ID   VATB3_METHJ             Reviewed;         469 AA.
AC   Q2FQF0;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=V-type ATP synthase beta chain 3 {ECO:0000255|HAMAP-Rule:MF_00310};
DE   AltName: Full=V-ATPase subunit B 3 {ECO:0000255|HAMAP-Rule:MF_00310};
GN   Name=atpB3 {ECO:0000255|HAMAP-Rule:MF_00310}; OrderedLocusNames=Mhun_1769;
OS   Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 /
OS   JF-1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX   NCBI_TaxID=323259;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1;
RX   PubMed=26744606; DOI=10.1186/s40793-015-0124-8;
RA   Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H.,
RA   Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M.,
RA   Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.;
RT   "Complete genome sequence of Methanospirillum hungatei type strain JF1.";
RL   Stand. Genomic Sci. 11:2-2(2016).
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; CP000254; ABD41490.1; -; Genomic_DNA.
DR   RefSeq; WP_011448754.1; NC_007796.1.
DR   AlphaFoldDB; Q2FQF0; -.
DR   SMR; Q2FQF0; -.
DR   STRING; 323259.Mhun_1769; -.
DR   EnsemblBacteria; ABD41490; ABD41490; Mhun_1769.
DR   GeneID; 3924743; -.
DR   KEGG; mhu:Mhun_1769; -.
DR   eggNOG; arCOG00865; Archaea.
DR   HOGENOM; CLU_022916_0_0_2; -.
DR   OMA; MLMMDSV; -.
DR   OrthoDB; 8899at2157; -.
DR   Proteomes; UP000001941; 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; 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.
PE   3: Inferred from homology;
KW   ATP synthesis; Hydrogen ion transport; Ion transport; Reference proteome;
KW   Transport.
FT   CHAIN           1..469
FT                   /note="V-type ATP synthase beta chain 3"
FT                   /id="PRO_0000322505"
SQ   SEQUENCE   469 AA;  52018 MW;  443A7A1A51589A01 CRC64;
     MTDLRFRTYT GVSKVVGPLM VLDGVEGIGY GEIAEITLPG GEVRIGQVLE TTTTRAMVQV
     FRGTRDLDTE KTQVRFRGEP MKISLSSDML GRTFDGSARP IDGGGPVIPE CIRDIYGSPI
     NPSAREHPRD SIQTGISSID GMNTLVRGQK LPIFSGAGLP HNLLASQIAR QAKVTGQAEK
     FAVVFAAMGI TYEESAFFIR EFEESGALER TVLFLNLADD PAIERIITPR LALTTAEYLA
     FDKGMHVLVV LTDLTNYCEA LREIAAAREE VPGRRGYPGY IYTDLASLYE RAGRIRGREG
     SITQIPILTM PDDDITHPVP DLTGYITEGQ IVLSRDLHRK GIYPPVDVLP CLSRLMQGGI
     GPGRTRADHA EVKNQLYSAY ARGIRLKSLV AVMGEEGLTP LDKLYIRFCD RFENDFIRQA
     SYEDRSFDDT LTLAWDLLSI LPKAELKRIS TEFIKMYYHG EEILECKGP