ID   VATB_HALLT              Reviewed;         474 AA.
AC   B9LS42;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=Hlac_0282;
OS   Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM
OS   34).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Halorubraceae; Halorubrum.
OX   NCBI_TaxID=416348;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34;
RX   PubMed=27617060; DOI=10.1186/s40793-016-0194-2;
RA   Anderson I.J., DasSarma P., Lucas S., Copeland A., Lapidus A.,
RA   Del Rio T.G., Tice H., Dalin E., Bruce D.C., Goodwin L., Pitluck S.,
RA   Sims D., Brettin T.S., Detter J.C., Han C.S., Larimer F., Hauser L.,
RA   Land M., Ivanova N., Richardson P., Cavicchioli R., DasSarma S.,
RA   Woese C.R., Kyrpides N.C.;
RT   "Complete genome sequence of the Antarctic Halorubrum lacusprofundi type
RT   strain ACAM 34.";
RL   Stand. Genomic Sci. 11:70-70(2016).
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; CP001365; ACM55887.1; -; Genomic_DNA.
DR   RefSeq; WP_012659528.1; NC_012029.1.
DR   AlphaFoldDB; B9LS42; -.
DR   SMR; B9LS42; -.
DR   STRING; 416348.Hlac_0282; -.
DR   EnsemblBacteria; ACM55887; ACM55887; Hlac_0282.
DR   GeneID; 7401208; -.
DR   KEGG; hla:Hlac_0282; -.
DR   eggNOG; arCOG00865; Archaea.
DR   HOGENOM; CLU_022916_0_0_2; -.
DR   OMA; MLMMDSV; -.
DR   Proteomes; UP000000740; Chromosome 1.
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; Transport.
FT   CHAIN           1..474
FT                   /note="V-type ATP synthase beta chain"
FT                   /id="PRO_1000132888"
SQ   SEQUENCE   474 AA;  52656 MW;  A4D726C6A1DF3E29 CRC64;
     MKEYQTITEI SGPLVYAEVD EAIGYDEIVE IETAQGETLR GQVLESSEGV VAIQVFEGTS
     GIDQNASVRF LGETMKMPVT EDLLGRVLDG SGRPIDDGPE IVPEERQDIV GAAINPYSRE
     YPEEFIETGV SAIDGMNTLV RGQKLPIFSS SGQPHSQLAM QIARQASVPE EEEGGDDEEG
     SEFAVIFGAM GITAEEANEF MQDFERTGAL ERSVVFMNLA DDPAVERTVT PRMVLTTAEY
     LAFEKDYHVL VILTDMTNYC EALREIGAAR EEVPGRRGYP GYMYTDLAQL YERAGRIQGR
     DGSVTQIPIL TMPGDDDTHP IPDLTGYITE GQIYVDPDLN SQGLQPPINV LPSLSRLMDD
     GIGEGLTRED HADVKDQMFA AYAEGEDLRD LVNIVGREAL SELDNKYLDF ADDFESEFVD
     QGFDQNRSIE ETLEIGWDLL SMLPKDALNR IDEEFIEKYY REDDSDRQVV EAAD