CDII4_ECO5C
ID CDII4_ECO5C Reviewed; 167 AA.
AC B3BM81;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=Immunity protein CdiI-o11;
DE Short=CdiI-o11-EC869;
GN Name=cdiI4; Synonyms=cdiIo11; ORFNames=ECH7EC869_5884;
OS Escherichia coli O157:H7 (strain EC869).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=478008;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC869;
RX PubMed=21421787; DOI=10.1128/aem.02554-10;
RA Eppinger M., Mammel M.K., Leclerc J.E., Ravel J., Cebula T.A.;
RT "Genome signatures of Escherichia coli O157:H7 isolates from the bovine
RT host reservoir.";
RL Appl. Environ. Microbiol. 77:2916-2925(2011).
RN [2]
RP FUNCTION, INTERACTION WITH CDIA, AND SUBUNIT.
RC STRAIN=EC869;
RX PubMed=21829394; DOI=10.1371/journal.pgen.1002217;
RA Poole S.J., Diner E.J., Aoki S.K., Braaten B.A., t'Kint de Roodenbeke C.,
RA Low D.A., Hayes C.S.;
RT "Identification of functional toxin/immunity genes linked to contact-
RT dependent growth inhibition (CDI) and rearrangement hotspot (Rhs)
RT systems.";
RL PLoS Genet. 7:E1002217-E1002217(2011).
RN [3]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=EC869;
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 [4] {ECO:0007744|PDB:4G6U}
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH CDIA, FUNCTION AS AN
RP IMMUNITY PROTEIN, AND SUBUNIT.
RC STRAIN=EC869;
RX PubMed=23236156; DOI=10.1073/pnas.1216238110;
RA Morse R.P., Nikolakakis K.C., Willett J.L., Gerrick E., Low D.A.,
RA Hayes C.S., Goulding C.W.;
RT "Structural basis of toxicity and immunity in contact-dependent growth
RT inhibition (CDI) systems.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:21480-21485(2012).
RN [5] {ECO:0007744|PDB:4ZQW}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH MACROCYCLIC PEPTIDE.
RX PubMed=26449640; DOI=10.1016/j.jmb.2015.09.020;
RA Morse R.P., Willett J.L., Johnson P.M., Zheng J., Credali A., Iniguez A.,
RA Nowick J.S., Hayes C.S., Goulding C.W.;
RT "Diversification of beta-augmentation interactions between CDI
RT toxin/immunity proteins.";
RL J. Mol. Biol. 427:3766-3784(2015).
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 (PubMed:21829394). Neutralizes the toxic
CC activity of cognate toxin CdiA-o11-EC869 (the C-terminal 289 residue CT
CC fragment). Does not inhibit toxic activity of CdiA from other toxin-
CC immunity modules or strains of E.coli (PubMed:21829394,
CC PubMed:26305955) (Probable). {ECO:0000269|PubMed:21829394,
CC ECO:0000269|PubMed:26305955, ECO:0000305|PubMed:23236156,
CC ECO:0000305|PubMed:26449640}.
CC -!- FUNCTION: Expression of this locus confers protection against other
CC bacteria carrying the locus. {ECO:0000269|PubMed:21829394}.
CC -!- SUBUNIT: Interacts with the C-terminal fragment (CT, residues 88-377)
CC of cognate toxin protein CdiA-o11-EC869 (PubMed:21829394,
CC PubMed:23236156, PubMed:26449640). Probably recognizes only the toxic
CC DNase subdomain of CdiA-o11-EC869 (approximately residues 222-377)
CC (Probable). {ECO:0000269|PubMed:21829394, ECO:0000269|PubMed:23236156,
CC ECO:0000269|PubMed:26449640, ECO:0000305|PubMed:26305955}.
CC -!- CAUTION: The sequences characterized in (PubMed:21829394) and
CC crystallized in (PubMed:23236156) are actually derived from cdiA-
CC CTo11/cdiIo11, an orphan cdiA-CT/cdiI module that only encodes the cdiA
CC CT fragment and its associated cdiI. It is however identical to that
CC shown in this entry, which does have the elements necessary for gene
CC expression. {ECO:0000305|PubMed:21829394, ECO:0000305|PubMed:23236156}.
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DR EMBL; ABHU01000020; EDU89602.1; -; Genomic_DNA.
DR RefSeq; WP_000885242.1; NZ_ABHU01000020.1.
DR PDB; 4G6U; X-ray; 2.35 A; B=1-167.
DR PDB; 4ZQW; X-ray; 2.00 A; B/D=1-167.
DR PDBsum; 4G6U; -.
DR PDBsum; 4ZQW; -.
DR AlphaFoldDB; B3BM81; -.
DR SMR; B3BM81; -.
DR EnsemblBacteria; EDU89602; EDU89602; ECH7EC869_5884.
DR Proteomes; UP000004641; Unassembled WGS sequence.
DR CDD; cd13445; CDI_inhibitor_EC869_like; 1.
DR Gene3D; 3.40.1590.10; -; 1.
DR InterPro; IPR009888; CdiI_Proteobact.
DR InterPro; IPR037891; Cdil-like_sf.
DR Pfam; PF07262; CdiI; 1.
DR SUPFAM; SSF160207; SSF160207; 1.
PE 1: Evidence at protein level;
KW 3D-structure.
FT CHAIN 1..167
FT /note="Immunity protein CdiI-o11"
FT /id="PRO_0000429690"
FT STRAND 8..16
FT /evidence="ECO:0007829|PDB:4ZQW"
FT STRAND 19..33
FT /evidence="ECO:0007829|PDB:4ZQW"
FT HELIX 48..60
FT /evidence="ECO:0007829|PDB:4ZQW"
FT HELIX 68..75
FT /evidence="ECO:0007829|PDB:4ZQW"
FT HELIX 77..95
FT /evidence="ECO:0007829|PDB:4ZQW"
FT HELIX 100..105
FT /evidence="ECO:0007829|PDB:4ZQW"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:4ZQW"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:4ZQW"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:4ZQW"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:4ZQW"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:4ZQW"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:4ZQW"
FT HELIX 151..162
FT /evidence="ECO:0007829|PDB:4ZQW"
SQ SEQUENCE 167 AA; 18957 MW; 3BD28B9B78755757 CRC64;
MAFNKDQDYW ANIFVTPDFL SVETYSGLGM TGRDPLFSPR LLQPDVDDKS LGEEILQALS
DSRTLDVLEE RVAFFDLEKS KEQYAAWIAT LMEKYGYRTK RALFKNMKKV GIHLVNDVIT
IRPSFHEKLE AWSGNRINES DYVVLPADSS PTEIGSGLRL ALSRCKG
