ID   ATPB_CANLF              Reviewed;          19 AA.
AC   P99504;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   23-FEB-2022, entry version 81.
DE   RecName: Full=ATP synthase subunit beta, mitochondrial {ECO:0000305};
DE            EC=7.1.2.2;
DE   AltName: Full=ATP synthase F1 subunit beta {ECO:0000250|UniProtKB:P06576};
DE   Flags: Fragment;
GN   Name=ATP5F1B {ECO:0000250|UniProtKB:P06576}; Synonyms=ATP5B;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Heart;
RX   PubMed=9504812; DOI=10.1002/elps.1150181514;
RA   Dunn M.J., Corbett J.M., Wheeler C.H.;
RT   "HSC-2DPAGE and the two-dimensional gel electrophoresis database of dog
RT   heart proteins.";
RL   Electrophoresis 18:2795-2802(1997).
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};
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. Component of an ATP synthase complex composed of
CC       ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-
CC       ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and
CC       ATP5MJ (By similarity). Interacts with PPIF (By similarity). Interacts
CC       with BCL2L1 isoform BCL-X(L); the interaction mediates the association
CC       of BCL2L1 isoform BCL-X(L) with the mitochondrial membrane F(1)F(0) ATP
CC       synthase and enhances neurons metabolic efficiency (By similarity).
CC       Interacts with CLN5 and PPT1. Interacts with S100A1; this interaction
CC       increases F1-ATPase activity (By similarity). Interacts with MTLN (By
CC       similarity). Interacts with TTC5/STRAP; the interaction results in
CC       decreased mitochondrial ATP production (By similarity).
CC       {ECO:0000250|UniProtKB:P00829, ECO:0000250|UniProtKB:P06576,
CC       ECO:0000250|UniProtKB:P10719, ECO:0000250|UniProtKB:P56480}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P00829}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P00829}; Matrix side
CC       {ECO:0000250|UniProtKB:P00829}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
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DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
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.
PE   1: Evidence at protein level;
KW   ATP synthesis; ATP-binding; CF(1); Direct protein sequencing;
KW   Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Nucleotide-binding; Reference proteome;
KW   Translocase; Transport.
FT   CHAIN           1..>19
FT                   /note="ATP synthase subunit beta, mitochondrial"
FT                   /id="PRO_0000144557"
FT   UNSURE          8
FT   UNSURE          17..19
FT   NON_TER         19
SQ   SEQUENCE   19 AA;  1875 MW;  BB9C163FDC60BB42 CRC64;
     ATQTSPSPKG AAAXXXRVV