ID I7I8T2_BABMR Unreviewed; 484 AA.
AC I7I8T2;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=BMR1_02g02380 {ECO:0000313|EMBL:CCF73633.1};
OS Babesia microti (strain RI).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Babesiidae; Babesia.
OX NCBI_TaxID=1133968 {ECO:0000313|EMBL:CCF73633.1, ECO:0000313|Proteomes:UP000002899};
RN [1] {ECO:0000313|EMBL:CCF73633.1, ECO:0000313|Proteomes:UP000002899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RI {ECO:0000313|EMBL:CCF73633.1,
RC ECO:0000313|Proteomes:UP000002899};
RX PubMed=22833609; DOI=10.1093/nar/gks700;
RA Cornillot E., Hadj-Kaddour K., Dassouli A., Noel B., Ranwez V.,
RA Vacherie B., Augagneur Y., Bres V., Duclos A., Randazzo S., Carcy B.,
RA Debierre-Grockiego F., Delbecq S., Moubri-Menage K., Shams-Eldin H.,
RA Usmani-Brown S., Bringaud F., Wincker P., Vivares C.P., Schwarz R.T.,
RA Schetters T.P., Krause P.J., Gorenflot A., Berry V., Barbe V.,
RA Ben Mamoun C.;
RT "Sequencing of the smallest Apicomplexan genome from the human pathogen
RT Babesia microti.";
RL Nucleic Acids Res. 40:9102-9114(2012).
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; FO082872; CCF73633.1; -; Genomic_DNA.
DR RefSeq; XP_012648242.1; XM_012792788.1.
DR AlphaFoldDB; I7I8T2; -.
DR GeneID; 24424261; -.
DR KEGG; bmic:BMR1_02g02380; -.
DR VEuPathDB; PiroplasmaDB:BMR1_02g02380; -.
DR OMA; GFKIKPR; -.
DR OrthoDB; 5473721at2759; -.
DR Proteomes; UP000002899; Chromosome II.
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:UP000002899};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366021}.
FT DOMAIN 26..88
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 149..374
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
SQ SEQUENCE 484 AA; 53669 MW; 7A2AEF7A8A2BF60F CRC64;
MVALDYSPAV KASLISFSPS LEYKTIVGVR GPLVILDNVR HPRFAEIVTI KLGDGSMRRG
QVLEVCGNKA VVQVFEGTSG IDNQSCSVEV SGDLLNLGVS EDMLGRVFNG SGNPLDSGDR
IIAEDYRDVN GFSINPVCRQ HPREMLETGI SAIDVMSSIV LGQKIPLFSA AGLPHNEIGA
QLCRQSALVG GKDVFDRHQD NFAIIFAAMG INMETATFFR RDFEKSATIG RVALFLNLAN
DPAVERIITP RLALTTAEYL AFDREMNVFV IMTDMTSYAD ALREVSAARD EVPGRRGYPG
YMYTDLSSLY ERSGRVLGCN GSITQFPILT MPNDDITHPI PDLTGYITEG QIFVDRALHN
RNIYPPINVL PSLSRLMKSG IGDGMTRADH PAVSDQLYSN YALGQDTRSM KAVVGEEALT
ADDLLYLEFT DKFESRFLNQ GPYERRTITQ SLDICWELLR TFPEDMLKKI KKDTLKKYYP
REGI
//
