ID   VATB_CLOP1              Reviewed;         460 AA.
AC   Q0TPW8;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=CPF_1889;
OS   Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB
OS   6125 / NCTC 8237 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 /
RC   Type A;
RX   PubMed=16825665; DOI=10.1101/gr.5238106;
RA   Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA   Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA   Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA   Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA   Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA   Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA   Paulsen I.T.;
RT   "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT   Clostridium perfringens.";
RL   Genome Res. 16:1031-1040(2006).
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; CP000246; ABG83271.1; -; Genomic_DNA.
DR   RefSeq; WP_003449785.1; NC_008261.1.
DR   AlphaFoldDB; Q0TPW8; -.
DR   SMR; Q0TPW8; -.
DR   STRING; 195103.CPF_1889; -.
DR   EnsemblBacteria; ABG83271; ABG83271; CPF_1889.
DR   GeneID; 29571010; -.
DR   KEGG; cpf:CPF_1889; -.
DR   eggNOG; COG1156; Bacteria.
DR   HOGENOM; CLU_022916_0_0_9; -.
DR   OMA; GFKIKPR; -.
DR   OrthoDB; 875807at2; -.
DR   Proteomes; UP000001823; 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; Transport.
FT   CHAIN           1..460
FT                   /note="V-type ATP synthase beta chain"
FT                   /id="PRO_0000322492"
SQ   SEQUENCE   460 AA;  51056 MW;  3C303481156CA932 CRC64;
     MLKEYRTVTE VVGPLMAVEG VEGVKYDELV EIEMQTGELR RGKVLEVNGD KAMVQLFEGS
     AGINLKNTKV RFLGRPLEIG VSEDMLGRVF DGMGRPKDNG PNIIPEKRLD INGEAINPVA
     RNYPSEFIQT GISAIDGLNT LVRGQKLPVF SGSGLPHKEL AAQIARQAKV LNSDSKFAVV
     FAAIGITFEE AEFFVDEFTK TGAIDRSVLF MNLASDPAIE RIATPRMALT TAEYLAYEKG
     MHVLVIMTDI TNYCEALREV SAARKEVPGR RGYPGYLYTD LSTLYERAGR LVGKEGSITQ
     IPILTMPEDD KTHPIPDLTG YITEGQIILS RELYKKGIMP PIDVLPSLSR LKDKGIGKGK
     TREDHADTMN QLFSAYAQGK QAKELAAILG ESALSDVDKA YAKFAEAFEN EYVSQGFTTN
     RTIEETLNLG WKLLKILPRT ELKRIRDEYL EKYMPVGEDE