ID   VATB_METB6              Reviewed;         462 AA.
AC   A7IAU7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=Mboo_2344;
OS   Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanoregulaceae; Methanoregula.
OX   NCBI_TaxID=456442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21154 / JCM 14090 / 6A8;
RX   PubMed=25998264; DOI=10.1099/mic.0.000117;
RA   Braeuer S., Cadillo-Quiroz H., Kyrpides N., Woyke T., Goodwin L.,
RA   Detter C., Podell S., Yavitt J.B., Zinder S.H.;
RT   "Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic
RT   peatland environments.";
RL   Microbiology 161:1572-1581(2015).
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; CP000780; ABS56858.1; -; Genomic_DNA.
DR   RefSeq; WP_012107919.1; NC_009712.1.
DR   AlphaFoldDB; A7IAU7; -.
DR   SMR; A7IAU7; -.
DR   STRING; 456442.Mboo_2344; -.
DR   EnsemblBacteria; ABS56858; ABS56858; Mboo_2344.
DR   GeneID; 5411037; -.
DR   KEGG; mbn:Mboo_2344; -.
DR   eggNOG; arCOG00865; Archaea.
DR   HOGENOM; CLU_022916_0_0_2; -.
DR   OMA; GFKIKPR; -.
DR   OrthoDB; 8899at2157; -.
DR   Proteomes; UP000002408; 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..462
FT                   /note="V-type ATP synthase beta chain"
FT                   /id="PRO_1000059374"
SQ   SEQUENCE   462 AA;  50853 MW;  7317469EFE68DE3F CRC64;
     MKEYRTITKI AGPLVFVEKT EPIGYQELVN IVLSDGTIKR GQVLDTSDDL VVVQIFETTT
     GIGRDSGVRF TGETIKMPVG REMLGRILSG GGKPIDGGPE IVPEKRLDIT GAAINPWARN
     SPSDFIQTGI STIDGTNTLV RGQKLPIFSG AGLPHNNVAL QIARQAKVPG STESFAVVFA
     AMGITKEEAN YFMQDFERTG ALEHAVVFLN LADDPAVERI ITPRLALTTA EYLAFELGMH
     VLVILTDMTN YCEALRQIGA AREEVPGRRG YPGYMYTDLA CIYERAGIIK GQKGSVTQIP
     ILTMPGDDIT HPIPDLTGYI TEGQIVVNRE LHRKGIYPPI NVLPSLSRLM NLGIGKGHTR
     EDHKKVSDQM YAGYAEGNDL RGLVAIVGKD ALSERDRGLL EFADLFEDKF VRQGYDEDRT
     IEDTLDLGWD LLSTLPVEQL TRIDRDLINK YHPKLKAGAK KE