ID   VATB_IGNH4              Reviewed;         471 AA.
AC   A8AAA9;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=Igni_0679;
OS   Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Ignicoccus.
OX   NCBI_TaxID=453591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIN4/I / DSM 18386 / JCM 14125;
RX   PubMed=19000309; DOI=10.1186/gb-2008-9-11-r158;
RA   Podar M., Anderson I., Makarova K.S., Elkins J.G., Ivanova N., Wall M.A.,
RA   Lykidis A., Mavromatis K., Sun H., Hudson M.E., Chen W., Deciu C.,
RA   Hutchison D., Eads J.R., Anderson A., Fernandes F., Szeto E., Lapidus A.,
RA   Kyrpides N.C., Saier M.H. Jr., Richardson P.M., Rachel R., Huber H.,
RA   Eisen J.A., Koonin E.V., Keller M., Stetter K.O.;
RT   "A genomic analysis of the archaeal system Ignicoccus hospitalis-
RT   Nanoarchaeum equitans.";
RL   Genome Biol. 9:R158.1-R158.18(2008).
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   -!- INTERACTION:
CC       A8AAA9; A8AC29: atpA; NbExp=2; IntAct=EBI-15831444, EBI-15831423;
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000255|HAMAP-Rule:MF_00310}.
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DR   EMBL; CP000816; ABU81861.1; -; Genomic_DNA.
DR   RefSeq; WP_011998713.1; NC_009776.1.
DR   AlphaFoldDB; A8AAA9; -.
DR   SMR; A8AAA9; -.
DR   DIP; DIP-58545N; -.
DR   IntAct; A8AAA9; 1.
DR   STRING; 453591.Igni_0679; -.
DR   EnsemblBacteria; ABU81861; ABU81861; Igni_0679.
DR   GeneID; 5562680; -.
DR   KEGG; iho:Igni_0679; -.
DR   eggNOG; arCOG00865; Archaea.
DR   HOGENOM; CLU_022916_0_0_2; -.
DR   OMA; MLMMDSV; -.
DR   OrthoDB; 8899at2157; -.
DR   PhylomeDB; A8AAA9; -.
DR   Proteomes; UP000000262; 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   1: Evidence at protein level;
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_0000322501"
SQ   SEQUENCE   471 AA;  52286 MW;  7162835A7FF79ADA CRC64;
     MAVPSVKGKE YESVSEIRGQ LLVVEGVSDA GYGELVDIEM PSGEKRRGIV LETGKGLAVV
     QVFEGTTGIS PAGTKVRFTG RILEMGVSED MLGRIMNALG EPIDGGAPIK AVEKRNVWGE
     PINPYAREYP DEFIETGISA IDGMNSLVRG QKLPIFSGSG LPHNKLAAQI ARQATVRGEE
     ESFAVVFAAV GIQYDELLFF KKAFEETGAI SRTAMFVSLA NEPAMMKIVT PRAALTLAEY
     LAFQKDMHVL VIITDMTNYC EALREISASR EEVPSRQGYP GYMYTDLATI YERAGRVKGS
     KGSITQMPIL TMPNDDITHP IPDLTGYITE GQIVLSRDLH NKGIYPPINV LMSLSRLMRD
     GIGKGKTRED HPDVANQLFA AYSRAVELRG LAAIVGEESL SEVDRKYLRF GEAFEQKFLK
     QDYYERRTIE QTLDLAWEVL SILPEEELTK IRPEYIKKYH PKYRVKAASQ K