ID   VATB_CLOPE              Reviewed;         460 AA.
AC   Q8XJW6;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 125.
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=CPE1637;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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; BA000016; BAB81343.1; -; Genomic_DNA.
DR   RefSeq; WP_003449785.1; NC_003366.1.
DR   AlphaFoldDB; Q8XJW6; -.
DR   SMR; Q8XJW6; -.
DR   STRING; 195102.gene:10490901; -.
DR   EnsemblBacteria; BAB81343; BAB81343; BAB81343.
DR   GeneID; 29571010; -.
DR   KEGG; cpe:CPE1637; -.
DR   HOGENOM; CLU_022916_0_0_9; -.
DR   OMA; GFKIKPR; -.
DR   Proteomes; UP000000818; 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_0000322491"
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