ATPB_YARLI
ID ATPB_YARLI Reviewed; 509 AA.
AC Q6CFT7;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=ATP synthase subunit beta, mitochondrial {ECO:0000250|UniProtKB:P00830};
DE EC=7.1.2.2 {ECO:0000255|RuleBase:RU003553, ECO:0000269|PubMed:25759169, ECO:0000269|PubMed:27373333};
DE Flags: Precursor;
GN Name=ATP2 {ECO:0000250|UniProtKB:P00830};
GN OrderedLocusNames=YALI0_B03982g {ECO:0000312|EMBL:CAG82701.2};
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591 {ECO:0000312|Proteomes:UP000001300};
RN [1] {ECO:0000312|Proteomes:UP000001300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
RN [2] {ECO:0000305}
RP IDENTIFICATION IN ATP SYNTHASE COMPLEX, FUNCTION OF ATP SYNTHASE COMPLEX,
RP SUBUNIT, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=CLIB 122 / E 150 {ECO:0000303|PubMed:25759169};
RX PubMed=25759169; DOI=10.1042/bj20150197;
RA Liu S., Charlesworth T.J., Bason J.V., Montgomery M.G., Harbour M.E.,
RA Fearnley I.M., Walker J.E.;
RT "The purification and characterization of ATP synthase complexes from the
RT mitochondria of four fungal species.";
RL Biochem. J. 468:167-175(2015).
RN [3] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF ATP SYNTHASE F1C10 COMPLEX,
RP STRUCTURE BY ELECTRON MICROSCOPY (7.7 ANGSTROMS) OF DIMERIC ATP SYNTHASE
RP COMPLEX, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=27373333; DOI=10.1016/j.molcel.2016.05.037;
RA Hahn A., Parey K., Bublitz M., Mills D.J., Zickermann V., Vonck J.,
RA Kuehlbrandt W., Meier T.;
RT "Structure of a Complete ATP Synthase Dimer Reveals the Molecular Basis of
RT Inner Mitochondrial Membrane Morphology.";
RL Mol. Cell 63:445-456(2016).
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 (PubMed:25759169). F-type ATP synthases
CC consist of two structural domains, F(1) - containing the
CC extramembraneous catalytic core, and F(0) - containing the membrane
CC proton channel, linked together by a central stalk and a peripheral
CC stalk (PubMed:27373333). During catalysis, ATP synthesis in the
CC catalytic domain of F(1) is coupled via a rotary mechanism of the
CC central stalk subunits to proton translocation (PubMed:27373333).
CC Subunits alpha/ATP1 and beta/ATP2 form the catalytic core in F(1)
CC (PubMed:27373333). Rotation of the central stalk against the
CC surrounding alpha/ATP1(3)beta/ATP2(3) subunits leads to hydrolysis of
CC ATP in three separate catalytic sites on the beta/ATP2 subunits
CC (PubMed:27373333). {ECO:0000269|PubMed:25759169,
CC ECO:0000269|PubMed:27373333}.
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|RuleBase:RU003553, ECO:0000269|PubMed:25759169,
CC ECO:0000269|PubMed:27373333};
CC -!- SUBUNIT: F-type ATP synthases have 2 components, the catalytic core
CC F(1) and the membrane-embedded component F(0), linked together by a
CC central stalk and a peripheral stalk (PubMed:27373333). The central
CC stalk, also called rotor shaft, is often seen as part of F(1)
CC (PubMed:27373333). The peripheral stalk is seen as part of F(0)
CC (PubMed:27373333). F(0) contains the membrane channel next to the rotor
CC (PubMed:27373333). F-type ATP synthases form dimers but each monomer
CC functions independently in ATP generation (PubMed:27373333). The dimer
CC consists of 17 different polypeptides: ATP1 (subunit alpha, 3 molecules
CC per monomer, part of F(1)), ATP2 (subunit beta, 3 copies per monomer,
CC part of F(1)), ATP3 (subunit gamma, part of the central stalk), ATP4
CC (subunit b, part of the peripheral stalk), ATP5/OSCP (subunit 5/OSCP,
CC part of the peripheral stalk), ATP6 (subunit a, part of the peripheral
CC stalk), ATP7 (subunit d, part of the peripheral stalk), ATP8 (subunit
CC 8, part of the peripheral stalk), OLI1 (subunit c, part of the rotor,
CC 10 molecules per monomer), ATP14 (subunit h, part of the peripheral
CC stalk), ATP15 (subunit epsilon, part of the central stalk), ATP16
CC (subunit delta, part of the central stalk), ATP17 (subunit f, part of
CC the peripheral stalk), ATP18 (subunit i/j, part of the peripheral
CC stalk), ATP19 (subunit k, dimer-specific, at interface between
CC monomers), ATP20 (subunit g, at interface between monomers), TIM11
CC (subunit e, at interface between monomers) (PubMed:27373333,
CC PubMed:25759169). {ECO:0000269|PubMed:25759169,
CC ECO:0000269|PubMed:27373333}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000305|PubMed:27373333}; Peripheral membrane protein
CC {ECO:0000305|PubMed:27373333}; Matrix side
CC {ECO:0000305|PubMed:27373333}. Note=The F-type ATP synthase complex is
CC anchored in the mitochondrial inner membrane via the F(0) domain with
CC the F(1) domain and the peripheral stalk extending into the
CC mitochondrial matrix. {ECO:0000305|PubMed:27373333}.
