ID   CDII_ECOST              Reviewed;         121 AA.
AC   A0A1S4NYE4;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   08-MAY-2019, sequence version 2.
DT   25-MAY-2022, entry version 9.
DE   RecName: Full=Immunity protein CdiI;
DE   AltName: Full=CdiI-STECO31;
GN   Name=cdiI {ECO:0000303|PubMed:29923643}; Synonyms=ECSTECO31_4008;
OS   Escherichia coli (strain STEC_O31).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=754081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=STEC_O31;
RA   Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., Jones K.,
RA   Santana-Cruz I., Liu X.;
RL   Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000312|PDB:5HKQ}
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH CDIA, FUNCTION, AND
RP   SUBUNIT.
RC   STRAIN=STEC_031;
RX   PubMed=29923643; DOI=10.1111/mmi.14007;
RA   Michalska K., Quan Nhan D., Willett J.L.E., Stols L.M., Eschenfeldt W.H.,
RA   Jones A.M., Nguyen J.Y., Koskiniemi S., Low D.A., Goulding C.W.,
RA   Joachimiak A., Hayes C.S.;
RT   "Functional plasticity of antibacterial EndoU toxins.";
RL   Mol. Microbiol. 109:509-527(2018).
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. Protects cells against the tRNA endonuclease
CC       activity of cognate toxin CdiA-STECO31 but not other non-cognate
CC       toxins, inhibits the tRNase activity of the isolated CT fragment of
CC       CdiA-STECO31. Binds the CT fragment of CdiA-STECO31, between two
CC       subdomains. {ECO:0000269|PubMed:29923643}.
CC   -!- SUBUNIT: Forms a 1:1 complex with cognate toxin CdiA-STECO31, binding
CC       between 2 toxin subdomains. {ECO:0000269|PubMed:29923643}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EJK94115.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305|PubMed:29923643};
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DR   EMBL; AFEX01000038; EJK94115.1; ALT_INIT; Genomic_DNA.
DR   PDB; 5HKQ; X-ray; 2.00 A; I=1-121.
DR   PDBsum; 5HKQ; -.
DR   AlphaFoldDB; A0A1S4NYE4; -.
DR   SMR; A0A1S4NYE4; -.
DR   InterPro; IPR041256; CdiI_4.
DR   Pfam; PF18624; CdiI_4; 1.
PE   1: Evidence at protein level;
KW   3D-structure.
FT   CHAIN           1..121
FT                   /note="Immunity protein CdiI"
FT                   /id="PRO_0000446872"
FT   HELIX           16..28
FT                   /evidence="ECO:0007829|PDB:5HKQ"
FT   HELIX           32..40
FT                   /evidence="ECO:0007829|PDB:5HKQ"
FT   STRAND          45..47
FT                   /evidence="ECO:0007829|PDB:5HKQ"
FT   STRAND          50..53
FT                   /evidence="ECO:0007829|PDB:5HKQ"
FT   HELIX           62..64
FT                   /evidence="ECO:0007829|PDB:5HKQ"
FT   STRAND          67..76
FT                   /evidence="ECO:0007829|PDB:5HKQ"
FT   HELIX           79..81
FT                   /evidence="ECO:0007829|PDB:5HKQ"
FT   STRAND          82..85
FT                   /evidence="ECO:0007829|PDB:5HKQ"
FT   HELIX           87..104
FT                   /evidence="ECO:0007829|PDB:5HKQ"
FT   HELIX           106..108
FT                   /evidence="ECO:0007829|PDB:5HKQ"
FT   HELIX           109..116
FT                   /evidence="ECO:0007829|PDB:5HKQ"
SQ   SEQUENCE   121 AA;  14347 MW;  4C37AFBE4649EADE CRC64;
     MNKYLFELPY ERSEPGWTIR SYFDLMYNEN RFLDAVENIV NKESYILDGI YCNFPDMNSY
     DESEHFEGVE FAVGYPPDED DIVIVSEETC FEYVRLACEK YLQLHPEDTE KVNKLLSKIP
     S