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VATB_METMJ
ID   VATB_METMJ              Reviewed;         461 AA.
AC   A3CS72;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=Memar_0288;
OS   Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX   NCBI_TaxID=368407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35101 / DSM 1498 / JR1;
RX   PubMed=21304656; DOI=10.4056/sigs.32535;
RA   Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A.,
RA   Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C.,
RA   Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S., Hauser L.,
RA   Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT   "Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981
RT   type strain JR1.";
RL   Stand. Genomic Sci. 1:189-196(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; CP000562; ABN56222.1; -; Genomic_DNA.
DR   RefSeq; WP_011843143.1; NC_009051.1.
DR   AlphaFoldDB; A3CS72; -.
DR   SMR; A3CS72; -.
DR   STRING; 368407.Memar_0288; -.
DR   EnsemblBacteria; ABN56222; ABN56222; Memar_0288.
DR   GeneID; 4847165; -.
DR   KEGG; mem:Memar_0288; -.
DR   eggNOG; arCOG00865; Archaea.
DR   HOGENOM; CLU_022916_0_0_2; -.
DR   OMA; GFKIKPR; -.
DR   OrthoDB; 8899at2157; -.
DR   Proteomes; UP000002146; Chromosome.
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..461
FT                   /note="V-type ATP synthase beta chain"
FT                   /id="PRO_1000059380"
SQ   SEQUENCE   461 AA;  50865 MW;  EAF43F2E66835766 CRC64;
     MKEYRTVAQI AGPLVFVEKT EPVGYSELVN IVTADGTVKR GQVLDTSDEI VVVQVFETTA
     GIGRDSGIRF TGETIKMPVG KDMLGRILSG GGKPIDGGPD IVPEKRLEIT GAAINPYARS
     SPEDFIQTGI STIDGTNTLV RGQKLPIFSA SGLPHNDVAL QIARQAKVPG STEEFAVVFA
     AMGITREEAN YFMADFEKTG ALERSVVFLN LADDPAVERT ITPRLALTTA EYLAFDLGYH
     VLVILTDMTN YCEALRQIGA AREEVPGRRG YPGYMYTDLA SIYERAGIIK GVKGSVTQIP
     ILTMPGDDIT HPIPDLTGYI TEGQIVVNRE LHRKGIYPPI NVLPSLSRLM NLGIGEGHTR
     EDHKKVSDQL YAAYAEGNDL RGLVAIVGKD ALSERDRMFL EFADLFEDRF VRQGLYEDRS
     IEETLDLGWE LLSTLPEEQL VRIDRELIQK YHPKYRKKAQ G
 
 
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