ID ATPB_CHICK Reviewed; 533 AA.
AC Q5ZLC5; P84168;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 24-JAN-2024, entry version 121.
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: Precursor;
GN Name=ATP5F1B {ECO:0000250|UniProtKB:P06576};
GN Synonyms=ATP5B {ECO:0000250|UniProtKB:P00829}; ORFNames=RCJMB04_6l18;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAG31468.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB {ECO:0000312|EMBL:CAG31468.1};
RC TISSUE=Bursa of Fabricius {ECO:0000312|EMBL:CAG31468.1};
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
RN [2] {ECO:0000305}
RP IDENTIFICATION, AND MASS SPECTROMETRY.
RC TISSUE=Embryo {ECO:0000269|PubMed:16287166};
RX PubMed=16287166; DOI=10.1002/pmic.200402056;
RA Agudo D., Gomez-Esquer F., Diaz-Gil G., Martinez-Arribas F., Delcan J.,
RA Schneider J., Palomar M.A., Linares R.;
RT "Proteomic analysis of the Gallus gallus embryo at stage-29 of
RT development.";
RL Proteomics 5:4946-4957(2005).
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. {ECO:0000305}.
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 -!- MASS SPECTROMETRY: Mass=51171; Mass_error=1; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16287166};
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255}.
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DR EMBL; AJ719809; CAG31468.1; -; mRNA.
DR RefSeq; NP_001026562.2; NM_001031391.2.
DR AlphaFoldDB; Q5ZLC5; -.
DR SMR; Q5ZLC5; -.
DR BioGRID; 686196; 2.
DR IntAct; Q5ZLC5; 1.
DR STRING; 9031.ENSGALP00000063712; -.
DR PaxDb; 9031-ENSGALP00000035339; -.
DR GeneID; 426673; -.
DR KEGG; gga:426673; -.
DR CTD; 426673; -.
DR VEuPathDB; HostDB:geneid_426673; -.
DR eggNOG; KOG1350; Eukaryota.
DR InParanoid; Q5ZLC5; -.
DR OrthoDB; 3420200at2759; -.
DR PhylomeDB; Q5ZLC5; -.
DR PRO; PR:Q5ZLC5; -.
DR Proteomes; UP000000539; Unassembled WGS sequence.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central.
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; ISS:UniProtKB.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR GO; GO:0001525; P:angiogenesis; IMP:UniProtKB.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IBA:GO_Central.
DR CDD; cd18110; ATP-synt_F1_beta_C; 1.
DR CDD; cd18115; ATP-synt_F1_beta_N; 1.
DR CDD; cd01133; F1-ATPase_beta_CD; 1.
DR Gene3D; 2.40.10.170; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 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 Pfam; PF02874; ATP-synt_ab_N; 1.
DR PIRSF; PIRSF039072; ATPase_subunit_beta; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF50615; N-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 ATP synthesis; ATP-binding; CF(1); Hydrogen ion transport; Ion transport;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding;
KW Reference proteome; Transit peptide; Translocase; Transport.
FT TRANSIT 1..53
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P00829"
FT CHAIN 54..533
FT /note="ATP synthase subunit beta, mitochondrial"
FT /id="PRO_0000223501"
FT BINDING 212..219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00829"
FT BINDING 244
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00829"
SQ SEQUENCE 533 AA; 56628 MW; 84C9945D1AAD8832 CRC64;
MLGLAGRCSA AAASAARPAL RRAAGPSHGF LPLLLSRGAG PAAAVGARRD HAAQAAPAAK
AGSATGRIVA VIGAVVDVQF DEGLPPILNA LEVQGRETRL VLEVAQHLGE NTVRTIAMDG
TEGLVRGQKV LDSGAPIRIP VGPETLGRIM NVIGEPIDER GPITTKQFAA IHAEAPEFVE
MSVEQKILVT GIKVVDLLAP YAKGGKIGLF GGAGVGKTVL IMELINNVAK AHGGYSVFAG
VGERTREGND LYHEMIESGV INLKDATSKV ALVYGQMNEP PGARARVALT GLTVAEYFRD
QEGQDVLLFI DNIFRFTQAG SEVSALLGRI PSAVGYQPTL ATDMGTMQER ITTTRKGSIT
SVQAIYVPAD DLTDPAPATT FAHLDATTVL SRAIAELGIY PAVDPLDSTS RIMDPNIVGP
EHYDVARGVQ KILQDYKSLQ DIIAILGMDE LSEEDKLTVA RARKIQRFLS QPFQVAEVFT
GHMGKLVPLK ETIKGFKQIL AGEYDHLPEQ AFYMVGPIEE AVAKAEKLAE EHA
//
