ID   VATB_HALWD              Reviewed;         475 AA.
AC   Q18FB8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, 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=HQ_3243A;
OS   Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloquadratum.
OX   NCBI_TaxID=362976;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16790 / HBSQ001;
RX   PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA   Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F.,
RA   Pfeiffer F., Oesterhelt D.;
RT   "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT   limits of water activity.";
RL   BMC Genomics 7:169-169(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; AM180088; CAJ53340.1; -; Genomic_DNA.
DR   RefSeq; WP_011572445.1; NC_008212.1.
DR   AlphaFoldDB; Q18FB8; -.
DR   SMR; Q18FB8; -.
DR   STRING; 362976.HQ_3243A; -.
DR   EnsemblBacteria; CAJ53340; CAJ53340; HQ_3243A.
DR   GeneID; 4193748; -.
DR   KEGG; hwa:HQ_3243A; -.
DR   eggNOG; arCOG00865; Archaea.
DR   HOGENOM; CLU_022916_0_0_2; -.
DR   OMA; MLMMDSV; -.
DR   Proteomes; UP000001975; 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; Reference proteome;
KW   Transport.
FT   CHAIN           1..475
FT                   /note="V-type ATP synthase beta chain"
FT                   /id="PRO_1000059372"
SQ   SEQUENCE   475 AA;  52672 MW;  0E03DCDEA45CFB0E CRC64;
     MKEYQTVTEI SGPLIYAEVD EPIGYDEIVE IETPNGDIKR GQVLESEDGL VAIQVFEGTS
     GIDTNASVRF SGETLKMKVT EDLLGRVLDG SGQPIDGGPE ILADERREIV GAAINPYARE
     YPEEFIQTGV AAVDGMNTLV RGQKLPIFSG SGLPHNELAL QIARQATVPE EENADDNEDD
     GSEFAVIFGA MGITAEEANE FMEDFERTGA LERSVVFMNL ADDPAVERTV TPRMVLTTAE
     YLAFEKDYHV LVILTDMTNY CEALREIGAA REEVPGRRGY PGYMYTDLAT LYERAGRIEG
     REGSVTQIPI LTMPGDDDTH PIPDLTGYIT EGQIYVDRDL NSQGVQPPVN VLPSLSRLMD
     DGIGEGLTRE DHADVSDQMY AAYAEGEDLR DLVNIVGREA LSDRDNKYLD FADRFETEFI
     DQGFEVNRSI NETLEIGWDL LSMLPKDELN RVDEDLIEKY YREENAGETA EIAAE