VATB_PLAFA
ID VATB_PLAFA Reviewed; 494 AA.
AC Q25691;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=V-type proton ATPase subunit B;
DE Short=V-ATPase subunit B;
DE AltName: Full=Vacuolar proton pump subunit B;
GN Name=VAPB;
OS Plasmodium falciparum.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5833;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7935619; DOI=10.1016/0166-6851(94)90121-x;
RA Karcz S.R., Herrmann V.R., Cowman A.F.;
RT "Cloning and characterization of the vacuolar ATPase B subunit from
RT Plasmodium falciparum.";
RL Mol. Biochem. Parasitol. 65:123-133(1994).
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 -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral
CC catalytic V1 complex (main components: subunits A, B, C, D, E, and F)
CC attached to an integral membrane V0 proton pore complex (main
CC component: the proteolipid protein).
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
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DR EMBL; U03915; AAA20218.1; -; mRNA.
DR AlphaFoldDB; Q25691; -.
DR SMR; Q25691; -.
DR PRIDE; Q25691; -.
DR EnsemblProtists; CAD49154; CAD49154; PF3D7_0406100.
DR VEuPathDB; PlasmoDB:PF3D7_0406100; -.
DR VEuPathDB; PlasmoDB:Pf7G8-2_000099600; -.
DR VEuPathDB; PlasmoDB:Pf7G8_040011400; -.
DR VEuPathDB; PlasmoDB:PfCD01_040011200; -.
DR VEuPathDB; PlasmoDB:PfDd2_040011500; -.
DR VEuPathDB; PlasmoDB:PfGA01_040011100; -.
DR VEuPathDB; PlasmoDB:PfGB4_040011600; -.
DR VEuPathDB; PlasmoDB:PfGN01_040011500; -.
DR VEuPathDB; PlasmoDB:PfHB3_040010300; -.
DR VEuPathDB; PlasmoDB:PfIT_040010800; -.
DR VEuPathDB; PlasmoDB:PfKE01_040012800; -.
DR VEuPathDB; PlasmoDB:PfKH01_040011200; -.
DR VEuPathDB; PlasmoDB:PfKH02_040011000; -.
DR VEuPathDB; PlasmoDB:PfML01_040012000; -.
DR VEuPathDB; PlasmoDB:PfNF135_040012000; -.
DR VEuPathDB; PlasmoDB:PfNF166_040012700; -.
DR VEuPathDB; PlasmoDB:PfNF54_040011800; -.
DR VEuPathDB; PlasmoDB:PfSD01_070021700; -.
DR VEuPathDB; PlasmoDB:PfSN01_040011200; -.
DR VEuPathDB; PlasmoDB:PfTG01_040011500; -.
DR OMA; GFKIKPR; -.
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 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 PANTHER; PTHR43389; PTHR43389; 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; SSF52540; 1.
DR TIGRFAMs; TIGR01040; V-ATPase_V1_B; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 2: Evidence at transcript level;
KW Hydrogen ion transport; Ion transport; Transport.
FT CHAIN 1..494
FT /note="V-type proton ATPase subunit B"
FT /id="PRO_0000144635"
SQ SEQUENCE 494 AA; 55789 MW; 4858BEED57064D56 CRC64;
MSKEVVNTKA EASRVNALAA VRNYKVCPRL EYKTISGVQG PLVIIEDVKF PKYSEIVTIH
LSDNTTRQGQ ILEVCGKKAV IQVFEGTSGI DNKNSYVEVS GDILKMPMSD EMLGRVFNGS
GKPIDKGPNI LADDYLDING NPINPQCRVY PKEMIQTGIS TIDVMNSIVR GQKIPLFSAA
GLPHNEIGAQ ICRQASLVQG KDVLDHSDDN FAVVFGAMGV NMETARYFRQ DFEENGKMER
VCLFLNLAND PTIERILTPR IALTTAEYLA FEKEMHVFVI LTDMSSYADA LREVSSAREE
VPGRRGYPGY MYSDLSTIYE RAGRVEGRNG SITQFPILTM PNDDITHPIP DLTGYITEGQ
IFVDRNLYNR QIYPPINVLP SLSRLMKSGI GHNMTRIDHP YVSDQLYSNY AIAQDVKAMK
AVIGEEALSN DDILYLEFLD KFEKRFITQN TYECRDIYQS LDIAWELLRI FPEDMLKKIK
TDILSKYYPR HHAN