ID   A0A2X0KQG1_9BASI        Unreviewed;       512 AA.
AC   A0A2X0KQG1;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Vacuolar proton pump subunit B {ECO:0000256|RuleBase:RU366021};
DE            Short=V-ATPase subunit B {ECO:0000256|RuleBase:RU366021};
DE   AltName: Full=Vacuolar proton pump subunit B {ECO:0000256|RuleBase:RU366021};
GN   ORFNames=BZ3500_MVSOF-1268-A1-R1_CHR1-3G01694
GN   {ECO:0000313|EMBL:SCZ89965.1};
OS   Microbotryum saponariae.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX   NCBI_TaxID=289078 {ECO:0000313|EMBL:SCZ89965.1, ECO:0000313|Proteomes:UP000249723};
RN   [1] {ECO:0000313|Proteomes:UP000249723}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Jeantristanb JTB J.-T., Ricardo R.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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. V-ATPase is responsible for acidifying and
CC       maintaining the pH of intracellular compartments.
CC       {ECO:0000256|RuleBase:RU366021}.
CC   -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral
CC       catalytic V1 complex attached to an integral membrane V0 proton pore
CC       complex. {ECO:0000256|RuleBase:RU366021}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000256|ARBA:ARBA00008936, ECO:0000256|RuleBase:RU366021}.
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DR   EMBL; FMWP01000014; SCZ89965.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2X0KQG1; -.
DR   STRING; 289078.A0A2X0KQG1; -.
DR   Proteomes; UP000249723; Unassembled WGS sequence.
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   CDD; cd18112; ATP-synt_V_A-type_beta_C; 1.
DR   CDD; cd18118; ATP-synt_V_A-type_beta_N; 1.
DR   CDD; cd01135; V_A-ATPase_B; 1.
DR   Gene3D; 3.40.50.12240; -; 1.
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   NCBIfam; TIGR01040; V-ATPase_V1_B; 1.
DR   PANTHER; PTHR43389; V-TYPE PROTON ATPASE SUBUNIT B; 1.
DR   PANTHER; PTHR43389:SF4; V-TYPE PROTON ATPASE SUBUNIT B; 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; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781,
KW   ECO:0000256|RuleBase:RU366021};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU366021};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249723};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366021}.
FT   DOMAIN          38..104
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02874"
FT   DOMAIN          161..396
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT                   nucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00006"
SQ   SEQUENCE   512 AA;  56835 MW;  E6D77569D0C320EE CRC64;
     MPASSTDPRI SDREVHAINV AAAVRRYDVE PRLDYRTVSA VNGPLVVLDN VKFPSYNEIV
     QLTLPDGTVR GGQVLEVSGR KAIVQVFEGT SGIDVNATHV EFSGSSMKLP VSEDMLGRIF
     NGSGNPIDKG PKVFAEEYLD INGAPINPYS RIYPEEMIQT GISTIDVMNS IARGQKIPIF
     SASGLPHNEI AAQICRQAGL VNKGERNPDG APTKGIHDGH EDNFSIVFAA MGVNMETARF
     FRQDFEENGS LDRVTLFLNL ANDPTIERII TPRLALTTAE YYAYQLEKHV LVILTDMSSY
     ADALREVSAA REEVPGRRGY PGYMYTDLST IYERAGRVEG RNGSITQIPI LTMPNDDITH
     PIPDLTGYIT EGQISVDRQL NNRQIYPPIN VLPSLSRLMK SAIGEKLTRK DHGDVSNQMY
     SMYAIGKDAA AMKAVVGEEA LSQEEKLALS FLGRFENEFV NQGLNENRSI FDSLDLAWSL
     LRTFPREQLN RIPKKILDEF YSRKATKVTP QQ
//