ID   ATPBM_DAUCA             Reviewed;         547 AA.
AC   P37399;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=ATP synthase subunit beta, mitochondrial;
DE            EC=7.1.2.2;
DE   Flags: Precursor;
GN   Name=ATPB; Synonyms=ATP2;
OS   Daucus carota (Wild carrot).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC   Daucus; Daucus sect. Daucus.
OX   NCBI_TaxID=4039;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Danvers Half-long; TISSUE=Callus;
RA   Apuya N.R., Zimmerman J.;
RL   Submitted (SEP-1991) to the EMBL/GenBank/DDBJ databases.
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; X60303; CAA42844.1; -; Genomic_DNA.
DR   PIR; S21988; S21988.
DR   AlphaFoldDB; P37399; -.
DR   SMR; P37399; -.
DR   PRIDE; P37399; -.
DR   GO; GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1); IEA:InterPro.
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   Gene3D; 1.10.1140.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_01347; ATP_synth_beta_bact; 1.
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   SUPFAM; SSF50615; SSF50615; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01039; atpD; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; ATP-binding; CF(1); Hydrogen ion transport; Ion transport;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding;
KW   Transit peptide; Translocase; Transport.
FT   TRANSIT         1..45
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           46..547
FT                   /note="ATP synthase subunit beta, mitochondrial"
FT                   /id="PRO_0000002437"
FT   REGION          52..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         226..233
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   547 AA;  59136 MW;  5AD2EFF0DFF1E23C CRC64;
     MASRRLLSSF LRSSTRRSLR PSFSNPRPSF LTSYCSSPAS ILRRYATAAP AKEPAASKPA
     GTAGTGKGTI TDEKTGAGAI GQVCQIIGAV VDVKFEEGLP PIMTALEVID FEIRLVLEVA
     PSLGENTVRT IAMDGTEGLV RGQKVLNTGA PITIPVGRAT LGRIINVIGE PIDHRGEIKT
     DQYLPIHREA PTFVDQATEQ QILVTGIKVV DLLAPYQKGG KIGLFGGDWV GKTVLIMELI
     NNVAKAHAVF AGVGERTREG NDLYKEMMES GVIKLGDQQA ESKCALVYGQ MNEPPGSRAR
     VGLTGLTVAE HFRDAEGEDV LLFVDKRFRF TQANSEVSAL LGRIPSAVGY QPTLATDLGG
     LQERITTTKK GSITSVQAIY VPADDLTDPA PATTFAHLDA TTVLSRQISE LGIYPAVDPL
     DSTSRMLTPE SGEEHYNTAR GVQKVLQNYK NLQDIIAILG MDELSEDDKL TVARARKIQR
     FLSQPFHVAE IFTGAPGKYV ELKECVTSFQ GVLDGKYDDL PEQSFYMLGG IEEVIAKAEK
     MAKENPQ