ID   VATB_CANTR              Reviewed;         511 AA.
AC   P22550;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=V-type proton ATPase subunit B {ECO:0000303|PubMed:2147996};
DE            Short=V-ATPase subunit B;
DE   AltName: Full=V-ATPase 57 kDa subunit;
DE   AltName: Full=Vacuolar proton pump subunit B;
GN   Name=VMA2;
OS   Candida tropicalis (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2147996; DOI=10.1093/nar/18.24.7446;
RA   Gu H.H., Gallagher M.J., Rupkey S., Dean G.E.;
RT   "Gene and derived peptide sequences for C. tropicalis vacuolar ATPase
RT   subunit b.";
RL   Nucleic Acids Res. 18:7446-7446(1990).
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 (By similarity). V-ATPase is responsible for
CC       acidifying and maintaining the pH of intracellular compartments (By
CC       similarity). {ECO:0000250|UniProtKB:P16140}.
CC   -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral
CC       catalytic V1 complex (components A to H) attached to an integral
CC       membrane V0 proton pore complex (components: a, c, c', c'', d, e, f and
CC       VOA1). {ECO:0000250|UniProtKB:P16140}.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250|UniProtKB:P16140};
CC       Peripheral membrane protein {ECO:0000305}; Cytoplasmic side
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
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DR   EMBL; X54875; CAA38656.1; -; Genomic_DNA.
DR   PIR; S13080; S13080.
DR   AlphaFoldDB; P22550; -.
DR   SMR; P22550; -.
DR   PRIDE; P22550; -.
DR   VEuPathDB; FungiDB:CTMYA2_038580; -.
DR   VEuPathDB; FungiDB:CTRG_00643; -.
DR   GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   ATP-binding; Hydrogen ion transport; Ion transport; Membrane;
KW   Nucleotide-binding; Transport; Vacuole.
FT   CHAIN           1..511
FT                   /note="V-type proton ATPase subunit B"
FT                   /id="PRO_0000144645"
FT   REGION          484..511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        488..503
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         381
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P21281"
SQ   SEQUENCE   511 AA;  57200 MW;  1AF55FA4BB296AF0 CRC64;
     MSLTDKELFE LNKKAVTEGF KIKPRINYTP VGGVNGPLVI LDNVKFPRYN EIVNLTLPDG
     TVRQGQVLEV RGTKAIVQVF EGTSGIDVKK TRVEFTGENL KIPVSEDMLG RIFDGSGRPI
     DKGPKIFAED YLDINGSPIN PYARIYPEEM ISTGVSAIDT MNSIARGQKI PIFSASGLPH
     NEIAAQICRQ AGLVRPTKDV HDGHEENFSI VFAAMGVNLE TSRFFKQDFE ENGSLERTTL
     FLNLANDPTI ERIITPRLAL TTAEFLAYQT ERHVLTILTD MSSYADALRE VSAAREEVPG
     RRGYPGYMYT DLSTIYERAG RVEGRNGSIT QVPILTMPND DITHPIPDLT GYITEGQIFI
     DRQLHNRGIY PPINVLPSLS RLMKSAIGEG MTRKDHGDVS NQLYAKYAIG KDAAAMKAVV
     GEEALSTEDK LSLEFLEKFE KNFISQGAYE NRTIFESLDL AWSLLRIYPK EMLNRISPKI
     LEEFYGRDRE QDDDEEEEED PDKSGDKLID A