ID   VATB_METLZ              Reviewed;         458 AA.
AC   A2SST6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=Mlab_1223;
OS   Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanocorpusculaceae; Methanocorpusculum.
OX   NCBI_TaxID=410358;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43576 / DSM 4855 / Z;
RX   PubMed=21304657; DOI=10.4056/sigs.35575;
RA   Anderson I.J., Sieprawska-Lupa M., Goltsman E., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Tice H., Dalin E., Barry K., Pitluck S., Hauser L.,
RA   Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT   "Complete genome sequence of Methanocorpusculum labreanum type strain Z.";
RL   Stand. Genomic Sci. 1:197-203(2009).
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; CP000559; ABN07392.1; -; Genomic_DNA.
DR   RefSeq; WP_011833595.1; NC_008942.1.
DR   AlphaFoldDB; A2SST6; -.
DR   SMR; A2SST6; -.
DR   STRING; 410358.Mlab_1223; -.
DR   EnsemblBacteria; ABN07392; ABN07392; Mlab_1223.
DR   GeneID; 4795870; -.
DR   KEGG; mla:Mlab_1223; -.
DR   eggNOG; arCOG00865; Archaea.
DR   HOGENOM; CLU_022916_0_0_2; -.
DR   OMA; GFKIKPR; -.
DR   OrthoDB; 8899at2157; -.
DR   Proteomes; UP000000365; 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; Reference proteome;
KW   Transport.
FT   CHAIN           1..458
FT                   /note="V-type ATP synthase beta chain"
FT                   /id="PRO_1000059377"
SQ   SEQUENCE   458 AA;  50441 MW;  C52CA4129109A3A3 CRC64;
     MKEYKTVSKV AGPLLFVEKT EPVSYEEQVS LVLADGTMKR GQVLDTSEDL VVVQCFETTT
     GLGRDTGVRF LGETFKMPVS KTMLGRILSG GGKPIDGGPA IVPDKRLDIN GAAINPYARG
     TPRDFIQTGI STIDGTNTLV RGQKLPIFSS AGLPHNEIAL QIARQAKVPG SSDEFAVVFA
     AMGITREEAN YFMADFERTG ALERAVVFLN LADDPAVERT VTPRLALTTA EYLAYELGYH
     VLVILTDMTN YCEALRQIGA AREEVPGRRG YPGYMYTDLA SIYERAGIIK GLKGSVTQIP
     ILTMPGDDIT HPIPDLTGYI TEGQIVISPE LHRKGIYPPI NVLPSLSRLM NLGIGKGMTR
     EDHKKVSDMM YSGYAEGVDL RGLVAIVGKD ALSERDQKFL EFADAFEDKF VRQGSDEDRT
     IAQTLDVGWG MFTQLPESEL EKRIDRDLIK TYHPNYRK