ID   VATB2_METHJ             Reviewed;         466 AA.
AC   Q2FL44;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=V-type ATP synthase beta chain 2 {ECO:0000255|HAMAP-Rule:MF_00310};
DE   AltName: Full=V-ATPase subunit B 2 {ECO:0000255|HAMAP-Rule:MF_00310};
GN   Name=atpB2 {ECO:0000255|HAMAP-Rule:MF_00310}; OrderedLocusNames=Mhun_1758;
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; ABD41479.1; -; Genomic_DNA.
DR   RefSeq; WP_011448743.1; NC_007796.1.
DR   AlphaFoldDB; Q2FL44; -.
DR   SMR; Q2FL44; -.
DR   STRING; 323259.Mhun_1758; -.
DR   EnsemblBacteria; ABD41479; ABD41479; Mhun_1758.
DR   GeneID; 3924708; -.
DR   KEGG; mhu:Mhun_1758; -.
DR   eggNOG; arCOG00865; Archaea.
DR   HOGENOM; CLU_022916_0_0_2; -.
DR   OMA; ICELRTP; -.
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; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR018538; HerA_barrel_dom.
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; PF09378; HAS-barrel; 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..466
FT                   /note="V-type ATP synthase beta chain 2"
FT                   /id="PRO_0000322504"
SQ   SEQUENCE   466 AA;  51684 MW;  4B482D136D2F527F CRC64;
     MQHGSLITVE YQTVNYVSGP LIFVERPKEI SFGETAQIIL PDGEARTGQI LDISEDIAVV
     QVFEGTRGID SHVTTVRFTG QSPLLDVSYD MLGRVLDGVG RPRDGGPEII PEARLDIAGM
     PINPYSRDKP AEFIQTGISA IDALNTLVRG QKLPIFSGAG LPANQLAAQI AKQAKVLGEG
     ENFAVVFAAM GITYKEASFF MKEFEESGAL ERVVFFLNLA DDPTIERIAT PRCALTAAEF
     LAYTHNLHVL VILTDMTNYC DALREISTAR EEIPGRRGYP GYMYTDLATI YERAGRIKGC
     TGSITQIPIL TMPDDDITHP VPDLTGYITE GQIVLSRDLF RKGINPPIDA LPCLSRLMNL
     GIGPGKTRED HRNVADQLYA SYAYGRDLRR LVAIVGEEAL SELDRNYLKF ADHFEKRFIS
     QGNVERSIET TLQVAWELFS LLPDEELKRI KEEYIDKYRT LIISGG