ID   VATB_METM5              Reviewed;         462 AA.
AC   A4FXD3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=MmarC5_0548;
OS   Methanococcus maripaludis (strain C5 / ATCC BAA-1333).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=402880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC BAA-1333;
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., Chertkov O., Brettin T., Bruce D., Han C.,
RA   Detter J.C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of chromosome of Methanococcus maripaludis C5.";
RL   Submitted (MAR-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; CP000609; ABO34862.1; -; Genomic_DNA.
DR   RefSeq; WP_011868317.1; NC_009135.1.
DR   AlphaFoldDB; A4FXD3; -.
DR   SMR; A4FXD3; -.
DR   STRING; 402880.MmarC5_0548; -.
DR   PRIDE; A4FXD3; -.
DR   EnsemblBacteria; ABO34862; ABO34862; MmarC5_0548.
DR   GeneID; 4928560; -.
DR   KEGG; mmq:MmarC5_0548; -.
DR   eggNOG; arCOG00865; Archaea.
DR   HOGENOM; CLU_022916_0_0_2; -.
DR   OMA; MLMMDSV; -.
DR   OrthoDB; 8899at2157; -.
DR   Proteomes; UP000000253; 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_1000059378"
SQ   SEQUENCE   462 AA;  50644 MW;  C371A472E9890A40 CRC64;
     MDAMQKTIEY TSVSRIAGPL MVIDGIEGIA YGEIVDITTP NGDKRTGQVL EAREEIAVVQ
     VFEGTSELNT SETKVRFTGD TAKIGVSHDM LGRIFNGAGK PLDGGPEIIA EKKLDINGYP
     LNPVSRNPPN AFVQTGVSTI DGTNTLVRGQ KIPIFSGSGL PHNKLATQIA RQAKVRGEGE
     QFAVVFAAMG ITGEESNYFM DEFKKTGALE KAVVFINLAD DPAIERILTP RIALTTAEYL
     AYEKGMHVLV ILTDLTNYCE ALREIAAARN EVPGRRGYPG YMYTDLACLY ERAGRVKGKE
     GTVTQIPILT MPDDDITHPI PDLTGYITEG QIVLSRELNR KGIYPPVDIL PSLSRLAGNG
     QGEGKTRDDH SKVISQAYAA YAEGRGLRDL VAVVGEEALT ERDRSFLKFA DAFENSIVTQ
     GVDEDRSIEE TLDYIWGLLT ILPREELKRV SDELIEKYLP KK