ATPB_SCHPO
ID ATPB_SCHPO Reviewed; 525 AA.
AC P22068;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=ATP synthase subunit beta, mitochondrial;
DE EC=7.1.2.2;
DE Flags: Precursor;
GN Name=atp2; ORFNames=SPAC222.12c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 45-64.
RC STRAIN=972 / ATCC 24843;
RX PubMed=1831760; DOI=10.1111/j.1432-1033.1991.tb21048.x;
RA Falson P., Leterme S., Boutry M.;
RT "Beta subunit of mitochondrial F1-ATPase from the fission yeast. Deduced
RT sequence of the wild type protein and identification of a mutation that
RT increases nucleotide binding.";
RL Eur. J. Biochem. 200:61-67(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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 -!- 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.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC Note=Peripheral membrane protein.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB60704.1; -; Genomic_DNA.
DR PIR; S17211; S17211.
DR RefSeq; NP_593151.1; NM_001018548.2.
DR AlphaFoldDB; P22068; -.
DR SMR; P22068; -.
DR BioGRID; 278415; 30.
DR STRING; 4896.SPAC222.12c.1; -.
DR iPTMnet; P22068; -.
DR MaxQB; P22068; -.
DR PaxDb; P22068; -.
DR PRIDE; P22068; -.
DR EnsemblFungi; SPAC222.12c.1; SPAC222.12c.1:pep; SPAC222.12c.
DR GeneID; 2541927; -.
DR KEGG; spo:SPAC222.12c; -.
DR PomBase; SPAC222.12c; atp2.
DR VEuPathDB; FungiDB:SPAC222.12c; -.
DR eggNOG; KOG1350; Eukaryota.
DR HOGENOM; CLU_022398_0_2_1; -.
DR InParanoid; P22068; -.
DR OMA; GFNMIMD; -.
DR PhylomeDB; P22068; -.
DR Reactome; R-SPO-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-SPO-8949613; Cristae formation.
DR PRO; PR:P22068; -.
DR Proteomes; UP000002485; Chromosome I.
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; IGI:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central.
DR GO; GO:0043531; F:ADP binding; IMP:PomBase.
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 GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IGI:PomBase.
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 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 Transit peptide; Translocase; Transport.
FT TRANSIT 1..44
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:1831760"
FT CHAIN 45..525
FT /note="ATP synthase subunit beta, mitochondrial"
FT /id="PRO_0000002453"
FT BINDING 203..210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 525 AA; 56876 MW; 32BD77B0B24363F1 CRC64;
MLKKQALSGI RRFSLATKQS FVKTSYKLPR KSWLNTAKFN TIRYASTEAA KHNKGSIKQV
IGAVVDCQFE DADSLPSILN ALEVKLPDNK RLVLEVAQHV GENTVRTIAM DGTEGLVRGT
AVIDTGSPIS IPVGPGTLGR IMNVIGEPVD ERGPIKAVKY SPIHADAPSF EEQSTTPEIL
ETGIKVVDLL APYARGGKIG LFGGAGVGKT VFIQELINNI AKAHGGYSVF TGVGERTREG
NDLYREMQET GVIKLEGESK AALVFGQMNE PPGARARVAL TGLTVAEYFR DIEGQDVLLF
IDNIFRFTQA GSEVSALLGR IPSAVGYQPT LATDMGAMQE RITTTKKGSI TSVQAVYVPA
DDLTDPAPAT TFAHLDATTV LSRSISELGI YPAVDPLDSK SRMMDPRILG EEHYNLAGSV
QQMLQEYKSL QDIIAILGMD ELSEADKLTV ERARKVQRFL SQPFAVAEVF TGIEGRLVSL
KDTIRSFKEI LEGKHDSLPE SAFYMVGSID DAVKKAEKIA QELAA
