ID   VATB_METM7              Reviewed;         462 AA.
AC   A6VFZ3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-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=MmarC7_0299;
OS   Methanococcus maripaludis (strain C7 / ATCC BAA-1331).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=426368;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C7 / ATCC BAA-1331;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C7.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000745; ABR65369.1; -; Genomic_DNA.
DR   RefSeq; WP_011976705.1; NC_009637.1.
DR   AlphaFoldDB; A6VFZ3; -.
DR   SMR; A6VFZ3; -.
DR   STRING; 426368.MmarC7_0299; -.
DR   EnsemblBacteria; ABR65369; ABR65369; MmarC7_0299.
DR   GeneID; 5328605; -.
DR   KEGG; mmz:MmarC7_0299; -.
DR   eggNOG; arCOG00865; Archaea.
DR   HOGENOM; CLU_022916_0_0_2; -.
DR   OMA; MLMMDSV; -.
DR   OrthoDB; 8899at2157; -.
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; 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   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_1000059379"
SQ   SEQUENCE   462 AA;  50756 MW;  EC86238EA94871CB CRC64;
     MDAMQKTIEY TSVSRIAGPL MVIDGIEGIA YGEIVDITTP NGDKRTGQVL EAREEIAVVQ
     VFEGTSELNT SETKVRFTGD TAKIGVSYDM LGRIFNGAGK PLDGGPEIIA EKKLDINGYP
     LNPVSRNPPN AFVQTGISTI DGTNTLVRGQ KIPIFSGSGL PHNKLATQIA RQAKVRGEGE
     QFAVVFAAMG ITGEESNYFM DEFKKTGALE KAVVFINLAD DPAIERILTP RIALTTAEYL
     AYEKGMHVLV ILTDLTNYCE ALREIAAARN EVPGRRGYPG YMYTDLACLY ERAGRVKGRE
     GTVTQIPILT MPDDDITHPI PDLTGYITEG QIVLSRELNR KGIYPPVDIL PSLSRLAGNG
     QGEGKTRDDH SKVISQAYAA YAEGRGLRDL VAVVGEEALT ERDRSFLKFA DAFENSIVTQ
     GVDEDRSIEE TLDYVWDLLT ILPREELKRV SDELIEKYLP KK