ATPBM_MAIZE
ID ATPBM_MAIZE Reviewed; 553 AA.
AC P19023;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=ATP synthase subunit beta, mitochondrial;
DE EC=7.1.2.2;
DE Flags: Precursor;
GN Name=ATPB; Synonyms=ATP2;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. MUTIND-FR7205035; TISSUE=Coleoptile;
RX PubMed=2145551; DOI=10.1093/nar/18.19.5885;
RA Winning B.M., Bathgate B., Purdue P.E., Leaver C.J.;
RT "Nucleotide sequence of a cDNA encoding the beta subunit of the
RT mitochondrial ATP synthase from Zea mays.";
RL Nucleic Acids Res. 18:5885-5885(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kernel;
RX PubMed=16667450; DOI=10.1104/pp.93.1.295;
RA Ehrenshaft M., Brambl R.;
RT "Respiration and mitochondrial biogenesis in germinating embryos of
RT maize.";
RL Plant Physiol. 93:295-304(1990).
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 -!- 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; X54233; CAA38140.1; -; mRNA.
DR EMBL; M36087; AAA70268.1; -; mRNA.
DR PIR; S11491; S11491.
DR RefSeq; NP_001105340.1; NM_001111870.1.
DR AlphaFoldDB; P19023; -.
DR SMR; P19023; -.
DR STRING; 4577.GRMZM2G113408_P01; -.
DR iPTMnet; P19023; -.
DR PaxDb; P19023; -.
DR PRIDE; P19023; -.
DR ProMEX; P19023; -.
DR EnsemblPlants; Zm00001eb295050_T002; Zm00001eb295050_P002; Zm00001eb295050.
DR GeneID; 542267; -.
DR Gramene; Zm00001eb295050_T002; Zm00001eb295050_P002; Zm00001eb295050.
DR KEGG; zma:542267; -.
DR MaizeGDB; 66952; -.
DR eggNOG; KOG1350; Eukaryota.
DR HOGENOM; CLU_022398_0_2_1; -.
DR OMA; TTEHYLP; -.
DR OrthoDB; 495235at2759; -.
DR Proteomes; UP000007305; Chromosome 6.
DR ExpressionAtlas; P19023; baseline and differential.
DR Genevisible; P19023; ZM.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IBA:GO_Central.
DR GO; GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1); IEA:InterPro.
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: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 GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IBA:GO_Central.
DR Gene3D; 1.10.10.910; -; 1.
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; IPR042079; ATP_synt_F1_beta_sf.
DR InterPro; IPR020971; ATP_synth_F1_beta_su.
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 Pfam; PF11421; Synthase_beta; 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 2: Evidence at transcript 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..47
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 48..553
FT /note="ATP synthase subunit beta, mitochondrial"
FT /id="PRO_0000002439"
FT REGION 16..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 228..235
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 553 AA; 59103 MW; EABF1BD3DA1E5831 CRC64;
MASRRVVSSL LRSASRLRAA SPAAPRPRAP PHRPSPAGYL FNRAAAYASS AAAQAAPATP
PPATGKTGGG KITDEFTGAG AIGQVCQVIG AVVDVRFDEG LPPILTALEV LDNNIRLVLE
VAQHLGENMV RTIAMDGTEG LVRGQRVLNT GSPITVPVGR ATLGRIINVI GEPIDEKGDI
KTNHFLPIHR EAPAFVEQAT EQQILVTGIK VVDLLAPYQR GGKIGLFGGA GVGKTVLIME
LINNVAKAHG GFSVFAGVGE RTREGNDLYR EMIESGVIKL DDKQSESKCA LVYGQMNEPP
GARARVGLTG LTVAEHFRDA EGQDVLLFID NIFRFTQANS EVSALLGRIP SAVGYQPTLA
TDLGGLQERI TTTKKGSITS VQAIYVPADD LTDPAPATTF AHLDATTVLS RQISELGIYP
AVDPLDSTSR MLSPHVLGED HYNTARGVQK VLQNYKNLQD IIAILGMDEL SEDDKLTVAR
ARKIQRFLSQ PFHVAEVFTG APGKYVELKE SVKSFQGVLD GKYDDLPEQS FYMVGGIEEV
IAKAEKIAKE SAS
