ID   VATB_ENTFA              Reviewed;         458 AA.
AC   Q834X8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 114.
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=EF_1499;
OS   Enterococcus faecalis (strain ATCC 700802 / V583).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=226185;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700802 / V583;
RX   PubMed=12663927; DOI=10.1126/science.1080613;
RA   Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA   Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA   Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA   DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA   Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA   Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT   "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT   faecalis.";
RL   Science 299:2071-2074(2003).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. The V-type 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; AE016830; AAO81290.1; -; Genomic_DNA.
DR   RefSeq; NP_815220.1; NC_004668.1.
DR   RefSeq; WP_002357674.1; NZ_KE136528.1.
DR   AlphaFoldDB; Q834X8; -.
DR   SMR; Q834X8; -.
DR   STRING; 226185.EF_1499; -.
DR   EnsemblBacteria; AAO81290; AAO81290; EF_1499.
DR   GeneID; 60893806; -.
DR   KEGG; efa:EF1499; -.
DR   PATRIC; fig|226185.45.peg.2001; -.
DR   eggNOG; COG1156; Bacteria.
DR   HOGENOM; CLU_022916_0_0_9; -.
DR   OMA; GFKIKPR; -.
DR   Proteomes; UP000001415; 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; IPR020003; ATPase_a/bsu_AS.
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   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..458
FT                   /note="V-type ATP synthase beta chain"
FT                   /id="PRO_1000059370"
SQ   SEQUENCE   458 AA;  51228 MW;  5386B48915D08597 CRC64;
     MIKEYRTINE VVGPLMIVEK VAGVKYEELI EVRMQNGEIR QGQVLEINGD KAMVQIFEGT
     SNINIRDSKV RFLGHPLELG VSPDMMGRVF DGLGRLKDNG PELLPEKKLD INGEVINPVA
     RDYPDEFIQT GISAIDHLNT LVRGQKLPVF SASGLPHKEL AAQIARQANV LNSEEEFAVV
     FAAIGITFEE AEYFMEDFRQ TGAIDRSVLF MNLANDPAIE RIATPRMALT AAEYLAYEKG
     MHVLVIMTDM TNYCEALREI SAARREVPGR RGYPGYLYTN LATLYERAGR IRGSKGSVTQ
     IPILTMPEED KTHPIPDLTG YITEGQIILS RELYKSGIQP PIDVLPSLSR LKDKGTGEGK
     TRGDHAATMN QLFSAYAQGK QAKELAVILG ESALSDVDKI YAAFAQRFEE EYVNQGFDTN
     RSIEETLDLG WELLSMLPRT ELKRIKEDML DQYLTEGK