ID   VATB_NATPD              Reviewed;         471 AA.
AC   Q3ITC7;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=NP_1032A;
OS   Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS   8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Natronomonas.
OX   NCBI_TaxID=348780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC   2260 / Gabara;
RX   PubMed=16169924; DOI=10.1101/gr.3952905;
RA   Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA   Oesterhelt D.;
RT   "Living with two extremes: conclusions from the genome sequence of
RT   Natronomonas pharaonis.";
RL   Genome Res. 15:1336-1343(2005).
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; CR936257; CAI48607.1; -; Genomic_DNA.
DR   RefSeq; WP_011322242.1; NC_007426.1.
DR   AlphaFoldDB; Q3ITC7; -.
DR   SMR; Q3ITC7; -.
DR   STRING; 348780.NP_1032A; -.
DR   EnsemblBacteria; CAI48607; CAI48607; NP_1032A.
DR   GeneID; 3702539; -.
DR   KEGG; nph:NP_1032A; -.
DR   eggNOG; arCOG00865; Archaea.
DR   HOGENOM; CLU_022916_0_0_2; -.
DR   OMA; MLMMDSV; -.
DR   OrthoDB; 8899at2157; -.
DR   Proteomes; UP000002698; 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..471
FT                   /note="V-type ATP synthase beta chain"
FT                   /id="PRO_0000322506"
SQ   SEQUENCE   471 AA;  52364 MW;  25F5ABA4EBCCB0B9 CRC64;
     MQKEYKTITE ISGPLVFAEV DEPVGYDEMV EIETPSGETR RGQVLESTSE FVAIQVFEGT
     SGIDRNSSVR FLGETLQMPL TEELLGRVLS GSGEPIDGGP EIEPDEEREI VGAAINPTAR
     EYPEEFIQTG VSAIDGMNTL IRGQKLPIFS GSGLPHNELA LQIARQASVP EEESGDDEAG
     SEFAVIFGAM GITQEEANEF MDDFERTGAL ERSVVFMNLA DDPAVERTVT PRMALTTAEY
     LAFEEGYHVL VILTDMTNYC EALREIGAAR EEVPGRRGYP GYMYTDLAQL YERAGRIEGR
     EGSVTQIPIL TMPGDDDTHP IPDLTGYITE GQIYIDRNLN SQGIEPPINV LPSLSRLMDD
     GIGEGFTRED HPDVSDQAYA AYAEGEDLRD LVNIVGREAL SERDNKYLDF ADRFEEEFVQ
     QGYDTNRDVE ETLDLAWELL SDLPKEELNR IDEEAIEEYY VEDEQAAQTA D