ID   CEA2_ECOLX              Reviewed;         581 AA.
AC   P04419;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 2.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Colicin-E2;
DE            EC=3.1.-.-;
GN   Name=col; Synonyms=ceaB;
OS   Escherichia coli.
OG   Plasmid ColE2-P9.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3892228; DOI=10.1007/bf00332940;
RA   Cole S.T., Saint-Joanis B., Pugsley A.P.;
RT   "Molecular characterisation of the colicin E2 operon and identification of
RT   its products.";
RL   Mol. Gen. Genet. 198:465-472(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 377-581.
RX   PubMed=6095211; DOI=10.1093/nar/12.22.8733;
RA   Lau P.C.K., Rowsome R.W., Zuker M., Visentin L.P.;
RT   "Comparative nucleotide sequences encoding the immunity proteins and the
RT   carboxyl-terminal peptides of colicins E2 and E3.";
RL   Nucleic Acids Res. 12:8733-8745(1984).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 478-581.
RX   PubMed=2987833; DOI=10.1093/nar/13.5.1623;
RA   Masaki H., Toba M., Ohta T.;
RT   "Structure and expression of the ColE2-P9 immunity gene.";
RL   Nucleic Acids Res. 13:1623-1635(1985).
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; M29885; AAA23068.1; -; Genomic_DNA.
DR   EMBL; X01163; CAA25609.1; -; Genomic_DNA.
DR   EMBL; X02227; CAA26145.1; -; Genomic_DNA.
DR   PIR; I40687; NDECE2.
DR   PDB; 2YSU; X-ray; 3.50 A; B=313-447.
DR   PDB; 3U43; X-ray; 1.72 A; B=449-581.
DR   PDBsum; 2YSU; -.
DR   PDBsum; 3U43; -.
DR   AlphaFoldDB; P04419; -.
DR   SMR; P04419; -.
DR   TCDB; 1.C.1.4.1; the channel-forming colicin (colicin) family.
DR   EvolutionaryTrace; P04419; -.
DR   GO; GO:0005727; C:extrachromosomal circular DNA; IEA:InterPro.
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; IPR024575; Cloacin_colicin_fam.
DR   InterPro; IPR037146; Colicin/pyocin_DNase_dom_sf.
DR   InterPro; IPR024566; Colicin_R_dom.
DR   InterPro; IPR044925; His-Me_finger_sf.
DR   InterPro; IPR003615; HNH_nuc.
DR   InterPro; IPR016128; Pyosin/cloacin_T_dom.
DR   InterPro; IPR036302; Pyosin/cloacin_T_dom_sf.
DR   Pfam; PF03515; Cloacin; 1.
DR   Pfam; PF11570; E2R135; 1.
DR   PRINTS; PR01295; CLOACIN.
DR   SMART; SM00507; HNHc; 1.
DR   SUPFAM; SSF54060; SSF54060; 1.
DR   SUPFAM; SSF69369; SSF69369; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic; Antimicrobial; Bacteriocin; Endonuclease;
KW   Hydrolase; Metal-binding; Nuclease; Plasmid; Zinc.
FT   CHAIN           1..581
FT                   /note="Colicin-E2"
FT                   /id="PRO_0000218680"
FT   REGION          1..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          242..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          293..320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          421..488
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          513..566
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..257
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..320
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        421..456
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        464..488
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        531..556
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         549
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         574
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         578
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        429..431
FT                   /note="QER -> RS (in Ref. 2; CAA25609)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        473
FT                   /note="A -> R (in Ref. 2; CAA25609)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        504
FT                   /note="F -> L (in Ref. 2; CAA25609)"
FT                   /evidence="ECO:0000305"
FT   HELIX           325..375
FT                   /evidence="ECO:0007829|PDB:2YSU"
FT   STRAND          384..386
FT                   /evidence="ECO:0007829|PDB:2YSU"
FT   HELIX           387..440
FT                   /evidence="ECO:0007829|PDB:2YSU"
FT   HELIX           451..453
FT                   /evidence="ECO:0007829|PDB:3U43"
FT   HELIX           469..474
FT                   /evidence="ECO:0007829|PDB:3U43"
FT   HELIX           483..489
FT                   /evidence="ECO:0007829|PDB:3U43"
FT   STRAND          493..496
FT                   /evidence="ECO:0007829|PDB:3U43"
FT   HELIX           497..509
FT                   /evidence="ECO:0007829|PDB:3U43"
FT   HELIX           512..515
FT                   /evidence="ECO:0007829|PDB:3U43"
FT   HELIX           520..527
FT                   /evidence="ECO:0007829|PDB:3U43"
FT   HELIX           536..538
FT                   /evidence="ECO:0007829|PDB:3U43"
FT   STRAND          547..552
FT                   /evidence="ECO:0007829|PDB:3U43"
FT   HELIX           554..556
FT                   /evidence="ECO:0007829|PDB:3U43"
FT   TURN            563..565
FT                   /evidence="ECO:0007829|PDB:3U43"
FT   STRAND          566..569
FT                   /evidence="ECO:0007829|PDB:3U43"
FT   HELIX           571..578
FT                   /evidence="ECO:0007829|PDB:3U43"
SQ   SEQUENCE   581 AA;  61629 MW;  E3A1825DAEB75B6E CRC64;
     MSGGDGRGHN TGAHSTSGNI NGGPTGLGVG GGASDGSGWS SENNPWGGGS GSGIHWGGGS
     GHGNGGGNGN SGGGSGTGGN LSAVAAPVAF GFPALSTPGA GGLAVSISAG ALSAAIADIM
     AALKGPFKFG LWGVALYGVL PSQIAKDDPN MMSKIVTSLP ADDITESPVS SLPLDKATVN
     VNVRVVDDVK DERQNISVVS GVPMSVPVVD AKPTERPGVF TASIPGAPVL NISVNNSTPE
     VQTLSPGVTN NTDKDVRPAG FTQGGNTRDA VIRFPKDSGH NAVYVSVSDV LSPDQVKQRQ
     DEENRRQQEW DATHPVEAAE RNYERARAEL NQANEDVARN QERQAKAVQV YNSRKSELDA
     ANKTLADAIA EIKQFNRFAH DPMAGGHRMW QMAGLKAQRA QTDVNNKQAA FDAAAKEKSD
     ADAALSAAQE RRKQKENKEK DAKDKLDKES KRNKPGKATG KGKPVGDKWL DDAGKDSGAP
     IPDRIADKLR DKEFKNFDDF RKKFWEEVSK DPDLSKQFKG SNKTNIQKGK APFARKKDQV
     GGRERFELHH DKPISQDGGV YDMNNIRVTT PKRHIDIHRG K