ID   CDII_ECONC              Reviewed;         106 AA.
AC   P0DSM8;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   08-MAY-2019, sequence version 1.
DT   25-MAY-2022, entry version 9.
DE   RecName: Full=Immunity protein CdiI {ECO:0000303|PubMed:28973472};
DE   AltName: Full=CdiI-NC101;
GN   Name=cdiI {ECO:0000303|PubMed:28973472}; ORFNames=ECNC101_09169;
OS   Escherichia coli (strain NC101).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=753642;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NC101;
RA   Suzuki H., Richards V., Lefebure T., Pavinski Bitar P., Lang P.,
RA   Stanhope M.;
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION.
RC   STRAIN=NC101;
RX   PubMed=26305955; DOI=10.1073/pnas.1512124112;
RA   Willett J.L., Gucinski G.C., Fatherree J.P., Low D.A., Hayes C.S.;
RT   "Contact-dependent growth inhibition toxins exploit multiple independent
RT   cell-entry pathways.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:11341-11346(2015).
RN   [3] {ECO:0007744|PDB:5I4Q, ECO:0007744|PDB:5I4R}
RP   X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) IN COMPLEX WITH GDP; EF-TU AND
RP   CDIA-CT-NC101, FUNCTION, AND SUBUNIT.
RC   STRAIN=NC101;
RX   PubMed=28973472; DOI=10.1093/nar/gkx700;
RA   Michalska K., Gucinski G.C., Garza-Sanchez F., Johnson P.M., Stols L.M.,
RA   Eschenfeldt W.H., Babnigg G., Low D.A., Goulding C.W., Joachimiak A.,
RA   Hayes C.S.;
RT   "Structure of a novel antibacterial toxin that exploits elongation factor
RT   Tu to cleave specific transfer RNAs.";
RL   Nucleic Acids Res. 45:10306-10320(2017).
CC   -!- FUNCTION: Immunity protein component of a toxin-immunity protein
CC       module, which functions as a cellular contact-dependent growth
CC       inhibition (CDI) system. CDI modules allow bacteria to communicate with
CC       and inhibit the growth of closely related neighboring bacteria in a
CC       contact-dependent fashion. Neutralizes the toxic activity of cognate
CC       toxin CdiA-NC101 (the C-terminal 154 residue CT fragment)
CC       (PubMed:26305955). Does not inhibit toxic activity of CdiA from other
CC       toxin-immunity modules or strains of E.coli (Probable). Mediates
CC       dimerization of the ternary CdiA-CT-NC101, CdiI-NC101 and EF-Tu
CC       complex; both CdiI molecules contact both EF-Tu molecules
CC       (PubMed:28973472). {ECO:0000269|PubMed:26305955,
CC       ECO:0000269|PubMed:28973472, ECO:0000305|PubMed:26305955}.
CC   -!- SUBUNIT: Forms a contact-dependent growth inhibition complex of CdiA-
CC       CT-NC101, CdiI-NC101 and EF-Tu; the complex is a dimer of
CC       heterotrimers. {ECO:0000269|PubMed:28973472}.
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DR   EMBL; AEFA01000002; EFM55010.1; -; Genomic_DNA.
DR   RefSeq; WP_000355946.1; NZ_AEFA01000002.1.
DR   PDB; 5I4Q; X-ray; 2.35 A; B=1-106.
DR   PDB; 5I4R; X-ray; 3.30 A; B/F=1-106.
DR   PDBsum; 5I4Q; -.
DR   PDBsum; 5I4R; -.
DR   AlphaFoldDB; P0DSM8; -.
DR   SMR; P0DSM8; -.
PE   1: Evidence at protein level;
KW   3D-structure.
FT   CHAIN           1..106
FT                   /note="Immunity protein CdiI"
FT                   /id="PRO_0000447224"
FT   HELIX           4..40
FT                   /evidence="ECO:0007829|PDB:5I4Q"
FT   HELIX           44..66
FT                   /evidence="ECO:0007829|PDB:5I4Q"
FT   HELIX           74..82
FT                   /evidence="ECO:0007829|PDB:5I4Q"
FT   HELIX           88..99
FT                   /evidence="ECO:0007829|PDB:5I4Q"
SQ   SEQUENCE   106 AA;  13065 MW;  20B91075114AF47C CRC64;
     MDIWPEFQRD LEMYRDVVLS IKRNLRLYEE CIESLVHQIG STNFDNAQPL FDDLFRMQSE
     LATMLYKYEY KPGKRIQDLI YHLDRDDFYS RKYWHKKFSD GLAWPE