ID   VATE_CLOPS              Reviewed;         198 AA.
AC   Q0SSH9;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=CPR_1612;
OS   Clostridium perfringens (strain SM101 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=289380;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM101 / 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. {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; CP000312; ABG87064.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0SSH9; -.
DR   SMR; Q0SSH9; -.
DR   EnsemblBacteria; ABG87064; ABG87064; CPR_1612.
DR   KEGG; cpr:CPR_1612; -.
DR   OMA; YAGNIDC; -.
DR   Proteomes; UP000001824; 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; Transport.
FT   CHAIN           1..198
FT                   /note="V-type ATP synthase subunit E"
FT                   /id="PRO_0000322518"
SQ   SEQUENCE   198 AA;  22438 MW;  8D0B27A1E35BB02D CRC64;
     MSNLNNLTSK ILNDAEEKKK YILAEAEAQK DKIISKKTNR AEADKEEIIT KANIEAEVKK
     ARIISNAKLS VRNDMLRAKQ DVISKVFNEA IEKLQNLSNG DYKYYVISTL DSLELEGTEV
     IIINEKDKDI FSNEFLEALN KELESKGKKG SITLNMEGKF NGGFILDRNG IQINNTFEAL
     INSLRGELEF EVNKVLFD