ID   VATE_CLOD6              Reviewed;         187 AA.
AC   Q184F0;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=V-type ATP synthase subunit E;
DE   AltName: Full=V-ATPase subunit E {ECO:0000255|HAMAP-Rule:MF_00311};
GN   Name=atpE {ECO:0000255|HAMAP-Rule:MF_00311}; OrderedLocusNames=CD630_29580;
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. {ECO:0000255|HAMAP-Rule:MF_00311}.
CC   -!- SIMILARITY: Belongs to the V-ATPase E subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_00311}.
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DR   EMBL; AM180355; CAJ69851.1; -; Genomic_DNA.
DR   RefSeq; WP_003422659.1; NZ_CP010905.2.
DR   RefSeq; YP_001089475.1; NC_009089.1.
DR   AlphaFoldDB; Q184F0; -.
DR   SMR; Q184F0; -.
DR   STRING; 272563.CD630_29580; -.
DR   EnsemblBacteria; CAJ69851; CAJ69851; CD630_29580.
DR   GeneID; 66355365; -.
DR   KEGG; cdf:CD630_29580; -.
DR   KEGG; pdc:CDIF630_03242; -.
DR   PATRIC; fig|272563.120.peg.3125; -.
DR   eggNOG; COG1390; Bacteria.
DR   OMA; YAGNIDC; -.
DR   PhylomeDB; Q184F0; -.
DR   BioCyc; PDIF272563:G12WB-3123-MON; -.
DR   Proteomes; UP000001978; Chromosome.
DR   GO; GO:0033178; C:proton-transporting two-sector ATPase complex, catalytic domain; IEA:InterPro.
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:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.2320.30; -; 1.
DR   HAMAP; MF_00311; ATP_synth_E_arch; 1.
DR   InterPro; IPR038495; ATPase_E_C.
DR   InterPro; IPR002842; ATPase_V1_Esu.
DR   Pfam; PF01991; vATP-synt_E; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; Hydrogen ion transport; Ion transport; Reference proteome;
KW   Transport.
FT   CHAIN           1..187
FT                   /note="V-type ATP synthase subunit E"
FT                   /id="PRO_0000322514"
SQ   SEQUENCE   187 AA;  21111 MW;  AE2841923348D8BC CRC64;
     MGNEQKMIDR IIADAKQEAQ EILDKAKSEA DLKVNSANEK AEKEMASYTK LAEAEAEKAA
     SKEISGAYME AKKQILSKKQ EILEEVILEA KNKLLNLKDN EYEEIILNMI EKSNCTDDSE
     IVLSKKDKKT LKDVLSKKGI KVSDETRDIT GGFIVKKGDI EYNYSFEAII AVEHEYIEQI
     AAEILFN