ID M0ZV40_SOLTU Unreviewed; 488 AA.
AC M0ZV40;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
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 Name=102593980 {ECO:0000313|EnsemblPlants:PGSC0003DMT400008803};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400008803, ECO:0000313|Proteomes:UP000011115};
RN [1] {ECO:0000313|Proteomes:UP000011115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
RN [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400008803}
RP IDENTIFICATION.
RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400008803};
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
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 RefSeq; XP_006364499.1; XM_006364437.1.
DR RefSeq; XP_006364500.1; XM_006364438.2.
DR AlphaFoldDB; M0ZV40; -.
DR EnsemblPlants; PGSC0003DMT400008802; PGSC0003DMT400008802; PGSC0003DMG400003419.
DR EnsemblPlants; PGSC0003DMT400008803; PGSC0003DMT400008803; PGSC0003DMG400003419.
DR GeneID; 102593980; -.
DR Gramene; PGSC0003DMT400008802; PGSC0003DMT400008802; PGSC0003DMG400003419.
DR Gramene; PGSC0003DMT400008803; PGSC0003DMT400008803; PGSC0003DMG400003419.
DR Gramene; RHC01H1G4671.2.1; RHC01H1G4671.2.1; RHC01H1G4671.2.
DR KEGG; sot:102593980; -.
DR HOGENOM; CLU_022916_3_0_1; -.
DR OrthoDB; 5473721at2759; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; M0ZV40; baseline.
DR GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
DR GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
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:0046034; P:ATP metabolic process; IEA:InterPro.
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:SF32; VACUOLAR PROTON PUMP SUBUNIT B; 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}; Plastid {ECO:0000256|ARBA:ARBA00022640};
KW Reference proteome {ECO:0000313|Proteomes:UP000011115};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366021}.
FT DOMAIN 24..90
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 147..377
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
SQ SEQUENCE 488 AA; 54243 MW; 3523C4689B2810F3 CRC64;
MGSAPNNLEM EEGTLEVGME YRTVSGVAGP LVILDKVKGP KYQEIVNIRL GDGTTRRGQV
LEVDGEKAVV QVFEGTSGID NKYTTVQFTG EVLKTPVSLD MLGRIFNGSG KPIDNGPPIL
PEAYRDISGS SINPSERTYP EEMIQTGIST VDVMNSIARG QKIPLFSAAG LPHNEIAAQI
CRQAGLVKRL EKSDNLLEGG EEDNFAIVFA AMGVNMETAQ FFKRDFEENG SMERVTLFLN
LANDPTIERI ITPRIALTTA EYLAYECGKH VLVILTDMSS YADALREVSA AREEVPGRRG
YPGYMYTDLA TIYERAGRIE GRTGSITQIP ILTMPNDDIT HPTPDLTGYI TEGQIYIDRQ
LHNRQIYPPI NVLPSLSRLM KSAIGEGMTR RDHSDVSNQL YANYAIGKDV QAMKAVVGEE
ALSSEDLLYL EFLDKFERKF VSQGAYDTRN IFQSLDLAWT LLRIFPRELL HRIPAKTLDQ
YYSRDASN
//
