ID D7KT90_ARALL Unreviewed; 486 AA.
AC D7KT90;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 13-SEP-2023, entry version 73.
DE RecName: Full=Vacuolar proton pump subunit B {ECO:0000256|RuleBase:RU366021};
DE Short=V-ATPase subunit B {ECO:0000256|RuleBase:RU366021};
DE AltName: Full=Vacuolar proton pump subunit B {ECO:0000256|RuleBase:RU366021};
GN ORFNames=ARALYDRAFT_476752 {ECO:0000313|EMBL:EFH63882.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|EMBL:EFH63882.1}
RP NUCLEOTIDE SEQUENCE.
RG US DOE Joint Genome Institute (JGI-PGF);
RA Ottilar R., Schmutz J., Salamov A., Cheng J.F., Lucas S., Pitluck S.,
RA Gundlach H., Guo Y., Haberer G., Nasrallah J., Mayer K.F.X.,
RA van de Peer Y., Weigel D., Grigoriev I.V.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EFH63882.1}
RP NUCLEOTIDE SEQUENCE.
RG US DOE Joint Genome Institute (JGI-PGF);
RA Bakker E., Bergelson J., Cheng J.Fang., Clark R.M., Fawcett J., Gaut B.,
RA Grigoriev I., Gundlach H., Guo Y., Haberer G., Hollister J., Hu T.T.,
RA Mayer K.F.X., Nasrallah J., Nordborg M., Otillar R., Pattyn P., Schmutz J.,
RA Spannagl M., van de Peer Y., Wang X., Weigel D., Yang L.;
RT "The basis of rapid genome size change in Arabidopsis.";
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Non-catalytic subunit of the V1 complex of vacuolar(H+)-
CC ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral
CC complex (V1) that hydrolyzes ATP and a membrane integral complex (V0)
CC that translocates protons. V-ATPase is responsible for acidifying and
CC maintaining the pH of intracellular compartments.
CC {ECO:0000256|RuleBase:RU366021}.
CC -!- FUNCTION: Non-catalytic subunit of the peripheral V1 complex of
CC vacuolar ATPase. V-ATPase is responsible for acidifying a variety of
CC intracellular compartments in eukaryotic cells.
CC {ECO:0000256|ARBA:ARBA00002690}.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral
CC catalytic V1 complex attached to an integral membrane V0 proton pore
CC complex. {ECO:0000256|RuleBase:RU366021}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000256|ARBA:ARBA00008936, ECO:0000256|RuleBase:RU366021}.
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DR EMBL; GL348714; EFH63882.1; -; Genomic_DNA.
DR RefSeq; XP_002887623.1; XM_002887577.1.
DR AlphaFoldDB; D7KT90; -.
DR STRING; 81972.D7KT90; -.
DR EnsemblPlants; fgenesh2_kg.2__1882__AT1G76030.1; fgenesh2_kg.2__1882__AT1G76030.1; fgenesh2_kg.2__1882__AT1G76030.1.
DR Gramene; fgenesh2_kg.2__1882__AT1G76030.1; fgenesh2_kg.2__1882__AT1G76030.1; fgenesh2_kg.2__1882__AT1G76030.1.
DR eggNOG; KOG1351; Eukaryota.
DR HOGENOM; CLU_022916_3_0_1; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblPlants.
DR GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
DR GO; GO:0051015; F:actin filament binding; IEA:EnsemblPlants.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0051017; P:actin filament bundle assembly; IEA:EnsemblPlants.
DR GO; GO:0051693; P:actin filament capping; IEA:EnsemblPlants.
DR GO; GO:0046034; P:ATP metabolic process; IEA:InterPro.
DR GO; GO:0010255; P:glucose mediated signaling pathway; IEA:EnsemblPlants.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:EnsemblPlants.
DR CDD; cd18112; ATP-synt_V_A-type_beta_C; 1.
DR CDD; cd18118; ATP-synt_V_A-type_beta_N; 1.
DR CDD; cd01135; V_A-ATPase_B; 1.
DR Gene3D; 3.40.50.12240; -; 1.
DR HAMAP; MF_00310; ATP_synth_B_arch; 1.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR005723; ATPase_V1-cplx_bsu.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022879; V-ATPase_su_B/beta.
DR NCBIfam; TIGR01040; V-ATPase_V1_B; 1.
DR PANTHER; PTHR43389; V-TYPE PROTON ATPASE SUBUNIT B; 1.
DR PANTHER; PTHR43389:SF22; V-TYPE PROTON ATPASE SUBUNIT B1-RELATED; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR PIRSF; PIRSF039114; V-ATPsynth_beta/V-ATPase_B; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781,
KW ECO:0000256|RuleBase:RU366021};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU366021};
KW Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366021}.
FT DOMAIN 22..88
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 145..375
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
SQ SEQUENCE 486 AA; 54064 MW; E533858E91FCAD57 CRC64;
MGTNDLDIEE GTLEIGMEYR TVSGVAGPLV ILDKVKGPKY QEIVNIRLGD GSTRRGQVLE
VDGEKAVVQV FEGTSGIDNK FTTVQFTGEV LKTPVSLDML GRIFNGSGKP IDNGPPILPE
AYLDISGSSI NPSERTYPEE MIQTGISTID VMNSIARGQK IPLFSAAGLP HNEIAAQICR
QAGLVKRLEK TVDLLEDHGE DNFAIVFAAM GVNMETAQFF KRDFEENGSM ERVTLFLNLA
NDPTIERIIT PRIALTTAEY LAYECGKHVL VILTDMSSYA DALREVSAAR EEVPGRRGYP
GYMYTDLATI YERAGRIEGR KGSITQIPIL TMPNDGITHP TPDLTGYITE GQIYIDRQLH
NRQIYPPINV LPSLSRLMKS AIGEGMTRKD HSDVSNQLYA NYAIGKDVQA MKAVVGEEAL
SSEDLLYLEF LDKFERKFVM QGAYDTRNIF QSLDLAWTLL RIFPRELLHR IPAKTLDQFY
SRDSTT
//
