ID   VATB_ENCCU              Reviewed;         477 AA.
AC   Q8SR34;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=V-type proton ATPase subunit B {ECO:0000250|UniProtKB:P16140};
DE            Short=V-ATPase subunit B;
DE   AltName: Full=Vacuolar proton pump subunit B;
GN   Name=VMA2 {ECO:0000250|UniProtKB:P16140}; OrderedLocusNames=ECU10_1040;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=16691553; DOI=10.1002/pmic.200500796;
RA   Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT   "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT   (microsporidia): a reference map for proteins expressed in late sporogonial
RT   stages.";
RL   Proteomics 6:3625-3635(2006).
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   -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC       {ECO:0000269|PubMed:16691553}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
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DR   EMBL; AL590449; CAD25823.1; -; Genomic_DNA.
DR   RefSeq; NP_586219.1; NM_001042052.1.
DR   AlphaFoldDB; Q8SR34; -.
DR   SMR; Q8SR34; -.
DR   STRING; 284813.Q8SR34; -.
DR   GeneID; 859868; -.
DR   KEGG; ecu:ECU10_1040; -.
DR   VEuPathDB; MicrosporidiaDB:ECU10_1040; -.
DR   HOGENOM; CLU_022916_3_0_1; -.
DR   InParanoid; Q8SR34; -.
DR   OMA; GFKIKPR; -.
DR   OrthoDB; 541116at2759; -.
DR   Proteomes; UP000000819; Chromosome X.
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   1: Evidence at protein level;
KW   ATP-binding; Hydrogen ion transport; Ion transport; Membrane;
KW   Nucleotide-binding; Reference proteome; Transport; Vacuole.
FT   CHAIN           1..477
FT                   /note="V-type proton ATPase subunit B"
FT                   /id="PRO_0000383328"
FT   BINDING         365
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P21281"
SQ   SEQUENCE   477 AA;  53108 MW;  6AADCBFA2B8EE716 CRC64;
     MLESVRIEPK MSYRKIVGVN GPLVIMDNIR FLKYAEMVSL TLPDGSVRQG QVLEVSGKKA
     VIQVFEGTAG IDVKETQVTF TGETMKMGMS EDVLGRIFNG SGRVIDGGPK IIPEDYLDIQ
     GQPLNPYARI YPEEMIQTGI SSIDVMNSIA RGQKIPIFSA SGLPHNEIAA QICRQAGLVK
     RKDSIDSSDD NFAIVFAAMG VNVETANFFR NSFEASGSIG RTALFLNLAN DPTIERIITP
     RLALTAAEYL AYEREKHVLV IMTDMSSYAD ALREVSAARE EVPGRRGYPG YMYTDLSTIY
     ERAGRLEGRN GSITQIPILT MPNDDITHPI PDLTGYITEG QIYVDRQMHN RQIYPPINVL
     PSLSRLMKSA IGEGMTRKDH GDVSNQLYAK YAIGKDAQAM KAVVGEDSLS AEDRISIEFL
     ERFEREFISQ RHDELRTVDQ SLDIAWDLLK VFPREMLNRI PSDILDEFHS VAPVGVE