ID   VATB_METS3              Reviewed;         462 AA.
AC   A5UKB1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=Msm_0434;
OS   Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=420247;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS;
RX   PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA   Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA   Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT   "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT   human gut.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(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; CP000678; ABQ86639.1; -; Genomic_DNA.
DR   RefSeq; WP_004032182.1; NC_009515.1.
DR   AlphaFoldDB; A5UKB1; -.
DR   SMR; A5UKB1; -.
DR   STRING; 420247.Msm_0434; -.
DR   EnsemblBacteria; ABQ86639; ABQ86639; Msm_0434.
DR   GeneID; 5215808; -.
DR   KEGG; msi:Msm_0434; -.
DR   PATRIC; fig|420247.28.peg.434; -.
DR   eggNOG; arCOG00865; Archaea.
DR   HOGENOM; CLU_022916_0_0_2; -.
DR   OMA; MLMMDSV; -.
DR   Proteomes; UP000001992; 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   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; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
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; SSF50615; SSF50615; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; Hydrogen ion transport; Ion transport; Transport.
FT   CHAIN           1..462
FT                   /note="V-type ATP synthase beta chain"
FT                   /id="PRO_1000059382"
SQ   SEQUENCE   462 AA;  51159 MW;  0A7DF8531085FA55 CRC64;
     MNTNIKTREY TTISEVSGPL MVVEGVEGVG YNEIVDIETP NGEKRSGQVL EVTDDVAVIQ
     VFEGTTDLNT KNTKARFTGQ TAKIGVSRDM MGRMFNGIGK PIDGGPEIIP DEELDINGSP
     MNPASREFPE EFIQTGISTI DGMNTLVRGQ KLPIFSGSGL PHNELAAQIA RQAKVLGDDA
     EFAVIFAAMG ITHEEANFFM RDFERTGALE KVTVFMNLAD DPAIERILTP KMALTTAEYF
     AFTLGMQVLV ILTDMTNYCE ALREISAARD EVPGRRGYPG YMYTDLANIY ERAGRIDGKE
     GSITQMPILV MPQDDITHPI PDLTGYITEG QIVLSRELNR KGIYPPVDVL PSLSRLMSGG
     IGGDKTRDDH SGVSDQLYSA YAGGRELRDL VAVVGEEALT ERDQKFLEFA EEFEGKFITQ
     SKDEDRSIIE TLDLGWDLLK ILPKSELKRV KEEFIEQYLP KE