CEA5_ECOLX
ID CEA5_ECOLX Reviewed; 180 AA.
AC P18000;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Colicin-E5;
DE EC=3.1.-.-;
DE Flags: Fragment;
GN Name=col;
OS Escherichia coli.
OG Plasmid ColE5-099.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2549375; DOI=10.1007/bf02464892;
RA Lau P.C.K., Condie J.A.;
RT "Nucleotide sequences from the colicin E5, E6 and E9 operons: presence of a
RT degenerate transposon-like structure in the ColE9-J plasmid.";
RL Mol. Gen. Genet. 217:269-277(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 6-180.
RX PubMed=2561131; DOI=10.1099/00221287-135-10-2783;
RA Curtis M.D., James R., Coddington A.;
RT "An evolutionary relationship between the ColE5-099 and the ColE9-J
RT plasmids revealed by nucleotide sequencing.";
RL J. Gen. Microbiol. 135:2783-2788(1989).
CC -!- FUNCTION: Colicins are polypeptide toxins produced by and active
CC against E.coli and closely related bacteria. This colicin is an
CC endonuclease.
CC -!- SIMILARITY: Belongs to the colicin/pyosin nuclease family.
CC {ECO:0000305}.
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DR EMBL; X15857; CAA33859.1; -; Genomic_DNA.
DR EMBL; M30445; AAA98051.1; -; Genomic_DNA.
DR PIR; A45799; A45799.
DR PIR; PQ0031; PQ0031.
DR PDB; 2A8K; X-ray; 1.50 A; A/B/C/D=74-180.
DR PDB; 2DFX; X-ray; 1.90 A; E=66-180.
DR PDB; 2DJH; X-ray; 1.90 A; A=66-180.
DR PDB; 2FHZ; X-ray; 1.15 A; B=74-180.
DR PDB; 3AO9; X-ray; 2.10 A; A/B=66-180.
DR PDB; 3VJ7; X-ray; 2.30 A; A=66-180.
DR PDBsum; 2A8K; -.
DR PDBsum; 2DFX; -.
DR PDBsum; 2DJH; -.
DR PDBsum; 2FHZ; -.
DR PDBsum; 3AO9; -.
DR PDBsum; 3VJ7; -.
DR AlphaFoldDB; P18000; -.
DR SMR; P18000; -.
DR EvolutionaryTrace; P18000; -.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0004540; F:ribonuclease activity; IEA:InterPro.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR Gene3D; 3.30.2310.30; -; 1.
DR InterPro; IPR038233; Colicin_D/E5_nuclease.
DR InterPro; IPR021964; Colicin_E5_C.
DR InterPro; IPR038234; Colicin_E5_C_sf.
DR Pfam; PF12106; Colicin_E5; 1.
DR SUPFAM; SSF102824; SSF102824; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Bacteriocin; Endonuclease;
KW Hydrolase; Nuclease; Plasmid.
FT CHAIN <1..180
FT /note="Colicin-E5"
FT /id="PRO_0000218681"
FT REGION 24..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..180
FT /note="Nuclease"
FT /evidence="ECO:0000255"
FT REGION 155..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 57
FT /note="K -> R (in Ref. 2; AAA98051)"
FT /evidence="ECO:0000305"
FT NON_TER 1
FT HELIX 88..93
FT /evidence="ECO:0007829|PDB:2FHZ"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:2FHZ"
FT HELIX 101..109
FT /evidence="ECO:0007829|PDB:2FHZ"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:2FHZ"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:2FHZ"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:2FHZ"
FT STRAND 132..141
FT /evidence="ECO:0007829|PDB:2FHZ"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:2FHZ"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:2FHZ"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:2FHZ"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:2A8K"
SQ SEQUENCE 180 AA; 19874 MW; 9DE1713F474B2BA4 CRC64;
RFAHDPMAGG HRMWQMAGLK AQRAQTDVNN KQAAFDAAAK EKADADAALS TAMESRKKKE
DNKRDAEGKL NDELAKNKGK IPGLKIDQKI RGQMPERGWT EDDIKNTVSN GATGTSFDKR
SPKKTPPDYL GRNDPATVYG SPGKYVVVND RTGEVTQISD KTDPGWVDDS RIQWGNKNDQ