B3BM80 · CDIA4_ECO5C
- ProteinDeoxyribonuclease CdiA-o11
- GenecdiA4
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids377 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion (PubMed:21829394, PubMed:25174572).
The C-terminal 289 residues (the CT fragment) has a strong DNase activity in the presence of Zn2+, completely degrading supercoiled and linear plasmids, and inhibits growth. In the presence of Mg2+ it nicks dsDNA (PubMed:23236156).
Toxic activity is neutralized by coexpression of the cognate immunity protein CdiI-o11-EC869, but not by non-cognate immunity proteins from other toxin-immunity modules or other strains of E.coli (PubMed:21829394).
Gains access to the cytoplasm of target cells by using integral inner membrane protein YciB (PubMed:26305955).
The C-terminal 289 residues (the CT fragment) has a strong DNase activity in the presence of Zn2+, completely degrading supercoiled and linear plasmids, and inhibits growth. In the presence of Mg2+ it nicks dsDNA (PubMed:23236156).
Toxic activity is neutralized by coexpression of the cognate immunity protein CdiI-o11-EC869, but not by non-cognate immunity proteins from other toxin-immunity modules or other strains of E.coli (PubMed:21829394).
Gains access to the cytoplasm of target cells by using integral inner membrane protein YciB (PubMed:26305955).
Expression of this locus confers protection against other bacteria carrying the locus.
Cofactor
Note: Bind 1 Zn2+ per subunit.
Features
Showing features for active site, binding site.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | deoxyribonuclease I activity | |
Molecular Function | metal ion binding | |
Molecular Function | toxin activity |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDeoxyribonuclease CdiA-o11
- EC number
- Short namesDNase CdiA
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionB3BM80
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Note: Toxin translocation into the target cell depends on the proton motive force of the target cell, but not on tolA or tonB.
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 257 | Loss of DNase activity in vitro. | ||||
Sequence: E → A | ||||||
Mutagenesis | 278 | Loss of DNase activity in vitro and in vivo. Unable to inhibit target cell growth via CDI. | ||||
Sequence: D → A | ||||||
Mutagenesis | 322-330 | No longer interacts with cognate immunity protein CdiI-o11. | ||||
Sequence: KEYALSGRE → HTHTLSGEQ | ||||||
Mutagenesis | 322-332 | No longer interacts with cognate CdiI-o11, loss of DNase activity. | ||||
Sequence: KEYALSGRELT → GSG | ||||||
Mutagenesis | 323-329 | Still interacts with cognate immunity protein CdiI-o11. | ||||
Sequence: EYALSGR → TYSLSGV |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000429689 | 1-377 | Deoxyribonuclease CdiA-o11 | |||
Sequence: MVNATLSVVQKNSAFVGSATGELAARAIGMLYPGVKQSDLSEEQKQTISTLATVSAGLAGGLTGSSTASAAVGAQSGKNAVENNYLSTNQSLTFDKELSDCRKSGGNCQDIIDKWEKISDEQSAEIDQKLKDNPLEAQVIDKEVAKGGYDMTQRPGWLGNIGVEVMTSDEAKAYVQKWNGRDLTKIDVNSPEWTKFAVFASDPENQAMLVSGGLLVKDITKAAISFMSRNTATATVNASEVGMQWGQGNMKQGMPWEDYVGKSLPADARLPKNFKIFDYYDGATKTATSVKSIDTQTMAKLANPNQVYSSIKGNIDAAAKFKEYALSGRELTSSMISNREIQLAIPADTTKTQWAEINRAIEYGKSQGVKVTVTQVK |
Interaction
Subunit
Interacts with cognate immunity protein CdiI-o11-EC869, which blocks its toxic DNase activity.
Structure
Family & Domains
Features
Showing features for motif, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 81-84 | VENN CT cleavage motif | ||||
Sequence: VENN | ||||||
Region | 85-233 | Inner membrane translocation domain (IMTD), targets to YciB | ||||
Sequence: YLSTNQSLTFDKELSDCRKSGGNCQDIIDKWEKISDEQSAEIDQKLKDNPLEAQVIDKEVAKGGYDMTQRPGWLGNIGVEVMTSDEAKAYVQKWNGRDLTKIDVNSPEWTKFAVFASDPENQAMLVSGGLLVKDITKAAISFMSRNTAT | ||||||
Region | 88-377 | CT domain, sufficient to interact with CdiI | ||||
Sequence: TNQSLTFDKELSDCRKSGGNCQDIIDKWEKISDEQSAEIDQKLKDNPLEAQVIDKEVAKGGYDMTQRPGWLGNIGVEVMTSDEAKAYVQKWNGRDLTKIDVNSPEWTKFAVFASDPENQAMLVSGGLLVKDITKAAISFMSRNTATATVNASEVGMQWGQGNMKQGMPWEDYVGKSLPADARLPKNFKIFDYYDGATKTATSVKSIDTQTMAKLANPNQVYSSIKGNIDAAAKFKEYALSGRELTSSMISNREIQLAIPADTTKTQWAEINRAIEYGKSQGVKVTVTQVK | ||||||
Region | 222-377 | Has DNase activity in vivo, cannot be expressed in the absence of CdiI | ||||
Sequence: AAISFMSRNTATATVNASEVGMQWGQGNMKQGMPWEDYVGKSLPADARLPKNFKIFDYYDGATKTATSVKSIDTQTMAKLANPNQVYSSIKGNIDAAAKFKEYALSGRELTSSMISNREIQLAIPADTTKTQWAEINRAIEYGKSQGVKVTVTQVK |
Domain
A beta-hairpin (residues 322-332) fits into a pocket in cognate immunity protein CdiI-o11 and helps confer immunity protein specificity (PubMed:23236156, PubMed:26449640).
The inner membrane translocation domain (IMTD) targets the toxin to a specific target cell inner membrane protein (YciB in this case), which delivers the toxin to the target cell cytoplasm. Exchanging this IMTD between CdiA proteins alters the inner membrane protein delivery system but not the CdiI immunity protein, strongly suggesting CdiI recognizes only the toxic domain (PubMed:26305955).
The inner membrane translocation domain (IMTD) targets the toxin to a specific target cell inner membrane protein (YciB in this case), which delivers the toxin to the target cell cytoplasm. Exchanging this IMTD between CdiA proteins alters the inner membrane protein delivery system but not the CdiI immunity protein, strongly suggesting CdiI recognizes only the toxic domain (PubMed:26305955).
Family and domain databases
Sequence
- Sequence statusComplete
- Length377
- Mass (Da)40,578
- Last updated2008-07-22 v1
- ChecksumD90AB8DC831A6E03
Keywords
- Technical term