ATPB_DICDI
ID ATPB_DICDI Reviewed; 651 AA.
AC Q55CS9;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 128.
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}; Synonyms=atp5b;
GN ORFNames=DDB_G0269916;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP PROTEIN SEQUENCE OF 120-130; 252-289 AND 605-613, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RA Bienvenut W.V., Patel H., Brunton V.G., Frame M.C.;
RL Submitted (JUL-2007) to UniProtKB.
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16512674; DOI=10.1021/pr050350q;
RA Reinders Y., Schulz I., Graef R., Sickmann A.;
RT "Identification of novel centrosomal proteins in Dictyostelium discoideum
RT by comparative proteomic approaches.";
RL J. Proteome Res. 5:589-598(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=AX2;
RX PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA Soldati T.;
RT "Proteomics fingerprinting of phagosome maturation and evidence for the
RT role of a Galpha during uptake.";
RL Mol. Cell. Proteomics 5:2228-2243(2006).
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 (By
CC similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
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 EMBL; AAFI02000005; EAL72308.1; -; Genomic_DNA.
DR RefSeq; XP_646402.1; XM_641310.1.
DR AlphaFoldDB; Q55CS9; -.
DR SMR; Q55CS9; -.
DR IntAct; Q55CS9; 1.
DR STRING; 44689.DDB0233951; -.
DR PaxDb; Q55CS9; -.
DR EnsemblProtists; EAL72308; EAL72308; DDB_G0269916.
DR GeneID; 8617357; -.
DR KEGG; ddi:DDB_G0269916; -.
DR dictyBase; DDB_G0269916; atp5b.
DR eggNOG; KOG1350; Eukaryota.
DR HOGENOM; CLU_022398_0_2_1; -.
DR InParanoid; Q55CS9; -.
DR OMA; GFNMIMD; -.
DR PhylomeDB; Q55CS9; -.
DR Reactome; R-DDI-1268020; Mitochondrial protein import.
DR PRO; PR:Q55CS9; -.
DR Proteomes; UP000002195; Chromosome 1.
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; ISS:dictyBase.
DR GO; GO:0005739; C:mitochondrion; ISS:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
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:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; ISS:dictyBase.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; ISS:dictyBase.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IBA:GO_Central.
DR GO; GO:0046689; P:response to mercury ion; IDA:dictyBase.
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; 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.
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..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 31..651
FT /note="ATP synthase subunit beta, mitochondrial"
FT /id="PRO_0000328545"
FT BINDING 257..264
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00829"
FT BINDING 289
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00829"
SQ SEQUENCE 651 AA; 70845 MW; CE772BF38410CD8F CRC64;
MFVARRLSKN ITQISKTAVK TSVRAVPVRG FKTTSVNQAA APAPKTSQEK EYFEKNKSLL
DKESNEESTE VDYSKLNENQ GVVHQVIGAV VDVYFPHGKL PYINDALIVD DFQAENVEKV
IEDLNNPSLK GKIDFNNVPI SNIKLVLEVA QHLGDGIVRC VALDITDGLG RGALVLNTGS
PLMVPVGQAT LGRIMNVIGE PIDGCGPIPA TEKRPIWRAP PPFADLAPSA SILETGIKVI
DLLAPYSRGG KIGLFGGAGV GKTVLIQELI NNIAKAHGGF SVFTGVGERT REGNDLYHEM
VEAGVIKKEG PGSKVALVFG QMNEPPGARA RVTLTGLTVA EYFRDAEGQD VLLFIDNIFR
FTQAGSEMSA LLGRIPSAVG YQPTLATDMG CMQERIATTK KGSITSVQAV YVPADDLTDP
APATTFAHLD ATTVLSRAIS ELGIYPCVDP LDSTSLMMDP NIIGVEHYKV ATDVQKILQE
YKSLQDIIAI LGMDDLSEDQ KATVFRARKI QRFLSQPFEV AHAFTNMEGR FVKLSDSIKA
FKGILEGKYD HLPEAAFYMV GGIEDVEIKA AKLLESAGKE EKKTTTTSTT GQVKEETVRE
KVTRLVDEAY NAKVKKLKEY GASTAHLEEL RAQYEKNFES EISQLEVLLK K
