ID D3QYZ8_MAGIU Unreviewed; 463 AA.
AC D3QYZ8;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=V-type ATP synthase beta chain {ECO:0000256|HAMAP-Rule:MF_00310};
DE AltName: Full=V-ATPase subunit B {ECO:0000256|HAMAP-Rule:MF_00310};
GN Name=atpB {ECO:0000256|HAMAP-Rule:MF_00310};
GN OrderedLocusNames=HMPREF0868_1428 {ECO:0000313|EMBL:ADC91736.1};
OS Mageeibacillus indolicus (strain UPII9-5) (Clostridiales genomosp. BVAB3
OS (strain UPII9-5)).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Mageeibacillus.
OX NCBI_TaxID=699246 {ECO:0000313|EMBL:ADC91736.1, ECO:0000313|Proteomes:UP000008234};
RN [1] {ECO:0000313|Proteomes:UP000008234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UPII9-5 {ECO:0000313|Proteomes:UP000008234};
RA Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RT "Sequence of Clostridiales genomosp. BVAB3 str. UPII9-5.";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. The V-type beta chain is a regulatory subunit.
CC {ECO:0000256|HAMAP-Rule:MF_00310}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000256|ARBA:ARBA00008936, ECO:0000256|HAMAP-Rule:MF_00310}.
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DR EMBL; CP001850; ADC91736.1; -; Genomic_DNA.
DR RefSeq; WP_012992931.1; NC_013895.2.
DR AlphaFoldDB; D3QYZ8; -.
DR STRING; 699246.HMPREF0868_1428; -.
DR KEGG; clo:HMPREF0868_1428; -.
DR eggNOG; COG1156; Bacteria.
DR HOGENOM; CLU_022916_0_0_9; -.
DR OrthoDB; 9802718at2; -.
DR Proteomes; UP000008234; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR GO; GO:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IEA:UniProtKB-UniRule.
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; IPR027417; P-loop_NTPase.
DR InterPro; IPR022879; V-ATPase_su_B/beta.
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; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW ATP synthesis {ECO:0000256|HAMAP-Rule:MF_00310};
KW Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_00310};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW Rule:MF_00310}; Reference proteome {ECO:0000313|Proteomes:UP000008234};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00310}.
FT DOMAIN 9..74
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 131..350
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
SQ SEQUENCE 463 AA; 51787 MW; 87DD70127D03EDC4 CRC64;
MAKEYQTIEE VAGPLMLVRK VQDVKYYEMG EIELPNGELR RCRVLEINGE NALVQLFENS
VGINIQDSKV RFLGHGLELP VSEDMLGRVF DGMGHPADGG PELIPEARMD VNGLPLNPTA
RDYPDEFIQT GVSAIDGLNT LVRGQKLPIF SASGLPHSQL GAQIARQAKV IGDKEQKFAV
VFAAMGITFE EADYFIKDFQ RTGAIDRTVL FINLADQPAI ERIATPRMAL TCAEYLAFKK
DMHVLVIMTD ITYYAEALRE VSAARKEVPG RRGYPGYLYT DLATMYERAG RVKGKKGSIT
MVPILTMPDE DKTHPIPDLT GYITEGQIIL SRELYKKGLR PPVDVLPSLS RLKDKGIGEG
KTREDHAGTM NQLFAAYSRG KDARELAVIL GESSLSEMDR LYARFATEFE EKYVSQGFDT
NRSIEETLDL GWKLLGILPR SELKRIKESI LDKYYVPADP MKH
//
