ID A0A0D3GAJ4_9ORYZ Unreviewed; 1216 AA.
AC A0A0D3GAJ4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=ATP synthase subunit beta {ECO:0000256|RuleBase:RU003553};
DE EC=7.1.2.2 {ECO:0000256|RuleBase:RU003553};
OS Oryza barthii.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=65489 {ECO:0000313|EnsemblPlants:OBART05G25070.1};
RN [1] {ECO:0000313|EnsemblPlants:OBART05G25070.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART05G25070.1};
RX DOI=10.1007/s12284-009-9025-z;
RA Rounsley S., Marri P.R., Yu Y., He R., Sisneros N., Goicoechea J.L.,
RA Lee S.J., Angelova A., Kudrna D., Luo M., Affourtit J., Desany B.,
RA Knight J., Niazi F., Egholm M., Wing R.A.;
RT "De novo next generation sequencing of plant genomes.";
RL Rice 2:35-43(2009).
RN [2] {ECO:0000313|EnsemblPlants:OBART05G25070.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
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:0000256|ARBA:ARBA00003086}.
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. {ECO:0000256|RuleBase:RU003553}.
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:0000256|ARBA:ARBA00001741,
CC ECO:0000256|RuleBase:RU003553};
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:0000256|ARBA:ARBA00011648,
CC ECO:0000256|RuleBase:RU003553}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000256|ARBA:ARBA00008936}.
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DR AlphaFoldDB; A0A0D3GAJ4; -.
DR STRING; 65489.A0A0D3GAJ4; -.
DR PaxDb; 65489-OBART05G25070-1; -.
DR EnsemblPlants; OBART05G25070.1; OBART05G25070.1; OBART05G25070.
DR Gramene; OBART05G25070.1; OBART05G25070.1; OBART05G25070.
DR eggNOG; KOG1350; Eukaryota.
DR eggNOG; KOG4302; Eukaryota.
DR HOGENOM; CLU_007035_0_0_1; -.
DR Proteomes; UP000026960; Chromosome 5.
DR GO; GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1); IEA:InterPro.
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; IEA:UniProtKB-EC.
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; cd18115; ATP-synt_F1_beta_N; 1.
DR CDD; cd01133; F1-ATPase_beta_CD; 1.
DR Gene3D; 1.20.58.1520; -; 1.
DR Gene3D; 2.40.10.170; -; 1.
DR Gene3D; 1.10.10.910; ATP synthase, F1 beta subunit; 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; IPR042079; ATP_synt_F1_beta_sf.
DR InterPro; IPR020971; ATP_synth_F1_beta_su.
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:SF88; ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR Pfam; PF03999; MAP65_ASE1; 1.
DR Pfam; PF11421; Synthase_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 3: Inferred from homology;
KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310,
KW ECO:0000256|RuleBase:RU003553};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003553};
KW CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|RuleBase:RU003553};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003553};
KW Reference proteome {ECO:0000313|Proteomes:UP000026960};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 219..491
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 15..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1017..1075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1124..1157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 605..632
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 711..738
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1017..1038
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1067
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1216 AA; 134768 MW; 0AC8DB52A608EE5A CRC64;
MATRRALSSL VRAASRLRGA SPAPRPRGPL HRPSPAGYLF NRAAAYATAA AAKEAAPPAP
ATGKATAGGK ITDEFTGAGA VGQVCQVIGA VVDVRFDEGL PPILTALEVL DHNIRLVLEV
AQHLGENMVR TIAMDGTEGL VRGQRVLNTG SPITVPVGRA TLGRIMNVIG EPIDEKGDIT
TNHFLPIHRE APAFVEQATE QQILVTGIKV VDLLAPYQRG GKIGLFGGAG VGKTVLIMEL
INNVAKAHGG FSVFAGVGER TREGNDLYRE MIESGVIKLG DKQSESKCAL VYGQMNEPPG
ARARVGLTGL TVAEHFRDAE GQDVLLFIDN IFRFTQANSE VSALLGRIPS AVGYQPTLAT
DLGGLQERIT TTKKGSITSV QAIYVPADDL TDPAPATTFA HLDATTVLSR QISELGIYPA
VDPLDSTSRM LSPHVLGEDH YNTARGVQKV LQNYKNLQDI IAILGMDELS EDDKLTVARA
RKIQRFLSQP FHVAEVFTGA PGKYVELKES VNSFQGVLDG KYDDLPEQSF YMVGGIEEVI
AKAEKIAKEL RGIVLTRSGN PKERLLPMKT ICGSLMHELQ VIWDEIGEPE AARDRMLLEL
EQECLEVYRR KVDQANRSRA QLRQAIAQSE AELAAICSAM GETTVHVRQS NQKACGLRDE
LGAILPYLEE MKRKKVERWN QFLDVVGRIK KISSEIRPAN FDPFKVSVDQ SDLSLRKLEE
LRVELKSLEK EKGERVKQVM EYLKTLHSLC VVLGVDFKKT ISEIHPSLDE AEGPRNISNT
TIEMLALAIQ RLRETKMQRM QKLQDLASTL LELWNLMDTP FEEQQAYQNI TCNIAASEAE
LTEQNTLSIE FLNYVEAEVL RLEQHKASKM KELVLKKKTE LEEHRRRAHL VGEEGAIDPS
LLLEQIEAYI STVKEEAFSR KDILERVEKW LNAREEEAWL EDYNKDDNRY NAGRGAHIML
KRAEKARVLV SKIPGMVDVL ETKTRAWETE RGNEFTYDGV RLILMLEEYM VVRQEKEQER
KRQRDQKKLQ DQRKAEQEAL YGSKSSSSKS HSTKKVPRNS TPGVQPPKSE ILHSKTIRAA
KKTEDINTPS PGHKGLDTVG LPIRKLFPSS NSSTLLEMET PRKPFSQITP GNISSSPVRP
ISTGGTEENR TPKTFAPVPT TPMTVSPHMQ MAVTPVLTAK AVSVLSYDEP ELTSQEDTEY
SFEEKRLAVY LAAQVA
//