CC -!- MASS SPECTROMETRY: Mass=50901.3; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:25759169};
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR382128; CAG82701.2; -; Genomic_DNA.
DR RefSeq; XP_500475.2; XM_500475.2.
DR PDB; 5FL7; X-ray; 3.50 A; D/E/F=1-509.
DR PDBsum; 5FL7; -.
DR AlphaFoldDB; Q6CFT7; -.
DR SMR; Q6CFT7; -.
DR STRING; 4952.CAG82701; -.
DR EnsemblFungi; CAG82701; CAG82701; YALI0_B03982g.
DR GeneID; 2907185; -.
DR KEGG; yli:YALI0B03982g; -.
DR VEuPathDB; FungiDB:YALI0_B03982g; -.
DR HOGENOM; CLU_022398_0_2_1; -.
DR InParanoid; Q6CFT7; -.
DR OMA; GFNMIMD; -.
DR Proteomes; UP000001300; Chromosome B.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IBA:GO_Central.
DR GO; GO:0005754; C:mitochondrial proton-transporting ATP synthase, catalytic core; IEA:EnsemblFungi.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central.
DR GO; GO:0043531; F:ADP binding; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
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 GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; ATP synthesis; ATP-binding; CF(1); Hydrogen ion transport;
KW Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Nucleotide-binding; Reference proteome; Transit peptide; Translocase;
KW Transport.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25759169"
FT CHAIN 33..509
FT /note="ATP synthase subunit beta, mitochondrial"
FT /evidence="ECO:0000305"
FT /id="PRO_0000445312"
FT BINDING 189..196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27373333,
FT ECO:0007744|PDB:5FL7"
FT SITE 384
FT /note="Required for activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10106"
FT STRAND 40..47
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 77..86
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 89..96
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:5FL7"
FT TURN 170..175
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 195..208
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 213..219
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 222..235
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 245..251
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 257..260
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 263..276
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 281..287
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 289..300
FT /evidence="ECO:0007829|PDB:5FL7"
FT TURN 301..304
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 317..324
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 334..340
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 351..356
FT /evidence="ECO:0007829|PDB:5FL7"
FT TURN 357..359
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 361..364
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 368..372
FT /evidence="ECO:0007829|PDB:5FL7"
FT TURN 381..383
FT /evidence="ECO:0007829|PDB:5FL7"
FT TURN 391..393
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 396..414
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 416..421
FT /evidence="ECO:0007829|PDB:5FL7"
FT TURN 422..425
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 429..445
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 453..456
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 466..476
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 485..487
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 497..505
FT /evidence="ECO:0007829|PDB:5FL7"
SQ SEQUENCE 509 AA; 54535 MW; FC26BAEF249DCA71 CRC64;
MVLPRLIPRL SRSAFKVAQA NNRVFNAPFR GMASSAGVGS GKIRTVIGAV VDVQFEQDNL
PAILNALTID RGEGNKLVLE VAQHLGENTV RTIAMDGTEG LVRGTSVADT GAPITIPVGR
GTLGRIINVC GEPIDERGPI EATKFLPIHA DPPTFAEQST TAEVLETGIK VVDLLAPYAR
GGKIGLFGGA GVGKTVFIQE LINNIAKAHG GFSVFCGVGE RTREGNDLYR EMKETGVINL
EGESKVTLVF GQMNEPPGAR ARVALTGLTI AEYFRDEEGQ DVLLFVDNIF RFTQAGSEVS
ALLGRIPSAV GYQPTLATDM GALQERITTT QKGSVTSVQA VYVPADDLTD PAPATTFAHL
DATTVLSRGI SELGIYPAVD PLDSKSRLLD IDVVGQEHYD VASNVQQTLQ AYKSLQDIIA
ILGMDELSEQ DKLTVERARK IQRFLSQPFT VAEVFTGIEG RLVSLKDTVR SFKEILDGKH
DALPEAAFYM VGGIEEVVAK AEKLAAESK
