ID   ATPB_HEMPU              Reviewed;         523 AA.
AC   Q25117;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=ATP synthase subunit beta, mitochondrial;
DE            EC=7.1.2.2;
DE   Flags: Precursor;
OS   Hemicentrotus pulcherrimus (Sea urchin) (Strongylocentrotus pulcherrimus).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC   Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC   Hemicentrotus.
OX   NCBI_TaxID=7650;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   PubMed=7765182;
RA   Satoh Y.I., Shimizu T., Sendai Y., Kinoh H., Suzuki N.;
RT   "Nucleotide sequence of the proton ATPase beta-subunit homologue of the sea
RT   urchin Hemicentrotus pulcherrimus.";
RL   Zool. Sci. 11:153-156(1994).
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; D17361; BAA04178.1; -; mRNA.
DR   AlphaFoldDB; Q25117; -.
DR   SMR; Q25117; -.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
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: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; 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   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   Transit peptide; Translocase; Transport.
FT   TRANSIT         1..?19
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?20..523
FT                   /note="ATP synthase subunit beta, mitochondrial"
FT                   /id="PRO_0000002447"
FT   BINDING         201..208
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   523 AA;  56075 MW;  3656AD23CE2CFB4D CRC64;
     MFSRVAKTSF SAVRAAKSQF SHSLSQQTSK TWVPAATCSK RSYAAEAKTS AAPVSGQIVA
     VIGAVVDVQF EDDLPPILNA LEVQGRTSRL VLEVAQHLGE NTVRTIAMDG TEGLIRGQKC
     VDTGSPISIP VGPETLGRII NVIGEPIDER GPIGTDRRSA IHAEAPEFVE MSVNQEILVT
     GIKVVDLLAP YAKGGKIGLF GGAGVGKTVL IMELINNVAK AHGGYSVFAG VGERTREGND
     LYHEMIEGGV ISLKDDTSKV ALVYGQMNEP PGARARVALT GLTVAEYFRD QEGQDVLLFI
     DNIFRFTQAG SEVSALLGRI PSAVGYQPTL ATDMGTMQER ITTTKKGSIT SVQAIYVPAD
     DLTDPAPATT FAHLDATTVL SRGIAELGIY PAVDPLDSSS RIMDPNVVGE RHYSIARGVQ
     KILQDNKTLQ DIIAILGMDE LSEDDKLTVS RARKIQRFLS QPFQVAEVFT GSPGKLVSMA
     ETIDGFESII KGECDHLPEI AFYMVGNIQD VKDKADRLAE ELS