ID   VATB_METPE              Reviewed;         464 AA.
AC   B8GFQ7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=Mpal_2676;
OS   Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanoregulaceae; Methanosphaerula.
OX   NCBI_TaxID=521011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1556 / DSM 19958 / E1-9c;
RX   PubMed=26543115; DOI=10.1128/genomea.01280-15;
RA   Cadillo-Quiroz H., Browne P., Kyrpides N., Woyke T., Goodwin L., Detter C.,
RA   Yavitt J.B., Zinder S.H.;
RT   "Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a
RT   Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.";
RL   Genome Announc. 3:0-0(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; CP001338; ACL17940.1; -; Genomic_DNA.
DR   RefSeq; WP_012619259.1; NC_011832.1.
DR   AlphaFoldDB; B8GFQ7; -.
DR   SMR; B8GFQ7; -.
DR   STRING; 521011.Mpal_2676; -.
DR   EnsemblBacteria; ACL17940; ACL17940; Mpal_2676.
DR   GeneID; 7272498; -.
DR   KEGG; mpl:Mpal_2676; -.
DR   eggNOG; arCOG00865; Archaea.
DR   HOGENOM; CLU_022916_0_0_2; -.
DR   OMA; GFKIKPR; -.
DR   OrthoDB; 8899at2157; -.
DR   Proteomes; UP000002457; 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..464
FT                   /note="V-type ATP synthase beta chain"
FT                   /id="PRO_1000132890"
SQ   SEQUENCE   464 AA;  51120 MW;  E2FF30E1237C5A71 CRC64;
     MKEYRTINKI AGPLVFIEKT EPIGYEELVN IVLYDGTIKR GQVLDTSDDL VVVQVFETTT
     GIGKDSGVRF TGETIKMPVG RDMLGRILSG SGKPIDGGPE IVPEKRLDIT GAAINPYARA
     SPSDFIETGI STIDGTNTLV RGQKLPIFSG AGLPHNNVAL QIARQAKVPG STEEFAVVFA
     AMGITQEEAN YFMQDFERTG ALERAVVFLN LADDPAVERI ITPRLALTTA EYLAFELGMH
     VLVILTDMTN YCEALRQIGA AREEVPGRRG YPGYMYTDLA SLYERAGIIK GQKGSVTQIP
     ILTMPGDDIT HPIADLTGYI TEGQIVISRE LHRKGIYPPI NVLPSLSRLM NLGIGKGHTR
     EDHKKVSDQM YAAYAEGNDL RGLVAIVGKD ALSERDRTFL EFADLFENRF VRQGFDEDRT
     IADTLDLGWE LLSSLPVEQL TRIDRDLIAK YHPQFKNAGA AQKR