ID   VATB_NEUCR              Reviewed;         513 AA.
AC   P11593; Q7RVH9;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 169.
DE   RecName: Full=V-type proton ATPase subunit B {ECO:0000250|UniProtKB:P16140};
DE            Short=V-ATPase subunit B;
DE   AltName: Full=V-ATPase 57 kDa subunit;
DE   AltName: Full=Vacuolar proton pump subunit B;
GN   Name=vma-2 {ECO:0000303|PubMed:2844751}; ORFNames=B18P7.150, NCU08515;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2844751; DOI=10.1016/s0021-9258(18)68176-1;
RA   Bowman B.J., Allen R., Wechser M.A., Bowman E.J.;
RT   "Isolation of genes encoding the Neurospora vacuolar ATPase. Analysis of
RT   vma-2 encoding the 57-kDa polypeptide and comparison to vma-1.";
RL   J. Biol. Chem. 263:14002-14007(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; J03956; AAA33622.1; -; Genomic_DNA.
DR   EMBL; BX842594; CAE75688.1; -; Genomic_DNA.
DR   EMBL; CM002237; EAA33929.1; -; Genomic_DNA.
DR   PIR; A30800; A30800.
DR   RefSeq; XP_963165.1; XM_958072.3.
DR   AlphaFoldDB; P11593; -.
DR   SMR; P11593; -.
DR   STRING; 5141.EFNCRP00000008447; -.
DR   PRIDE; P11593; -.
DR   EnsemblFungi; EAA33929; EAA33929; NCU08515.
DR   GeneID; 3879313; -.
DR   KEGG; ncr:NCU08515; -.
DR   VEuPathDB; FungiDB:NCU08515; -.
DR   HOGENOM; CLU_022916_3_0_1; -.
DR   InParanoid; P11593; -.
DR   OMA; GFKIKPR; -.
DR   Proteomes; UP000001805; Chromosome 6, Linkage Group II.
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:0007035; P:vacuolar acidification; IBA:GO_Central.
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; Reference proteome; Transport; Vacuole.
FT   CHAIN           1..513
FT                   /note="V-type proton ATPase subunit B"
FT                   /id="PRO_0000144646"
FT   REGION          484..513
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        484..507
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         375
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P21281"
SQ   SEQUENCE   513 AA;  56808 MW;  F91E371C1DAB0269 CRC64;
     MADPRVPSSY NVTPRIRYNT VGGVNGPLVI LDNVKFPRYN EIVTLTLPDG TQRSGQVLEA
     RGNRAVVQVF EGTSGIDVKK TKVEFTGESL KLGVSEDMLG RIFDGSGRAI DKGPKVLAEE
     YLDINGSPIN PYAREYPQEM ISTGISAIDT MNSIARGQKI PIFSAAGLPH NEIAAQICRQ
     AGLVQRQGIT NKGVHDGHEE NFSIVFGAMG VNLETARFFT RDFEENGSLG RTTLFLNLAN
     DPTIERIITP RLALTTAEYY AYQLEKHVLV ILTDLSSYCD ALREVSAARE EVPGRRGFPG
     YMYTDLSTIY ERAGRVAGRN GSITQIPILT MPNDDITHPI PDLTGYITEG QIFVDRGLHN
     RGIYPPINVL PSLSRLMKSA IGEGMTRKDH GDVSNQLYAK YAIGRDAAAM KAVVGEEALS
     NEDKLSLEFL DKFERSFIAQ GPYESRTIFE SLDLAWSLLR IYRKDMLNRI PKKIIDEFYS
     RSAADRKGKG KDKPTTKDTR DTAAPEEENL IDA