ID   ATPB_PENGL              Reviewed;         114 AA.
AC   P85446;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 2.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=ATP synthase subunit beta, mitochondrial;
DE            EC=7.1.2.2;
DE   Flags: Fragments;
GN   Name=atp2;
OS   Penicillium glabrum (Penicillium frequentans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=69773;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND ALLERGEN.
RC   STRAIN=B7 {ECO:0000269|Ref.1};
RA   Raquel H., Jeno P., Moita C., Cardoso C., Sao Jose H., San-Romao V.,
RA   Pinto Ricardo C., Oliveira M.M.;
RT   "Identification of putative allergens from Penicillium glabrum using two-
RT   dimensional (2-D) gel electrophoresis immunoblotting approach.";
RL   Submitted (FEB-2008) to UniProtKB.
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         Evidence={ECO:0000255|PROSITE-ProRule:PRU10106, ECO:0000305};
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:0000305}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}. Mitochondrion inner
CC       membrane {ECO:0000305}. Note=Peripheral membrane protein.
CC       {ECO:0000305}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC       {ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000255}.
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DR   AlphaFoldDB; P85446; -.
DR   PRIDE; P85446; -.
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   InterPro; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   1: Evidence at protein level;
KW   Allergen; ATP synthesis; ATP-binding; CF(1); Direct protein sequencing;
KW   Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Nucleotide-binding; Translocase; Transport.
FT   CHAIN           <1..>114
FT                   /note="ATP synthase subunit beta, mitochondrial"
FT                   /id="PRO_0000324674"
FT   BINDING         44..51
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P23704"
FT   NON_CONS        14..15
FT                   /evidence="ECO:0000303|Ref.1"
FT   NON_CONS        38..39
FT                   /evidence="ECO:0000303|Ref.1"
FT   NON_CONS        51..52
FT                   /evidence="ECO:0000303|Ref.1"
FT   NON_CONS        68..69
FT                   /evidence="ECO:0000303|Ref.1"
FT   NON_CONS        84..85
FT                   /evidence="ECO:0000303|Ref.1"
FT   NON_CONS        103..104
FT                   /evidence="ECO:0000303|Ref.1"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|Ref.1"
FT   NON_TER         114
FT                   /evidence="ECO:0000303|Ref.1"
SQ   SEQUENCE   114 AA;  12033 MW;  DDD2323BEFA5D83F CRC64;
     KVHQVIGAVV DVKFRVPVGA GTLGRIINVT GDPIDERGKI GLFGGAGVGK TKVALVFGQM
     NEPPGARARF TQAGSEVSAL LGRMRGISEL GIYPAVDPLD SKSRVQQMLQ EYKS