CEA7_ECOLX
ID CEA7_ECOLX Reviewed; 576 AA.
AC Q47112; Q51604;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Colicin-E7;
DE EC=3.1.-.-;
GN Name=colE7; Synonyms=cea;
OS Escherichia coli.
OG Plasmid ColE7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K317;
RX PubMed=1603061; DOI=10.1007/bf00587577;
RA Soong B.W., Lu F.M., Chak K.-F.;
RT "Characterization of the cea gene of the ColE7 plasmid.";
RL Mol. Gen. Genet. 233:177-183(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 371-576.
RC STRAIN=K317;
RA Lau P.C.K., Parsons M.;
RT "Nucleotide sequence encoding the immunity and lysis proteins and the
RT carboxyl-terminal peptides of colicins E4 and E7.";
RL Submitted (DEC-1991) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 371-576.
RX PubMed=10368275; DOI=10.1016/s0969-2126(99)80012-4;
RA Ko T.P., Liao C.C., Ku W.-Y., Chak K.-F., Yuan H.S.;
RT "The crystal structure of the DNase domain of colicin E7 in complex with
RT its inhibitor Im7 protein.";
RL Structure 7:91-102(1999).
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 -!- INTERACTION:
CC Q47112; P13479: imm; NbExp=3; IntAct=EBI-1035016, EBI-1029882;
CC Q47112; Q03708: imm; NbExp=7; IntAct=EBI-1035016, EBI-1035025;
CC -!- SIMILARITY: Belongs to the colicin/pyosin nuclease family.
CC {ECO:0000305}.
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DR EMBL; M62409; AAA98054.1; -; Genomic_DNA.
DR EMBL; X63620; CAA45164.1; -; Genomic_DNA.
DR PIR; S22453; S22453.
DR RefSeq; WP_021530049.1; NZ_WSXM01000092.1.
DR RefSeq; YP_009060493.1; NC_024962.1.
DR PDB; 1M08; X-ray; 2.10 A; A/B=447-576.
DR PDB; 1MZ8; X-ray; 2.00 A; B/D=446-576.
DR PDB; 1PT3; X-ray; 2.50 A; A/B=449-576.
DR PDB; 1UJZ; X-ray; 2.10 A; B=446-573.
DR PDB; 1ZNS; X-ray; 2.50 A; A=444-576.
DR PDB; 1ZNV; X-ray; 2.00 A; B/D=444-576.
DR PDB; 2AXC; X-ray; 1.70 A; A=60-316.
DR PDB; 2ERH; X-ray; 2.00 A; B=447-573.
DR PDB; 2IVH; X-ray; 2.80 A; A=449-576.
DR PDB; 2JAZ; X-ray; 2.03 A; B/D=446-576.
DR PDB; 2JB0; X-ray; 1.91 A; B=446-576.
DR PDB; 2JBG; X-ray; 2.20 A; B/D=446-576.
DR PDB; 3FBD; X-ray; 2.90 A; A/D=445-576.
DR PDB; 3GJN; X-ray; 2.48 A; B/C=446-576.
DR PDB; 3GKL; X-ray; 2.20 A; A/B=446-576.
DR PDB; 3ZFK; X-ray; 1.70 A; A/B=450-573.
DR PDB; 7CEI; X-ray; 2.30 A; B=371-576.
DR PDBsum; 1M08; -.
DR PDBsum; 1MZ8; -.
DR PDBsum; 1PT3; -.
DR PDBsum; 1UJZ; -.
DR PDBsum; 1ZNS; -.
DR PDBsum; 1ZNV; -.
DR PDBsum; 2AXC; -.
DR PDBsum; 2ERH; -.
DR PDBsum; 2IVH; -.
DR PDBsum; 2JAZ; -.
DR PDBsum; 2JB0; -.
DR PDBsum; 2JBG; -.
DR PDBsum; 3FBD; -.
DR PDBsum; 3GJN; -.
DR PDBsum; 3GKL; -.
DR PDBsum; 3ZFK; -.
DR PDBsum; 7CEI; -.
DR AlphaFoldDB; Q47112; -.
DR SMR; Q47112; -.
DR DIP; DIP-16990N; -.
DR IntAct; Q47112; 2.
DR PRIDE; Q47112; -.
