ID   VATB_PYRFU              Reviewed;         462 AA.
AC   Q8U4A5;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=PF0183;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
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   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000255|HAMAP-Rule:MF_00310}.
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DR   EMBL; AE009950; AAL80307.1; -; Genomic_DNA.
DR   RefSeq; WP_011011296.1; NZ_CP023154.1.
DR   AlphaFoldDB; Q8U4A5; -.
DR   SMR; Q8U4A5; -.
DR   STRING; 186497.PF0183; -.
DR   EnsemblBacteria; AAL80307; AAL80307; PF0183.
DR   GeneID; 41711974; -.
DR   KEGG; pfu:PF0183; -.
DR   PATRIC; fig|186497.12.peg.190; -.
DR   eggNOG; arCOG00865; Archaea.
DR   HOGENOM; CLU_022916_0_0_2; -.
DR   OMA; MLMMDSV; -.
DR   OrthoDB; 8899at2157; -.
DR   PhylomeDB; Q8U4A5; -.
DR   Proteomes; UP000001013; 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..462
FT                   /note="V-type ATP synthase beta chain"
FT                   /id="PRO_0000144663"
SQ   SEQUENCE   462 AA;  51915 MW;  5AB9F8AFA2C86283 CRC64;
     MAKEYSTISR IYGPLMIVEG VKGVAYGEVV EIETEWGEKR KGQVLDAREN LAIVQVFEGT
     RDLDIKTTRV RFTGETLKVP VSMDMLGRIF NGIGKPIDGG PEIIPEDRRD VHGAPLNPVA
     RAYPRDFIQT GISAIDGMNT LVRGQKLPIF SGSGLPHNKL AAQIARQAKV LGEEESFAVV
     FAAMGITYEE ANFFKKSFEE TGAIERAVLF LNLADDPAIE RIITPRMALT VAEYLAFDYD
     MHVLVILTDM TNYCEALREI SAAREEVPGR RGYPGYMYTD LATIYERAGR VRGKKGSITQ
     MPILTMPDDD ITHPIPDLTG YITEGQIVLS RDLHRRGIYP PIDVLPSLSR LMKDGIGKGR
     TREDHPQLAQ QLYAAYAEGR SLRDLVAVVG EEALSETDKK YLEFADRFER EFVAQGYDED
     RSIEETLDLG WELLAILPET ELKRVKKEMI MKYHPKYRGR SS