ID   CEA8_ECOLX              Reviewed;         205 AA.
AC   P09882;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Colicin-E8;
DE            EC=3.1.-.-;
DE   Flags: Fragment;
GN   Name=col;
OS   Escherichia coli.
OG   Plasmid ColE8.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3323826; DOI=10.1007/bf00331154;
RA   Uchimura T., Lau P.C.K.;
RT   "Nucleotide sequences from the colicin E8 operon: homology with plasmid
RT   ColE2-P9.";
RL   Mol. Gen. Genet. 209:489-493(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3290201; DOI=10.1128/jb.170.7.3237-3242.1988;
RA   Toba M., Masaki H., Ohta T.;
RT   "Colicin E8, a DNase which indicates an evolutionary relationship between
RT   colicins E2 and E3.";
RL   J. Bacteriol. 170:3237-3242(1988).
CC   -!- FUNCTION: This plasmid-coded bactericidal protein is an endonuclease
CC       active on both single- and double-stranded DNA but with undefined
CC       specificity.
CC   -!- FUNCTION: Colicins are polypeptide toxins produced by and active
CC       against E.coli and closely related bacteria.
CC   -!- SIMILARITY: Belongs to the colicin/pyosin nuclease family.
CC       {ECO:0000305}.
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DR   EMBL; M21404; AAA23073.1; -; Genomic_DNA.
DR   EMBL; X06119; CAA29491.1; -; Genomic_DNA.
DR   PIR; A28184; NDECE8.
DR   AlphaFoldDB; P09882; -.
DR   SMR; P09882; -.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   CDD; cd00085; HNHc; 1.
DR   Gene3D; 3.90.540.10; -; 1.
DR   InterPro; IPR037146; Colicin/pyocin_DNase_dom_sf.
DR   InterPro; IPR044925; His-Me_finger_sf.
DR   InterPro; IPR003615; HNH_nuc.
DR   SMART; SM00507; HNHc; 1.
DR   SUPFAM; SSF54060; SSF54060; 1.
PE   3: Inferred from homology;
KW   Antibiotic; Antimicrobial; Bacteriocin; Endonuclease; Hydrolase;
KW   Metal-binding; Nuclease; Plasmid; Zinc.
FT   CHAIN           <1..205
FT                   /note="Colicin-E8"
FT                   /id="PRO_0000218683"
FT   REGION          24..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          136..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..80
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..109
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..181
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         173
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         198
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         202
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   205 AA;  23198 MW;  B3E292480A669155 CRC64;
     RFAHDPMAGG HRMWQMAGLK AQRAQTDVNN KQAAFDAAAK EKSDADAALS AAQERRKQKE
     NKEKDAKDKL DKESKRNKPG KATGKGKPVG DKWLDDAGKD SGAPIPDRIA DKLRDKEFKN
     FDDFRRKFWE EVSKDPELSK QFNPGNKKRL SQGLAPRARN KDTVGGRRSF ELHHDKPISQ
     DGGVYDMDNL RITTPKRHID IHRGQ