ID ATPB_MESAU Reviewed; 362 AA.
AC Q0QEP2;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 24-JAN-2024, entry version 74.
DE RecName: Full=ATP synthase subunit beta, mitochondrial {ECO:0000250|UniProtKB:P56480};
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};
GN Synonyms=ATP5B {ECO:0000312|EMBL:ABD77235.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1] {ECO:0000312|EMBL:ABD77235.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver {ECO:0000312|EMBL:ABD77235.1};
RX PubMed=16751257; DOI=10.1093/molbev/msl027;
RA Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.;
RT "Housekeeping genes for phylogenetic analysis of eutherian relationships.";
RL Mol. Biol. Evol. 23:1493-1503(2006).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20400973; DOI=10.1038/aja.2010.19;
RA Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT (GP96) are unique to hamster caput epididymal spermatozoa.";
RL Asian J. Androl. 12:344-355(2010).
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 {ECO:0000250|UniProtKB:P10719}.
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:0000250|UniProtKB:P00829};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:57722;
CC Evidence={ECO:0000250|UniProtKB:P00829};
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:0000255}.
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DR EMBL; DQ403102; ABD77235.1; -; mRNA.
DR AlphaFoldDB; Q0QEP2; -.
DR SMR; Q0QEP2; -.
DR Proteomes; UP000189706; 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; ISS:UniProtKB.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR CDD; cd18110; ATP-synt_F1_beta_C; 1.
DR CDD; cd01133; F1-ATPase_beta_CD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR005722; ATP_synth_F1_bsu.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
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 NCBIfam; TIGR01039; atpD; 1.
DR PANTHER; PTHR15184; ATP SYNTHASE; 1.
DR PANTHER; PTHR15184:SF71; ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR SUPFAM; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP synthesis; ATP-binding; CF(1); Hydrogen ion transport;
KW Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Translocase;
KW Transport.
FT CHAIN <1..>362
FT /note="ATP synthase subunit beta, mitochondrial"
FT /id="PRO_0000394745"
FT BINDING 60..67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00829"
FT BINDING 92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00829"
FT MOD_RES 14
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 14
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 51
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06576"
FT MOD_RES 112
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 112
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 117
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 117
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 165
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 279
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06576"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10719"
FT MOD_RES 333
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 338
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:ABD77235.1"
FT NON_TER 362
FT /evidence="ECO:0000312|EMBL:ABD77235.1"
SQ SEQUENCE 362 AA; 39384 MW; C5E7CBBD7FF09C1B CRC64;
IGEPINERGP IKTKQFAPIH AEAPDFLNMS VDQEILVTGI KVVDLLAPYA KGGKIGLFGG
AVVGKTVLIM ELINNVAKAH GGYSVFAGVG ERTREGNDLY HEMIESGVIN LKDATSKVAL
VYGQMNEPPG ARARVALTGL TVAEYFRDQE GQDVLLFIDN IFRFTQAGSE VSALLGRIPS
AVGYQPTLAT DMGTMQERIT TTKKGSITSV QAIYVPADDL TDPAPATTFA HLDATTVLSR
AIAELGIYPA VDPLDSTSRI MDPNIVGNEH YDVARGVQKI LQDYKSLQDI IAILGMDELS
EEDKLTVSRA RKIQRFLSQP FQVAEVFTGH MGKLVPLKET IKGFQQMLAG DYDHLPEQAY
YI
//
