{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"C4SGN7","uniProtkbId":"CDIA_YERMW","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2009-07-28","entryVersion":66,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Yersinia mollaretii (strain ATCC 43969 / DSM 18520 / CIP 103324 / CNY 7263 / WAIP 204)","taxonId":349967,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Yersiniaceae","Yersinia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"29923643"}],"value":"tRNA nuclease CdiA"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"29923643"}],"value":"tRNase CdiA"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29923643"}],"value":"3.1.-.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"29923643"}],"value":"Contact-dependent inhibitor A"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"29923643"}],"value":"CdiA-43969"}]},{"fullName":{"value":"Toxin CdiA"}}],"flag":"Precursor"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"29923643"}],"value":"cdiA"},"orfNames":[{"value":"ymoll0001_27200"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29923643"}],"value":"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. Targeting of the CT domain (residues 2824-2963) in the absence of immunity protein inhibits cell growth and causes tRNA(UUC-Glu) cleavage in the anticodon loop; expression of cognate immunity protein CdiI-43969 neutralizes growth inhibition and tRNA(UUC-Glu) remains intact, whereas non-cognate immunity proteins do not confer protection from the toxic effects"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"The CdiA protein is thought to be exported from the cell through the central lumen of CdiB, the other half of its two-partner system (TPS). The TPS domain probably remains associated with CdiB while the FHA-1 domain forms an extended filament with the receptor-binding domain (RBD) at its extremity; in the secretion arrested state the C-terminus of the RBD and YP domains form a hairpin-like structure as the FHA-2, PT and CT domains are periplasmic. The YP domain is probably responsible for this arrest at the point where it re-enters the host cell periplasm. Upon binding to a target cell outer membrane receptor a signal is transmitted to activate secretion. The filament elongates slightly, the rest of CdiA is secreted and the FHA-2 domain becomes stably associated with the target cell's outer membrane where it facilitates entry of the toxic CT domain into the target cell periplasm. From there the toxic CT domain is cleaved and gains access to the target cell cytoplasm via an inner membrane protein"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"29923643"}],"value":"Forms a 1:1 complex with cognate immunity protein CdiI"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Secreted to the cell surface by CdiB, its two partner secretion pathway (TPS) partner"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255"}],"value":"Secreted","id":"SL-0243"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"29923643"}],"value":"Target cell, target cell cytoplasm","id":"SL-0486"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"In the N-terminal section; belongs to the CdiA toxin family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"In the C-terminal section; belongs to the bacterial EndoU family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":29,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Chain","location":{"start":{"value":30,"modifier":"EXACT"},"end":{"value":2963,"modifier":"EXACT"}},"description":"tRNA nuclease CdiA","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":"PRO_0000446870"},{"type":"Region","location":{"start":{"value":35,"modifier":"EXACT"},"end":{"value":320,"modifier":"EXACT"}},"description":"Two-partner system transport domain (TPS)","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q3YL96"}]},{"type":"Region","location":{"start":{"value":573,"modifier":"EXACT"},"end":{"value":1074,"modifier":"EXACT"}},"description":"FHA-1","evidences":[{"evidenceCode":"ECO:0000305"}]},{"type":"Region","location":{"start":{"value":1075,"modifier":"EXACT"},"end":{"value":1342,"modifier":"EXACT"}},"description":"Receptor binding domain (RBD)","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"A0A1S4NYE3"}]},{"type":"Region","location":{"start":{"value":1343,"modifier":"EXACT"},"end":{"value":1528,"modifier":"EXACT"}},"description":"YP domain","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q3YL96"}]},{"type":"Region","location":{"start":{"value":1529,"modifier":"EXACT"},"end":{"value":1751,"modifier":"EXACT"}},"description":"Periplasmic FHA-1 repeat (pFR)","evidences":[{"evidenceCode":"ECO:0000305"}]},{"type":"Region","location":{"start":{"value":1759,"modifier":"EXACT"},"end":{"value":1787,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":1762,"modifier":"EXACT"},"end":{"value":2314,"modifier":"EXACT"}},"description":"FHA-2","evidences":[{"evidenceCode":"ECO:0000305"}]},{"type":"Region","location":{"start":{"value":1992,"modifier":"EXACT"},"end":{"value":2012,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":2694,"modifier":"EXACT"},"end":{"value":2963,"modifier":"EXACT"}},"description":"C-terminal effector domain (CT)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29923643"}]},{"type":"Motif","location":{"start":{"value":2694,"modifier":"EXACT"},"end":{"value":2697,"modifier":"EXACT"}},"description":"VEDN CT cleavage motif","evidences":[{"evidenceCode":"ECO:0000305"}]},{"type":"Compositional bias","location":{"start":{"value":1759,"modifier":"EXACT"},"end":{"value":1770,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1771,"modifier":"EXACT"},"end":{"value":1782,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"id":"KW-0255","category":"Molecular function","name":"Endonuclease"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-0540","category":"Molecular function","name":"Nuclease"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"id":"KW-0964","category":"Cellular component","name":"Secreted"},{"id":"KW-0732","category":"Domain","name":"Signal"},{"id":"KW-1266","category":"Cellular component","name":"Target cell cytoplasm"},{"id":"KW-0800","category":"Molecular function","name":"Toxin"},{"id":"KW-0843","category":"Biological process","name":"Virulence"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-FNJS4S8KFCVHS","citationType":"submission","authors":["Read T.D.","Akmal A.","Bishop-Lilly K.","Chen P.E.","Cook C.","Kiley M.P.","Lentz S.","Mateczun A.","Nagarajan N.","Nolan N.","Osborne B.I.","Pop M.","Sozhamannan S.","Stewart A.C.","Sulakvelidze A.","Thomason B.","Willner K.","Zwick M.E."],"title":"Annotation of the Yersinia mollaretii ATCC 43969 genome.","publicationDate":"DEC-2008","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 43969 / DSM 18520 / CIP 103324 / CNY 7263 / WAIP 204","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"29923643","citationType":"journal article","authors":["Michalska K.","Quan Nhan D.","Willett J.L.E.","Stols L.M.","Eschenfeldt W.H.","Jones A.M.","Nguyen J.Y.","Koskiniemi S.","Low D.A.","Goulding C.W.","Joachimiak A.","Hayes C.S."],"citationCrossReferences":[{"database":"PubMed","id":"29923643"},{"database":"DOI","id":"10.1111/mmi.14007"}],"title":"Functional plasticity of antibacterial EndoU toxins.","publicationDate":"2018","journal":"Mol. 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