ID   VATB_THEGJ              Reviewed;         463 AA.
AC   C5A337;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=TGAM_0147;
OS   Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=593117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15229 / JCM 11827 / EJ3;
RX   PubMed=19558674; DOI=10.1186/gb-2009-10-6-r70;
RA   Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., Dutertre M.,
RA   Anthouard V., Forterre P., Wincker P., Confalonieri F.;
RT   "Genome analysis and genome-wide proteomics of Thermococcus gammatolerans,
RT   the most radioresistant organism known amongst the Archaea.";
RL   Genome Biol. 10:R70.1-R70.23(2007).
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; CP001398; ACS32649.1; -; Genomic_DNA.
DR   RefSeq; WP_015857769.1; NC_012804.1.
DR   AlphaFoldDB; C5A337; -.
DR   SMR; C5A337; -.
DR   STRING; 593117.TGAM_0147; -.
DR   PaxDb; C5A337; -.
DR   PRIDE; C5A337; -.
DR   EnsemblBacteria; ACS32649; ACS32649; TGAM_0147.
DR   GeneID; 7988727; -.
DR   KEGG; tga:TGAM_0147; -.
DR   PATRIC; fig|593117.10.peg.150; -.
DR   eggNOG; arCOG00865; Archaea.
DR   HOGENOM; CLU_022916_0_0_2; -.
DR   OMA; MLMMDSV; -.
DR   OrthoDB; 8899at2157; -.
DR   Proteomes; UP000001488; 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; Transport.
FT   CHAIN           1..463
FT                   /note="V-type ATP synthase beta chain"
FT                   /id="PRO_1000205048"
SQ   SEQUENCE   463 AA;  52109 MW;  3875D73A1027A48A CRC64;
     MPGMEYSTVS KIYGPLMIVE GVKGVAYGEV VEIETESGEK RKGQVLEARE NLAIVQVFEG
     TRDLDIKTTR VRFTGETLKV PVSMDMLGRI FNGIGKPIDG GPEIIPEDRR DVHGAPLNPV
     ARAYPRDFIQ TGISAIDGMN TLVRGQKLPI FSGSGLPHNM LAAQIARQAK VLGEEEQFAV
     VFAAMGITYE EANFFKKSFE ETGAIERAVL FLNLADDPAI ERIITPRMAL TVAEYLAFDY
     DMQVLVILTD MTNYAEALRE ISAAREEVPG RRGYPGYMYT DLATIYERAG RVRGKKGSIT
     QMPILTMPDD DITHPIPDLT GYITEGQIVL SRELHRKGIY PPIDVLPSLS RLMKDGIGKG
     RTREDHPQLS QQLYAAYAEG RSLRDLVAVV GEEALSETDR KYLKFADRFE REFVAQRYDE
     DRSIFETLDL GWELLAELPE SELKRVRKEY ILKYHPKYRK RGS