ID   VATB1_METHJ             Reviewed;         460 AA.
AC   Q2FP51;
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 1 {ECO:0000255|HAMAP-Rule:MF_00310};
DE   AltName: Full=V-ATPase subunit B 1 {ECO:0000255|HAMAP-Rule:MF_00310};
GN   Name=atpB1 {ECO:0000255|HAMAP-Rule:MF_00310}; OrderedLocusNames=Mhun_1184;
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; ABD40932.1; -; Genomic_DNA.
DR   RefSeq; WP_011448209.1; NC_007796.1.
DR   AlphaFoldDB; Q2FP51; -.
DR   SMR; Q2FP51; -.
DR   STRING; 323259.Mhun_1184; -.
DR   EnsemblBacteria; ABD40932; ABD40932; Mhun_1184.
DR   GeneID; 3923386; -.
DR   KEGG; mhu:Mhun_1184; -.
DR   eggNOG; arCOG00865; Archaea.
DR   HOGENOM; CLU_022916_0_0_2; -.
DR   OMA; GFKIKPR; -.
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; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR   InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
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; SSF50615; SSF50615; 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..460
FT                   /note="V-type ATP synthase beta chain 1"
FT                   /id="PRO_0000322503"
SQ   SEQUENCE   460 AA;  51049 MW;  E6B2C1181EDED82A CRC64;
     MKEYRTITQV AGPLVFVEKT EPVGYQELVN LVLADGSEKR GQVLDTSDDI VVVQVFETTT
     GIGKDTGVRF TGETIKMPVG KDMLGRILSG AGKPKDGGPD IVPEKRLEIT GAAINPWARG
     SPRQFIQTGI STIDLTNTLV RGQKLPIFSG SGLPHNEIAL QIARQAKVPG SDEQFAVVFA
     AMGITKEEEN QFMAEFERTG ALEHAVVFLN LADDPAVERI ITPRLALTTA EYLAFELDYH
     VLVILTDMTN YCEALRQIGA AREEVPGRRG YPGYMYTDLA SLYERAGIIK GKKGSVTQLS
     ILTMPGDDIT HPIPDLSGYI TEGQIVVNRD LHRKGIYPPI NVLPSLSRLM NLGIGKGFTR
     EDHKKVSDQL YAGYAEGVDL RGLVAIVGKD ALSERDRGFL EFAEMFENRF VRQGKDEDRT
     IDESLDLGWD LLKDIPEEQL VRIDRELIQK YHPKYRKKAE