondrial protein import.
DR Reactome; R-DME-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-DME-8949613; Cristae formation.
DR SignaLink; Q05825; -.
DR BioGRID-ORCS; 43829; 1 hit in 1 CRISPR screen.
DR ChiTaRS; ATPsynbeta; fly.
DR GenomeRNAi; 43829; -.
DR PRO; PR:Q05825; -.
DR Proteomes; UP000000803; Chromosome 4.
DR Bgee; FBgn0010217; Expressed in adult hindgut (Drosophila) and 29 other tissues.
DR ExpressionAtlas; Q05825; baseline and differential.
DR Genevisible; Q05825; DM.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IBA:GO_Central.
DR GO; GO:0005754; C:mitochondrial proton-transporting ATP synthase, catalytic core; ISS:FlyBase.
DR GO; GO:0005739; C:mitochondrion; HDA:FlyBase.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 GO; GO:0015986; P:proton motive force-driven ATP synthesis; ISS:FlyBase.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IBA:GO_Central.
DR Gene3D; 1.10.1140.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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 Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01039; atpD; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW ATP synthesis; ATP-binding; CF(1); Hydrogen ion transport; Ion transport;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding;
KW Reference proteome; Transit peptide; Translocase; Transport.
FT TRANSIT 1..31
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 32..505
FT /note="ATP synthase subunit beta, mitochondrial"
FT /id="PRO_0000002448"
FT BINDING 183..190
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 494..495
FT /note="VE -> CR (in Ref. 1; CAA50332)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 505 AA; 54108 MW; 92FA2CE1F0F919A2 CRC64;
MFALRAASKA DKNLLPFLGQ LSRSHAAKAA KAAAAANGKI VAVIGAVVDV QFDDNLPPIL
NALEVDNRSP RLVLEVAQHL GENTVRTIAM DGTEGLVRGQ KVLDTGYPIR IPVGAETLGR
IINVIGEPID ERGPIDTDKT AAIHAEAPEF VQMSVEQEIL VTGIKVVDLL APYAKGGKIG
LFGGAGVGKT VLIMELINNV AKAHGGYSVF AGVGERTREG NDLYNEMIEG GVISLKDKTS
KVALVYGQMN EPPGARARVA LTGLTVAEYF RDQEGQDVLL FIDNIFRFTQ AGSEVSALLG
RIPSAVGYQP TLATDMGSMQ ERITTTKKGS ITSVQAIYVP ADDLTDPAPA TTFAHLDATT
VLSRAIAELG IYPAVDPLDS TSRIMDPNII GQEHYNVARG VQKILQDYKS LQDIIAILGM
DELSEEDKLT VARARKIQRF LSQPFQVAEV FTGHAGKLVP LEQTIKGFSA ILAGDYDHLP
EVAFYMVGPI EEVVEKADRL AKEAA
