ID   VATB_METVS              Reviewed;         462 AA.
AC   A6UP55;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=Mevan_0368;
OS   Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148
OS   / SB).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=406327;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB;
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA   Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus vannielii SB.";
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; CP000742; ABR54277.1; -; Genomic_DNA.
DR   RefSeq; WP_011972180.1; NC_009634.1.
DR   AlphaFoldDB; A6UP55; -.
DR   SMR; A6UP55; -.
DR   STRING; 406327.Mevan_0368; -.
DR   EnsemblBacteria; ABR54277; ABR54277; Mevan_0368.
DR   GeneID; 5325780; -.
DR   KEGG; mvn:Mevan_0368; -.
DR   eggNOG; arCOG00865; Archaea.
DR   HOGENOM; CLU_022916_0_0_2; -.
DR   OMA; MLMMDSV; -.
DR   OrthoDB; 8899at2157; -.
DR   Proteomes; UP000001107; 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; 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_1000059384"
SQ   SEQUENCE   462 AA;  50586 MW;  246EC8E573BC7A3F CRC64;
     MDAMQKTIEY TSVSRIAGPL MVIEGIEGIA YGEIVDITTP NGEKRTGQVL EAREDIAVVQ
     VFEGTSELNT SETRVRFTGE TAKIGVSKDM LGRIFNGAGK PLDGGPEIIA EKKVDINGYP
     LNPVSRNPPN AFVQTGISTI DGTNTLVRGQ KIPIFSGSGL PHNMLAAQIA RQAKVRGEGE
     QFAVVFAAMG ITSEESNYFM DEFKKTGALE KAVVFINLAD DPAIERIITP RIALTTAEYL
     AYEKGMHVLV ILTDLTNYCE ALREIAAARN EVPGRRGYPG YMYTDLASLY ERAGRVKGKE
     GTVTQIPILT MPHDDITHPI PDLTGYITEG QIVLSRELNR KGIYPPVDIL PSLSRLAGNG
     QGPGKTRDDH AKVISQAYAA YAEGRGLRDL VAVVGEEALT ERDRAFLKFA DAFEGRVVTQ
     GVDEDRSIEE TLDIIWELLT ILPKSELKRV SDELIEKYLP KK