ID   VATB_METBF              Reviewed;         460 AA.
AC   Q46FH4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 119.
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=Mbar_A0385;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
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; CP000099; AAZ69368.1; -; Genomic_DNA.
DR   RefSeq; WP_011305421.1; NC_007355.1.
DR   AlphaFoldDB; Q46FH4; -.
DR   SMR; Q46FH4; -.
DR   STRING; 269797.Mbar_A0385; -.
DR   EnsemblBacteria; AAZ69368; AAZ69368; Mbar_A0385.
DR   GeneID; 3627211; -.
DR   KEGG; mba:Mbar_A0385; -.
DR   eggNOG; arCOG00865; Archaea.
DR   HOGENOM; CLU_022916_0_0_2; -.
DR   OMA; GFKIKPR; -.
DR   OrthoDB; 8899at2157; -.
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; Transport.
FT   CHAIN           1..460
FT                   /note="V-type ATP synthase beta chain"
FT                   /id="PRO_1000059375"
SQ   SEQUENCE   460 AA;  50340 MW;  AB13A540EA9F85FD CRC64;
     MVKEYKTITQ IAGPLVFVEK TEPVGYKEIV TINMPDGTTR RGEVLDSSSD IVVIQIFEGT
     TGLDKECGVV FTGETLKLPA SIDLLGRILS GSGEPLDGGP RIVPDQLLDI NGAAMNPYAR
     LPPKDFIQTG ISTIDGTNTL VRGQKLPIFS ASGLPHNEIA LQIARQAAVP GSESAFAVVF
     AAMGITNEEA QYFMSDFEKT GALERAVVFL NLADDPAVER IVTPRMALTA AEYLAYEHGM
     HVLVILTDIT NYAEALRQMG AARNEIPGRR GYPGYMYTDL ATLYERAGIV KGAKGSVTQI
     PILSMPGDDI THPIPDLSGY ITEGQIVVSR ELHRKGIYPP INVLPSLSRL MNSGIGADKT
     REDHKAVSDQ MYAGYAEGRD LRGLVAIVGK EALSERDVKF LEFADLFEDQ FVRQGRNENR
     TIADTLDIGW KILAHLPENQ LGRIDNKYIQ KYHPAHRKGQ