ID   VATB_METBU              Reviewed;         460 AA.
AC   Q12WL0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=Mbur_1244;
OS   Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS   ACE-M).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX   NCBI_TaxID=259564;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M;
RX   PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA   Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA   De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L.,
RA   Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N.,
RA   Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T.,
RA   Cavicchioli R.;
RT   "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT   burtonii: the role of genome evolution in cold adaptation.";
RL   ISME J. 3:1012-1035(2009).
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; CP000300; ABE52166.1; -; Genomic_DNA.
DR   RefSeq; WP_011499312.1; NC_007955.1.
DR   AlphaFoldDB; Q12WL0; -.
DR   SMR; Q12WL0; -.
DR   STRING; 259564.Mbur_1244; -.
DR   EnsemblBacteria; ABE52166; ABE52166; Mbur_1244.
DR   GeneID; 3998568; -.
DR   KEGG; mbu:Mbur_1244; -.
DR   HOGENOM; CLU_022916_0_0_2; -.
DR   OMA; GFKIKPR; -.
DR   OrthoDB; 8899at2157; -.
DR   Proteomes; UP000001979; Chromosome.
DR   GO; GO:0033178; C:proton-transporting two-sector ATPase complex, catalytic domain; IEA:InterPro.
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   HAMAP; MF_00310; ATP_synth_B_arch; 1.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR005724; ATPase_A1-cplx_bsu.
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; PTHR43389; 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; SSF52540; 1.
DR   TIGRFAMs; TIGR01041; ATP_syn_B_arch; 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..460
FT                   /note="V-type ATP synthase beta chain"
FT                   /id="PRO_1000059376"
SQ   SEQUENCE   460 AA;  50841 MW;  99AF0303BD332357 CRC64;
     MTKEYKTIVE VSGPLIFLEK TEPVGYGELV QINLPDGTTK RGQVLDTSAD MVVVQVFEGT
     VGLNEESGVV FSGETIKLPV SKDMLGRILS GAGEPLDGGP RIIPDKRVDI NGASMNPYSR
     MPPEDFIQTG ISTIDGTNTL VRGQKLPIFS GSGLPHNEIA LQIARQAKVP GSDEPFAVVF
     AAMGITNEEA QYFMDDFEKT GALERAVVFL NLADDPAVER IVTPRMALTA AEYLAYEHDM
     HVLVILTDIT NYCEALRQMG AAREEVPGRR GYPGYMYTDL ASLYERAGVI KGIKGSVTQF
     SILTMPGDDI THPIPDLSGY ITEGQIVVSR ELHRKGIYPP INVLPSLSRL MNSGIGEGKT
     RDDHKAVSDQ MYAAYAEGRD LRGLVAIVGK EALSERDRKM LEFADLFEDR FVRQSRDEDR
     TIDDTLRIAW EILAELPEAQ LTRIDNKYLD KYHPAHQKSE