ID A0A0E0HHW0_ORYNI Unreviewed; 1350 AA.
AC A0A0E0HHW0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=ATP synthase subunit beta {ECO:0000256|RuleBase:RU003553};
DE EC=7.1.2.2 {ECO:0000256|RuleBase:RU003553};
OS Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4536 {ECO:0000313|EnsemblPlants:ONIVA05G26280.1};
RN [1] {ECO:0000313|EnsemblPlants:ONIVA05G26280.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA05G26280.1};
RA Wing R.A., Hsing Y.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ONIVA05G26280.1}
RP IDENTIFICATION.
RC STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA05G26280.1};
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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|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 STRING; 4536.A0A0E0HHW0; -.
DR EnsemblPlants; ONIVA05G26280.1; ONIVA05G26280.1; ONIVA05G26280.
DR Gramene; ONIVA05G26280.1; ONIVA05G26280.1; ONIVA05G26280.
DR eggNOG; KOG1350; Eukaryota.
DR eggNOG; KOG4302; Eukaryota.
DR HOGENOM; CLU_007035_0_0_1; -.
DR OMA; QRMQKLW; -.
DR Proteomes; UP000006591; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
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; 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 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:UP000006591};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 295..567
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1151..1234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1258..1291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 739..766
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 845..872
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 12..30
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1175..1201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1350 AA; 149204 MW; 2F90E523183FDB33 CRC64;
MHHTTPAPPR FSGSRRPGPP ANPPTRRYLH HPPHPLSSSS LRSPPLLLPS RGGRRNQKKK
KSNPRSRPRV SGDLAAMATR RALSSLVRAA SRLRGASPAP RPRGPLHRPS PSGYLFNRAA
AYATAAAAKE AAPPAPATGK ATGGGKITDE FTGAGAVGQV CQVIGAVVDV RFDEGLPPIL
TALEVLDHNI RLVLEVAQHL GENMVRTIAM DGTEGLVRGQ RVLNTGSPIT VPVGRATLGR
IMNVIGEPID EKGDITTNHF LPIHREAPAF VEQATEQQIL VTGIKVVDLL APYQRGGKIG
LFGGAGVGKT VLIMELINNV AKAHGGFSVF AGVGERTREG NDLYREMIES GVIKLGDKQS
ESKCALVYGQ MNEPPGARAR VGLTGLTVAE HFRDAEGQDV LLFIDNIFRF TQANSEVSAL
LGRIPSAVGY QPTLATDLGG LQERITTTKK GSITSVQAIY VPADDLTDPA PATTFAHLDA
TTVLSRQISE LGIYPAVDPL DSTSRMLSPH VLGEDHYNTA RGVQKVLQNY KNLQDIIAIL
GMDELSEDDK LTVARARKIQ RFLSQPFHVA EVFTGAPGKY VELKESVNSF QGVLDGKYDD
LPEQSFYMVG GIEEVIAKAE KIAKDCFEQF SSIPHHFPQN RAAVSGQIHA AAAAAAAAAE
DDAAVPSFRP PVSPSVEPSH RDWLRGIVLT RSGNPKERLL PMKTICGSLM HELQVIWDEV
GEPEAARDRM LLELEQECLE VYRRKVDQAN RSRAQLRQAI AQSEAELAAI CSAMGETTVH
VKQSNQKACG LRDELGAILP YLEEMKRKKV ERWNQFLDVV GRIKKISSEI RPANFDPFKV
SVDQSDLSLR KLEELRVELK SLEKEKGERV KQVMEYLKTL HSLCVVLGVD FKKTISEIHP
SLDEAEGPRN ISNTTIEMLA LAIQRLRETK MQRMQKLQDL ASTLLELWNL MDTPFEEQQA
YQNITCNIAA SEAELTEQNT LSIEFLNYVE AEVLRLEQHK ASKMKELVLK KKTELEEHRR
RAHLVGEEGA IDPSLLLEQI EAYISTVKEE AFSRKDILER VEKWLNAREE EAWLEDYNKD
DNRYNAGRGA HIMLKRAEKA RVLVSKIPGM VDVLETKTRA WETERGNEFT YDGVRLILML
EEYMVVRQEK EQERKRQRDQ KKLQDQRKAE QEALYGSKPS SSKSHSTKKV PRNSTPGVQP
PKSEILHSKT IRATKKTEDI NTPSPGHKGL DTVGLPIRKL FPSSNSSTLL EMETPRKPFS
QITPGNISSA PVRPISTGGT EENRTPKTFA PVPTTPMTVS PHMQMAVTPV LTAKAVSVLS
YDEPELTSQE DTEYSFEEKR LAVYLAAQVA
//
