ID   VATB_ACET2              Reviewed;         460 AA.
AC   A3DHP1;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=Cthe_2268;
OS   Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC
OS   103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Acetivibrio.
OX   NCBI_TaxID=203119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL
RC   B-4536 / VPI 7372;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D.,
RA   Newcomb M., Richardson P.;
RT   "Complete sequence of Clostridium thermocellum ATCC 27405.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000568; ABN53470.1; -; Genomic_DNA.
DR   RefSeq; WP_003513513.1; NC_009012.1.
DR   AlphaFoldDB; A3DHP1; -.
DR   SMR; A3DHP1; -.
DR   STRING; 203119.Cthe_2268; -.
DR   PRIDE; A3DHP1; -.
DR   EnsemblBacteria; ABN53470; ABN53470; Cthe_2268.
DR   KEGG; cth:Cthe_2268; -.
DR   eggNOG; COG1156; Bacteria.
DR   HOGENOM; CLU_022916_0_0_9; -.
DR   OMA; GFKIKPR; -.
DR   OrthoDB; 875807at2; -.
DR   Proteomes; UP000002145; 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..460
FT                   /note="V-type ATP synthase beta chain"
FT                   /id="PRO_0000322496"
SQ   SEQUENCE   460 AA;  50723 MW;  47FE2CA5DF6F518A CRC64;
     MLKEYRTITE VAGPLMLVQK VEGVKYGELG EIELANGEIR RCKVLEVDGQ NALVQLFESS
     TGINVATSKV RFLGRSIELP VSMDMLGRVF SGMGKPLDGG PNIIPDKRLD INGLPMNPAA
     RNYPSEFIQT GISAIDGLNT LVRGQKLPIF SGSGLPHAQL AAQIARQAKV LGTDSKFAVV
     FAAVGITFEE ADYFISDFKR TGAIDRTVLF INLANDPAIE RISTPRMALT AAEYLAFDKG
     MHVLVIITDI TNYAEALREV SAARKEVPGR RGYPGYLYTD LATIYERAGR RIDSEGSITL
     IPILTMPEDD KTHPIPDLTG YITEGQIILS RELHRKGVTP PIDVLPSLSR LKDKGIGKGK
     TREDHADTMN QLFAAYARGK EAKELAVILG DAALSDTDKL YAKFADAFEK EYVSQGFNED
     RSIEKTLEIG WKLLSILPRS ELKRIRDEYL DKYLPKAAEN