ID   DDDI_BURC1              Reviewed;         123 AA.
AC   P0DUH6;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   07-APR-2021, sequence version 1.
DT   25-MAY-2022, entry version 4.
DE   RecName: Full=Double-stranded DNA deaminase immunity protein {ECO:0000305};
DE            Short=DddI {ECO:0000303|PubMed:32641830};
GN   Name=dddI {ECO:0000303|PubMed:32641830}; ORFNames=I35_7838.5;
OS   Burkholderia cenocepacia (strain H111).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=1055524;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H111;
RX   PubMed=24723723; DOI=10.1128/genomea.00298-14;
RA   Carlier A., Agnoli K., Pessi G., Suppiger A., Jenul C., Schmid N.,
RA   Tuemmler B., Pinto-Carbo M., Eberl L.;
RT   "Genome Sequence of Burkholderia cenocepacia H111, a Cystic Fibrosis Airway
RT   Isolate.";
RL   Genome Announc. 2:0-0(2014).
RN   [2] {ECO:0007744|PDB:6U08}
RP   X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) IN COMPLEX WITH DDDA TOXIN DOMAIN,
RP   FUNCTION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC   STRAIN=H111;
RX   PubMed=32641830; DOI=10.1038/s41586-020-2477-4;
RA   Mok B.Y., de Moraes M.H., Zeng J., Bosch D.E., Kotrys A.V., Raguram A.,
RA   Hsu F., Radey M.C., Peterson S.B., Mootha V.K., Mougous J.D., Liu D.R.;
RT   "A bacterial cytidine deaminase toxin enables CRISPR-free mitochondrial
RT   base editing.";
RL   Nature 583:631-637(2020).
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. Bacteria that have this module inhibit or
CC       kill bacteria without it, giving them a growth advantage. Specifically
CC       inhibits the toxic activity of cognate toxin DddA (C-terminal 163
CC       residue fragment) upon expression in E.coli.
CC       {ECO:0000305|PubMed:32641830}.
CC   -!- SUBUNIT: The toxic domain forms a 1:1 complex with the DddI immunity
CC       protein. This protein blocks the active site of the toxin.
CC       {ECO:0000269|PubMed:32641830}.
CC   -!- DISRUPTION PHENOTYPE: A double dddA-dddI deletion has a 100-fold growth
CC       disadvantage compared to wild-type in competition experiments.
CC       {ECO:0000269|PubMed:32641830}.
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DR   EMBL; HG938372; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; WP_043205978.1; NZ_HG938372.1.
DR   PDB; 6U08; X-ray; 2.49 A; B/D/F/H=1-123.
DR   PDBsum; 6U08; -.
DR   AlphaFoldDB; P0DUH6; -.
DR   SMR; P0DUH6; -.
DR   InterPro; IPR025680; DddI.
DR   Pfam; PF14430; Imm1; 1.
PE   1: Evidence at protein level;
KW   3D-structure.
FT   CHAIN           1..123
FT                   /note="Double-stranded DNA deaminase immunity protein"
FT                   /id="PRO_0000452478"
SQ   SEQUENCE   123 AA;  13916 MW;  23B81C5ABA6028AF CRC64;
     MYADDFDGEI EIDEVDSLVE FLSRRPAFDA NNFVLTFEES GFPQLNIFAK NDIAVVYYMD
     IGENFVSKGN SASGGTEKFY ENKLGGEVDL SKDCVVSKEQ MIEAAKQFFA TKQRPEQLTW
     SEL