DR EvolutionaryTrace; Q47112; -.
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..576
FT /note="Colicin-E7"
FT /id="PRO_0000218682"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..451
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..545
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 544
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 569
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 573
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:2AXC"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:2AXC"
FT HELIX 109..116
FT /evidence="ECO:0007829|PDB:2AXC"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:2AXC"
FT HELIX 136..142
FT /evidence="ECO:0007829|PDB:2AXC"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:2AXC"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:2AXC"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:2AXC"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:2AXC"
FT STRAND 179..185
FT /evidence="ECO:0007829|PDB:2AXC"
FT STRAND 188..197
FT /evidence="ECO:0007829|PDB:2AXC"
FT STRAND 199..205
FT /evidence="ECO:0007829|PDB:2AXC"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:2AXC"
FT STRAND 222..229
FT /evidence="ECO:0007829|PDB:2AXC"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:2AXC"
FT TURN 258..261
FT /evidence="ECO:0007829|PDB:2AXC"
FT STRAND 262..268
FT /evidence="ECO:0007829|PDB:2AXC"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:2AXC"
FT STRAND 278..284
FT /evidence="ECO:0007829|PDB:2AXC"
FT HELIX 288..307
FT /evidence="ECO:0007829|PDB:2AXC"
FT STRAND 447..449
FT /evidence="ECO:0007829|PDB:3FBD"
FT STRAND 451..454
FT /evidence="ECO:0007829|PDB:1ZNV"
FT TURN 462..469
FT /evidence="ECO:0007829|PDB:3ZFK"
FT HELIX 478..484
FT /evidence="ECO:0007829|PDB:3ZFK"
FT STRAND 488..491
FT /evidence="ECO:0007829|PDB:3ZFK"
FT HELIX 492..504
FT /evidence="ECO:0007829|PDB:3ZFK"
FT HELIX 507..510
FT /evidence="ECO:0007829|PDB:3ZFK"
FT HELIX 515..522
FT /evidence="ECO:0007829|PDB:3ZFK"
FT HELIX 531..533
FT /evidence="ECO:0007829|PDB:3ZFK"
FT STRAND 542..547
FT /evidence="ECO:0007829|PDB:3ZFK"
FT HELIX 549..551
FT /evidence="ECO:0007829|PDB:3ZFK"
FT STRAND 555..557
FT /evidence="ECO:0007829|PDB:3ZFK"
FT HELIX 558..560
FT /evidence="ECO:0007829|PDB:3ZFK"
FT STRAND 561..564
FT /evidence="ECO:0007829|PDB:3ZFK"
FT HELIX 566..572
FT /evidence="ECO:0007829|PDB:3ZFK"
FT TURN 573..575
FT /evidence="ECO:0007829|PDB:2JAZ"
SQ SEQUENCE 576 AA; 61350 MW; E5B05E73B2E17249 CRC64;
MSGGDGRGHN SGAHNTGGNI NGGPTGLGGN GGASDGSGWS SENNPWGGGS GSGVHWGGGS
GHGNGGGNSN SGGGSNSSVA APMAFGFPAL AAPGAGTLGI SVSGEALSAA IADIFAALKG
PFKFSAWGIA LYGILPSEIA KDDPNMMSKI VTSLPAETVT NVQVSTLPLD QATVSVTKRV
TDVVKDTRQH IAVVAGVPMS VPVVNAKPTR TPGVFHASFP GVPSLTVSTV KGLPVSTTLP
RGITEDKGRT AVPAGFTFGG GSHEAVIRFP KESGQKPVYV SVTDVLTPAQ VKQRQDEEKR
LQQEWNDAHP VEVAERNYEQ ARAELNQANK DVARNQERQA KAVQVYNSRK SELDAANKTL
ADAKAEIKQF ERFAREPMAA GHRMWQMAGL KAQRAQTDVN NKKAAFDAAA KEKSDADVAL
SSALERRKQK ENKEKDAKAK LDKESKRNKP GKATGKGKPV NNKWLNNAGK DLGSPVPDRI
ANKLRDKEFK SFDDFRKKFW EEVSKDPELS KQFSRNNNDR MKVGKAPKTR TQDVSGKRTS
FELHHEKPIS QNGGVYDMDN ISVVTPKRHI DIHRGK
