ID   VATE_CLOBH              Reviewed;         199 AA.
AC   A5I560; A7G6C6;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 71.
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};
GN   OrderedLocusNames=CBO2627, CLC_2501;
OS   Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441771;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX   PubMed=17519437; DOI=10.1101/gr.6282807;
RA   Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA   Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA   Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA   Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA   Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA   Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA   White B., Whithead S., Parkhill J.;
RT   "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT   Hall A and comparative analysis of the clostridial genomes.";
RL   Genome Res. 17:1082-1092(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT   and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(2007).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAL84187.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AM412317; CAL84187.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP000727; ABS37506.1; -; Genomic_DNA.
DR   RefSeq; WP_011986936.1; NC_009698.1.
DR   RefSeq; YP_001255125.1; NC_009495.1.
DR   RefSeq; YP_001388341.1; NC_009698.1.
DR   AlphaFoldDB; A5I560; -.
DR   SMR; A5I560; -.
DR   GeneID; 5186882; -.
DR   KEGG; cbh:CLC_2501; -.
DR   KEGG; cbo:CBO2627; -.
DR   PATRIC; fig|413999.7.peg.2610; -.
DR   HOGENOM; CLU_105846_0_0_9; -.
DR   PRO; PR:A5I560; -.
DR   Proteomes; UP000001986; 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..199
FT                   /note="V-type ATP synthase subunit E"
FT                   /id="PRO_0000322512"
SQ   SEQUENCE   199 AA;  22767 MW;  0DC9045C98FCACBB CRC64;
     MSNLENLTSK IIEDANKEAE ELLSEAKKEE NKIVDEKVKK GNKAKEQIIE KSKREAKTKA
     ERIISNTHLK IRNNKLEAKQ EMINKVFDEA VIKLQNLSKD EYLDFVKSSI LSLDIEGDEE
     IIISPNDKDK MDVNFMLTLN NKLKAKGKKG LLKISNENRN IKGGFILYKN GIEINNSFEA
     LVDSLRDELE QEIIEALFS