ID   VATB_CANAL              Reviewed;         512 AA.
AC   Q59PT0; A0A1D8PT25;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=V-type proton ATPase subunit B {ECO:0000250|UniProtKB:P16140};
DE            Short=V-ATPase subunit B {ECO:0000250|UniProtKB:P16140};
DE   AltName: Full=Vacuolar proton pump subunit B {ECO:0000250|UniProtKB:P16140};
GN   Name=VMA2 {ECO:0000303|PubMed:25038082};
GN   OrderedLocusNames=CAALFM_CR05780WA; ORFNames=CaO19.13955, CaO19.6634;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN   [4]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=25038082; DOI=10.1128/ec.00135-14;
RA   Rane H.S., Bernardo S.M., Hayek S.R., Binder J.L., Parra K.J., Lee S.A.;
RT   "The contribution of Candida albicans vacuolar ATPase subunit V1B encoded
RT   by VMA2 to stress response, autophagy, and virulence is independent of
RT   environmental pH.";
RL   Eukaryot. Cell 13:1207-1221(2014).
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). Plays an important role in
CC       resistance to several stresses, as well as in autophagy and virulence
CC       (PubMed:25038082). {ECO:0000250|UniProtKB:P16140,
CC       ECO:0000269|PubMed:25038082}.
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   -!- DISRUPTION PHENOTYPE: Results in the inability to grow at alcaline pH
CC       and altered resistance to calcium, osmotic stress, cold temperature,
CC       antifungal drugs and growth on non-fermentable carbon sources. Leads
CC       also to unability to fully assemble the V-ATPase at the vacuolar
CC       membrane and impairs its proton transport and ATPase activities.
CC       Finally, leads to autophagy defect and avirulence in a Caenorhabditis
CC       elegans infection model. {ECO:0000269|PubMed:25038082}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
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DR   EMBL; CP017630; AOW31294.1; -; Genomic_DNA.
DR   RefSeq; XP_711700.1; XM_706608.1.
DR   AlphaFoldDB; Q59PT0; -.
DR   SMR; Q59PT0; -.
DR   BioGRID; 1229299; 3.
DR   STRING; 237561.Q59PT0; -.
DR   PRIDE; Q59PT0; -.
DR   GeneID; 3646710; -.
DR   KEGG; cal:CAALFM_CR05780WA; -.
DR   CGD; CAL0000199755; VMA2.
DR   VEuPathDB; FungiDB:CR_05780W_A; -.
DR   eggNOG; KOG1351; Eukaryota.
DR   HOGENOM; CLU_022916_3_0_1; -.
DR   InParanoid; Q59PT0; -.
DR   OMA; GFKIKPR; -.
DR   OrthoDB; 541116at2759; -.
DR   PRO; PR:Q59PT0; -.
DR   Proteomes; UP000000559; Chromosome R.
DR   GO; GO:0005886; C:plasma membrane; IDA:CGD.
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; IBA:GO_Central.
DR   GO; GO:0046034; P:ATP metabolic process; IEA:InterPro.
DR   GO; GO:0006914; P:autophagy; IMP:CGD.
DR   GO; GO:0007035; P:vacuolar acidification; IMP:CGD.
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; Autophagy; Hydrogen ion transport; Ion transport; Membrane;
KW   Nucleotide-binding; Reference proteome; Transport; Vacuole; Virulence.
FT   CHAIN           1..512
FT                   /note="V-type proton ATPase subunit B"
FT                   /id="PRO_0000430554"
FT   REGION          484..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        488..504
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"
FT   SITE            378
FT                   /note="Required for activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10106"
SQ   SEQUENCE   512 AA;  57224 MW;  45CC68D4CE23D046 CRC64;
     MSLSDKELFE LNKKAVTEGF KIKPRINYNT VGGVNGPLVI LDNVKFPRYN EIVNLTLPDG
     SVRQGQVLEV 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 NRSIFESLDL AWSLLRIYPK ELLNRISPKI
     LEELYGRDRE QDDDEDEDEE DPDKSGDKLI DA