IMM7_ECOLX
ID IMM7_ECOLX Reviewed; 87 AA.
AC Q03708; Q47113;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Colicin-E7 immunity protein;
DE AltName: Full=ImmE7;
DE AltName: Full=Microcin-E7 immunity protein;
GN Name=imm; Synonyms=ceiE7;
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].
RX PubMed=2045785; DOI=10.1099/00221287-137-1-91;
RA Chak K.-F., Kuo W.S., Lu F.M., James R.;
RT "Cloning and characterization of the ColE7 plasmid.";
RL J. Gen. Microbiol. 137:91-100(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 (JUL-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=8692833; DOI=10.1073/pnas.93.13.6437;
RA Chak K.-F., Safo M.K., Ku W.-Y., Hsieh S.-Y., Yuan H.S.;
RT "The crystal structure of the immunity protein of colicin E7 suggests a
RT possible colicin-interacting surface.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:6437-6442(1996).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=9135159; DOI=10.1093/emboj/16.6.1444;
RA Hsieh S.-Y., Ko T.P., Tseng M.Y., Ku W.-Y., Chak K.-F., Yuan H.S.;
RT "A novel role of ImmE7 in the autoregulatory expression of the ColE7 operon
RT and identification of possible RNase active sites in the crystal structure
RT of dimeric ImmE7.";
RL EMBO J. 16:1444-1454(1997).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
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 protein is able to protect a cell, which harbors the
CC plasmid ColE7 encoding colicin E7, against colicin E7, it binds
CC specifically to the DNase-type colicin and inhibits its bactericidal
CC activity. Dimeric ImmE7 may possess a RNase activity that cleaves its
CC own mRNA at a specific site and thus autoregulates translational
CC expression of the downstream ceiE7 gene as well as degradation of the
CC upstream ceaE7 mRNA.
CC -!- INTERACTION:
CC Q03708; Q47112: colE7; NbExp=7; IntAct=EBI-1035025, EBI-1035016;
CC Q03708; P77754: spy; Xeno; NbExp=2; IntAct=EBI-1035025, EBI-1121716;
CC -!- SIMILARITY: Belongs to the colicins ColE2/ColE8/ColE9 and pyocins S1/S2
CC family. {ECO:0000305}.
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DR EMBL; M57540; AAA23071.1; -; Genomic_DNA.
DR EMBL; X63620; CAA45165.1; -; Genomic_DNA.
DR PIR; S27394; S27394.
DR RefSeq; WP_001560791.1; NZ_WSXM01000092.1.
DR RefSeq; YP_009060494.1; NC_024962.1.
DR PDB; 1AYI; X-ray; 2.00 A; A=1-87.
DR PDB; 1CEI; X-ray; 1.80 A; A=1-87.
DR PDB; 1MZ8; X-ray; 2.00 A; A/C=1-87.
DR PDB; 1UJZ; X-ray; 2.10 A; A=1-87.
DR PDB; 1UNK; X-ray; 1.80 A; A/B/C/D=1-87.
DR PDB; 1ZNV; X-ray; 2.00 A; A/C=1-87.
DR PDB; 2ERH; X-ray; 2.00 A; A=1-87.
DR PDB; 2JAZ; X-ray; 2.03 A; A/C=1-87.
DR PDB; 2JB0; X-ray; 1.91 A; A=1-87.
DR PDB; 2JBG; X-ray; 2.20 A; A/C=1-87.
DR PDB; 2K0D; NMR; -; X=2-87.
DR PDB; 4F37; X-ray; 2.57 A; A/B=2-87.
DR PDB; 5WNW; X-ray; 1.79 A; C=6-45.
DR PDB; 7CEI; X-ray; 2.30 A; A=1-87.
DR PDBsum; 1AYI; -.
DR PDBsum; 1CEI; -.
DR PDBsum; 1MZ8; -.
DR PDBsum; 1UJZ; -.
DR PDBsum; 1UNK; -.
DR PDBsum; 1ZNV; -.
DR PDBsum; 2ERH; -.
DR PDBsum; 2JAZ; -.
DR PDBsum; 2JB0; -.
DR PDBsum; 2JBG; -.
DR PDBsum; 2K0D; -.
DR PDBsum; 4F37; -.
DR PDBsum; 5WNW; -.
DR PDBsum; 7CEI; -.
DR AlphaFoldDB; Q03708; -.
DR BMRB; Q03708; -.
DR SMR; Q03708; -.
DR DIP; DIP-16989N; -.
DR IntAct; Q03708; 3.
DR TCDB; 8.B.24.5.5; the colicin immunity protein (colip) functional family.
DR EvolutionaryTrace; Q03708; -.
DR GO; GO:0015643; F:toxic substance binding; IEA:InterPro.
DR GO; GO:0030153; P:bacteriocin immunity; IEA:UniProtKB-KW.
DR CDD; cd16363; Col_Im_like; 1.
DR Gene3D; 1.10.1200.20; -; 1.
DR InterPro; IPR035900; Colicin_E_sf.
DR InterPro; IPR000290; Colicin_pyocin.
DR Pfam; PF01320; Colicin_Pyocin; 1.
DR PRINTS; PR01299; PYOCIN.
DR SUPFAM; SSF47345; SSF47345; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Bacteriocin immunity; Plasmid.
FT CHAIN 1..87
FT /note="Colicin-E7 immunity protein"
FT /id="PRO_0000218708"
FT CONFLICT 4
FT /note="K -> E (in Ref. 1; AAA23071)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="V -> E (in Ref. 1; AAA23071)"
FT /evidence="ECO:0000305"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:1CEI"
FT HELIX 12..25
FT /evidence="ECO:0007829|PDB:1CEI"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:1CEI"
FT HELIX 32..45
FT /evidence="ECO:0007829|PDB:1CEI"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:1CEI"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:1CEI"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:4F37"
FT HELIX 65..78
FT /evidence="ECO:0007829|PDB:1CEI"
SQ SEQUENCE 87 AA; 9895 MW; 2CA7D97057529335 CRC64;
MELKNSISDY TEAEFVQLLK EIEKENVAAT DDVLDVLLEH FVKITEHPDG TDLIYYPSDN
RDDSPEGIVK EIKEWRAANG KPGFKQG
