ID   VATE_CLOP1              Reviewed;         198 AA.
AC   Q0TPW4;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-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=CPF_1893;
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. {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; CP000246; ABG82231.1; -; Genomic_DNA.
DR   RefSeq; WP_003449544.1; NC_008261.1.
DR   AlphaFoldDB; Q0TPW4; -.
DR   SMR; Q0TPW4; -.
DR   STRING; 195103.CPF_1893; -.
DR   EnsemblBacteria; ABG82231; ABG82231; CPF_1893.
DR   GeneID; 29571006; -.
DR   KEGG; cpf:CPF_1893; -.
DR   eggNOG; COG1390; Bacteria.
DR   HOGENOM; CLU_105846_0_0_9; -.
DR   OMA; YAGNIDC; -.
DR   OrthoDB; 1477438at2; -.
DR   Proteomes; UP000001823; 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_0000322517"
SQ   SEQUENCE   198 AA;  22424 MW;  B6A14BD025804BC2 CRC64;
     MSNLNNLTSK ILNDAEEKKK YILADAEAQK DKIISKKTNR AEADKEEIIT KANIEAEVKK
     ARIISNAKLS VRNDMLRAKQ DVISKVFNEA IEKLQNLSNG DYKYYVISTL DSLELEGTEV
     IIINEKDKDI FSNEFLEALN KELESKGKKG SITLNMEGKF NGGFILDRNG IQINNTFEAL
     INSLRGELEF EVNKVLFD