ID B7XHX2_ENTBH Unreviewed; 467 AA.
AC B7XHX2;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 61.
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=EBI_22817 {ECO:0000313|EMBL:EED44432.1};
OS Enterocytozoon bieneusi (strain H348) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Enterocytozoonidae;
OC Enterocytozoon.
OX NCBI_TaxID=481877 {ECO:0000313|EMBL:EED44432.1, ECO:0000313|Proteomes:UP000001742};
RN [1] {ECO:0000313|EMBL:EED44432.1, ECO:0000313|Proteomes:UP000001742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H348 {ECO:0000313|EMBL:EED44432.1,
RC ECO:0000313|Proteomes:UP000001742};
RX PubMed=18060071; DOI=10.1371/journal.pone.0001277;
RA Corradi N., Akiyoshi D.E., Morrison H.G., Feng X., Weiss L.M., Tzipori S.,
RA Keeling P.J.;
RT "Patterns of genome evolution among the microsporidian parasites
RT Encephalitozoon cuniculi, Antonospora locustae and Enterocytozoon
RT bieneusi.";
RL PLoS ONE 2:E1277-E1277(2007).
RN [2] {ECO:0000313|EMBL:EED44432.1, ECO:0000313|Proteomes:UP000001742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H348 {ECO:0000313|EMBL:EED44432.1,
RC ECO:0000313|Proteomes:UP000001742};
RX PubMed=19132089; DOI=10.1371/journal.ppat.1000261;
RA Akiyoshi D.E., Morrison H.G., Lei S., Feng X., Zhang Q., Corradi N.,
RA Mayanja H., Tumwine J.K., Keeling P.J., Weiss L.M., Tzipori S.;
RT "Genomic survey of the non-cultivatable opportunistic human pathogen,
RT Enterocytozoon bieneusi.";
RL PLoS Pathog. 5:E1000261-E1000261(2009).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EED44432.1}.
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DR EMBL; ABGB01000016; EED44432.1; -; Genomic_DNA.
DR RefSeq; XP_002649600.1; XM_002649554.1.
DR AlphaFoldDB; B7XHX2; -.
DR STRING; 481877.B7XHX2; -.
DR VEuPathDB; MicrosporidiaDB:EBI_22817; -.
DR HOGENOM; CLU_022916_3_0_1; -.
DR InParanoid; B7XHX2; -.
DR OMA; GFKIKPR; -.
DR OrthoDB; 5473721at2759; -.
DR Proteomes; UP000001742; 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:0016787; F:hydrolase activity; 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 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}; Hydrolase {ECO:0000313|EMBL:EED44432.1};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU366021};
KW Reference proteome {ECO:0000313|Proteomes:UP000001742};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366021}.
FT DOMAIN 14..80
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 137..362
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
SQ SEQUENCE 467 AA; 52180 MW; 2DFADC336059E829 CRC64;
MFSKIEPTLT YKHISGVNGP LVILDNIRYL KYSEIVNLIL PNGEVRRGQV LEVLGKRAVV
QVFEGTSGID VNNTQVTFTG DILKMNVSED MLGRIFDGSS NVIDGGPPII PDDYLSIEGQ
PLNPEARIYP EEMIQTGISA IDVMSSIARG QKIPIFSGSG LPHNELAAQI CRQAGLVKKK
DCLDMSEDNF CIVFGAIGVN METAKFFKDQ FEENGSLERT VCFLNLASDP TIERIITPRL
VLTASEYLAY ETERHVLTIM TDISSYADAL REVSAAREEV PGRRGYPGYM YTDLSTLYER
AGRIEGKNGS ITQIPILTMP NDDITHPIPD LTGYITEGQI YIDRKMHNAG IYPPINVLPS
LSRLMKSAIG EGRTRKDHAD VSNQLYAKYA IGKDALAMKT IIGEESLNEE DKLATDFLNK
FEKTFISQGK NENRTIYDSL DKGWELLKTF PKHMLNRIPK NILDEFY
//
