ID VATB_HYPBU Reviewed; 476 AA.
AC A2BKX5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=V-type ATP synthase beta chain {ECO:0000255|HAMAP-Rule:MF_00310};
DE AltName: Full=V-ATPase subunit B {ECO:0000255|HAMAP-Rule:MF_00310};
GN Name=atpB {ECO:0000255|HAMAP-Rule:MF_00310}; OrderedLocusNames=Hbut_0783;
OS Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC Hyperthermus.
OX NCBI_TaxID=415426;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5456 / JCM 9403 / PLM1-5;
RX PubMed=17350933; DOI=10.1155/2007/745987;
RA Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M.,
RA She Q., Garrett R.A., Klenk H.-P.;
RT "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide
RT fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.";
RL Archaea 2:127-135(2007).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. The archaeal beta chain is a regulatory subunit.
CC {ECO:0000255|HAMAP-Rule:MF_00310}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|HAMAP-Rule:MF_00310}.
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DR EMBL; CP000493; ABM80636.1; -; Genomic_DNA.
DR AlphaFoldDB; A2BKX5; -.
DR SMR; A2BKX5; -.
DR STRING; 415426.Hbut_0783; -.
DR EnsemblBacteria; ABM80636; ABM80636; Hbut_0783.
DR KEGG; hbu:Hbut_0783; -.
DR eggNOG; arCOG00865; Archaea.
DR HOGENOM; CLU_022916_0_0_2; -.
DR OrthoDB; 32941at2157; -.
DR Proteomes; UP000002593; 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; Hydrogen ion transport; Ion transport; Reference proteome;
KW Transport.
FT CHAIN 1..476
FT /note="V-type ATP synthase beta chain"
FT /id="PRO_0000322500"
SQ SEQUENCE 476 AA; 52953 MW; 5DD000F26AA10425 CRC64;
MEAAMGPSPV IREYETIREV RGPLLIVEGI SDAAYDEIVE VELPSGERRR GRVLETARGY
AVVQVFEGTT GISVTGTKVR FLGRTLEIKV SDEMLGRVFN GLGDPIDGGP PITSGVRRDI
NGEPLNPAAR AYPEDFIQTG ISAIDGMNTM VRGQKLPIFS GSGLPHNKLA VQIARQATVR
SGEEFAVVFA AIGVMYDEAI FFKRFFEETG AIKRAALFIN LADEPASVRL ITPRVALTLA
EHLAFDLGMH VLVILTDMTN YCEALREISA AREEVPGRQG YPGYMYSDLA SIYERAGRAH
GRKGSITQMP ILTMPNDDIT HPIPDLTGYI TEGQIVLSRE LHNRGIYPPI NVLMSLSRLM
KEGIGPGKTR EDHANVSDQL YTAYSRAVEL RSLAAIVGEE SLSEVDRKYL RFGEAFEQRF
LKQGFYENRS IEETLDLAWE ILSILPESEL YKIKDEYIRK YHPKYRKKQS QSSGGK
//
