ID   CDII_ECOL5              Reviewed;         128 AA.
AC   Q0T964;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Immunity protein CdiI {ECO:0000303|PubMed:21085179};
GN   Name=cdiI {ECO:0000303|PubMed:21085179}; OrderedLocusNames=ECP_4579;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=536 / UPEC;
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(2006).
RN   [2]
RP   FUNCTION, STRAIN SPECIFICITY, INTERACTION WITH CDIA-CT, AND SUBUNIT.
RC   STRAIN=536 / UPEC;
RX   PubMed=21085179; DOI=10.1038/nature09490;
RA   Aoki S.K., Diner E.J., de Roodenbeke C.T., Burgess B.R., Poole S.J.,
RA   Braaten B.A., Jones A.M., Webb J.S., Hayes C.S., Cotter P.A., Low D.A.;
RT   "A widespread family of polymorphic contact-dependent toxin delivery
RT   systems in bacteria.";
RL   Nature 468:439-442(2010).
RN   [3]
RP   FUNCTION, AND SUBUNIT.
RC   STRAIN=536 / UPEC;
RX   PubMed=22333533; DOI=10.1101/gad.182345.111;
RA   Diner E.J., Beck C.M., Webb J.S., Low D.A., Hayes C.S.;
RT   "Identification of a target cell permissive factor required for contact-
RT   dependent growth inhibition (CDI).";
RL   Genes Dev. 26:515-525(2012).
RN   [4]
RP   FUNCTION.
RC   STRAIN=536 / UPEC;
RX   PubMed=24889811; DOI=10.1111/mmi.12658;
RA   Beck C.M., Diner E.J., Kim J.J., Low D.A., Hayes C.S.;
RT   "The F pilus mediates a novel pathway of CDI toxin import.";
RL   Mol. Microbiol. 93:276-290(2014).
RN   [5] {ECO:0007744|PDB:5J5V}
RP   X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH CDIA AND CYSK,
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=27531961; DOI=10.1073/pnas.1607112113;
RA   Johnson P.M., Beck C.M., Morse R.P., Garza-Sanchez F., Low D.A.,
RA   Hayes C.S., Goulding C.W.;
RT   "Unraveling the essential role of CysK in CDI toxin activation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:9792-9797(2016).
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 nuclease
CC       activity of CdiA, its cognate toxin protein, but not against CdiA from
CC       E.coli strain EC93 or D.dadantii strain 3937. Binding to CdiA-CT in the
CC       CdiA-CysK complex probably blocks the tRNA-binding site of CdiA-CT
CC       (PubMed:27531961). {ECO:0000269|PubMed:21085179,
CC       ECO:0000269|PubMed:22333533, ECO:0000269|PubMed:24889811,
CC       ECO:0000269|PubMed:27531961}.
CC   -!- SUBUNIT: Interacts with cognate CdiA-CT but not CdiA-CT from D.dadantii
CC       strain 3937 (PubMed:21085179). CysK forms a complex with CdiA-CT/CdiI
CC       (PubMed:22333533). One CdiA toxin subunit binds to each subunit of the
CC       CysK homodimer, and one CdiI immunity protein binds to each toxin
CC       subunit; the immune complex is thus a dimer of trimers
CC       (PubMed:27531961). {ECO:0000269|PubMed:21085179,
CC       ECO:0000269|PubMed:22333533, ECO:0000269|PubMed:27531961}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000247; ABG72515.1; -; Genomic_DNA.
DR   RefSeq; WP_000631802.1; NC_008253.1.
DR   PDB; 5J5V; X-ray; 2.75 A; C/F=1-128.
DR   PDBsum; 5J5V; -.
DR   AlphaFoldDB; Q0T964; -.
DR   SMR; Q0T964; -.
DR   STRING; 362663.ECP_4579; -.
DR   EnsemblBacteria; ABG72515; ABG72515; ECP_4579.
DR   KEGG; ecp:ECP_4579; -.
DR   HOGENOM; CLU_1956160_0_0_6; -.
DR   OMA; QKGTFAQ; -.
DR   Proteomes; UP000009182; Chromosome.
DR   InterPro; IPR040547; CdiI.
DR   Pfam; PF18616; CdiI_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure.
FT   CHAIN           1..128
FT                   /note="Immunity protein CdiI"
FT                   /id="PRO_0000432078"
FT   HELIX           4..8
FT                   /evidence="ECO:0007829|PDB:5J5V"
FT   HELIX           17..19
FT                   /evidence="ECO:0007829|PDB:5J5V"
FT   HELIX           22..30
FT                   /evidence="ECO:0007829|PDB:5J5V"
FT   HELIX           35..37
FT                   /evidence="ECO:0007829|PDB:5J5V"
FT   HELIX           40..48
FT                   /evidence="ECO:0007829|PDB:5J5V"
FT   HELIX           53..66
FT                   /evidence="ECO:0007829|PDB:5J5V"
FT   STRAND          72..74
FT                   /evidence="ECO:0007829|PDB:5J5V"
FT   HELIX           77..82
FT                   /evidence="ECO:0007829|PDB:5J5V"
FT   HELIX           87..89
FT                   /evidence="ECO:0007829|PDB:5J5V"
FT   HELIX           94..104
FT                   /evidence="ECO:0007829|PDB:5J5V"
FT   HELIX           113..121
FT                   /evidence="ECO:0007829|PDB:5J5V"
SQ   SEQUENCE   128 AA;  14817 MW;  6D3CC98652073EE9 CRC64;
     MITLRKLIGN INMTKEPEQQ SPLELWFERI IDVPLEKLTV EDLCRAIRQN LCIDQLMPRV
     LEVLTKEPLA GEYYDGELIA ALSTIKGEDL KDQKSTFTQI RQLINQLEPS DINDDLRKDI
     LKINQIIV