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VATB_CLOD6
ID   VATB_CLOD6              Reviewed;         457 AA.
AC   Q184E3;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=CD630_29550;
OS   Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=272563;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=630;
RX   PubMed=16804543; DOI=10.1038/ng1830;
RA   Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA   Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA   Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA   Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA   Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA   Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA   Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT   "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT   mobile, mosaic genome.";
RL   Nat. Genet. 38:779-786(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; AM180355; CAJ69847.1; -; Genomic_DNA.
DR   RefSeq; WP_003422669.1; NZ_CP010905.2.
DR   RefSeq; YP_001089471.1; NC_009089.1.
DR   AlphaFoldDB; Q184E3; -.
DR   SMR; Q184E3; -.
DR   STRING; 272563.CD630_29550; -.
DR   PRIDE; Q184E3; -.
DR   EnsemblBacteria; CAJ69847; CAJ69847; CD630_29550.
DR   GeneID; 66355361; -.
DR   KEGG; cdf:CD630_29550; -.
DR   KEGG; pdc:CDIF630_03238; -.
DR   PATRIC; fig|272563.120.peg.3121; -.
DR   eggNOG; COG1156; Bacteria.
DR   OMA; GFKIKPR; -.
DR   PhylomeDB; Q184E3; -.
DR   BioCyc; PDIF272563:G12WB-3119-MON; -.
DR   Proteomes; UP000001978; 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..457
FT                   /note="V-type ATP synthase beta chain"
FT                   /id="PRO_0000322489"
SQ   SEQUENCE   457 AA;  50560 MW;  7AFE966190ECCEEC CRC64;
     MIKEYKSIQE VAGPLMLING VEGVKFDELG EIELSNGEIR RCKVLEVNGD TALVQLFESS
     TGINLAESKV RFLGKSLDFG VSPDILGRVF SGMGRPIDGG PEIIPDKRLD INGAPINPAA
     RDYPAEFIQT GVSAIDGLNT LVRGQKLPIF SGSGLPHANL AVQIARQAKV RGTDSKFAVV
     FAAVGITFED AEFFISDFKA TGAIDRSVVF VNLANDPAVE RVSTPRMALT AAEYLAFEQD
     MHVLVIITDI TNYAEALREV SAAKKEVPGR RGYPGYLYTD LATMYERAGK MKGHEGSITM
     IPILTMPEDD KTHPIPDLTG YITEGQIILS RELYKKDIQP PIDVLPSLSR LKDKGIGKGK
     TREDHADTMN QLFAAYSRGK DAKELMAILG ESALSEIDLM YAKFADEFEK EYVSQGFRTD
     RTIEQTLEIG WKLLSMLPKS ELKRIRDEYF EKYMPKE
 
 
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