TOXN_BACTK
ID TOXN_BACTK Reviewed; 194 AA.
AC Q3YN09;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 30.
DE RecName: Full=Endoribonuclease ToxN {ECO:0000303|PubMed:23267117};
DE EC=3.1.-.-;
DE AltName: Full=Toxin ToxN {ECO:0000303|PubMed:19124776};
GN Name=toxN {ECO:0000303|PubMed:19124776}; ORFNames=pAW63_066;
OS Bacillus thuringiensis subsp. kurstaki.
OG Plasmid pAW63.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=29339;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35866 / NRRL B-4488 / HD-73; PLASMID=pAW63;
RX PubMed=16042811; DOI=10.1186/1471-2164-6-103;
RA Van der Auwera G.A., Andrup L., Mahillon J.;
RT "Conjugative plasmid pAW63 brings new insights into the genesis of the
RT Bacillus anthracis virulence plasmid pXO2 and of the Bacillus thuringiensis
RT plasmid pBT9727.";
RL BMC Genomics 6:103-103(2005).
RN [2]
RP FUNCTION, AND EXPRESSION IN E.COLI.
RC STRAIN=ATCC 35866 / NRRL B-4488 / HD-73; PLASMID=pAW63;
RX PubMed=19124776; DOI=10.1073/pnas.0808832106;
RA Fineran P.C., Blower T.R., Foulds I.J., Humphreys D.P., Lilley K.S.,
RA Salmond G.P.;
RT "The phage abortive infection system, ToxIN, functions as a protein-RNA
RT toxin-antitoxin pair.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:894-899(2009).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH ANTITOXIN TOXI,
RP FUNCTION, SUBUNIT, MUTAGENESIS OF PHE-29; LYS-31; SER-57; ARG-58; TYR-110
RP AND LYS-148, AND RNA-BINDING.
RC STRAIN=ATCC 35866 / NRRL B-4488 / HD-73; PLASMID=pAW63;
RX PubMed=23267117; DOI=10.1073/pnas.1216039110;
RA Short F.L., Pei X.Y., Blower T.R., Ong S.L., Fineran P.C., Luisi B.F.,
RA Salmond G.P.;
RT "Selectivity and self-assembly in the control of a bacterial toxin by an
RT antitoxic noncoding RNA pseudoknot.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:E241-E249(2013).
CC -!- FUNCTION: Toxic component of a type III toxin-antitoxin (TA) system
CC (PubMed:19124776). An endoribonuclease which cleaves between the first
CC and second A of AAAAA sequences; it tolerates other nucleotides in
CC positions +2 and +4 of the consensus. Digests cognate antitoxin RNA
CC ToxI as shown by the 2'-3'-cyclic phosphate at the 3' end of the 34-nt
CC repeats and probably other RNAs (PubMed:23267117). Inhibits growth when
CC expressed in E.coli without causing cell lysis; this bacteriostatic
CC effect is neutralized by cognate RNA antitoxin ToxI, which has 2.9
CC nearly identical 34 nucleotide-long repeats (PubMed:19124776). Non-
CC cognate antitoxin RNA from P.atrosepticum does not inhibit this toxin
CC (PubMed:23267117). The toxin-antitoxin pair function in plasmid
CC maintenance (a plasmid addiction system), but unlike its P.atrosepticum
CC homolog it is not seen to confer resistance to bacteriophages
CC (PubMed:23267117). {ECO:0000269|PubMed:19124776,
CC ECO:0000269|PubMed:23267117}.
CC -!- SUBUNIT: One ToxN monomer binds to a 34-nt-long single repeat of the
CC ToxI RNA; this complex forms a triangular heterohexameric complex with
CC ToxN connected by the ToxI RNA to another toxin molecule. The ToxI
CC repeats are cleavage products of their precursor. The ToxI repeat forms
CC a pseudoknot which occludes the toxin active site.
CC {ECO:0000269|PubMed:23267117}.
CC -!- MISCELLANEOUS: Encoded on a conjugative plasmid that includes genes for
CC a type IV secretion system. {ECO:0000303|PubMed:16042811}.
CC -!- SIMILARITY: Belongs to the ToxN/AbiQ toxin family. {ECO:0000305}.
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DR EMBL; DQ025752; AAZ06636.1; -; Genomic_DNA.
DR RefSeq; WP_000182254.1; NZ_PHSM01000020.1.
DR PDB; 4ATO; X-ray; 2.20 A; A=1-194.
DR PDBsum; 4ATO; -.
DR AlphaFoldDB; Q3YN09; -.
DR SMR; Q3YN09; -.
DR PRIDE; Q3YN09; -.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0006276; P:plasmid maintenance; IMP:UniProtKB.
DR InterPro; IPR025911; ToxN/AbiQ_toxin.
DR Pfam; PF13958; ToxN_toxin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Endonuclease; Hydrolase; Nuclease; Plasmid;
KW RNA-binding; Toxin-antitoxin system.
FT CHAIN 1..194
FT /note="Endoribonuclease ToxN"
FT /id="PRO_0000432893"
FT REGION 171..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 114..182
FT /evidence="ECO:0000255"
FT MUTAGEN 29
FT /note="F->A: Overexpression no longer inhibits growth in
FT E.coli."
FT /evidence="ECO:0000269|PubMed:23267117"
FT MUTAGEN 31
FT /note="K->A: Overexpression no longer inhibits growth in
FT E.coli."
FT /evidence="ECO:0000269|PubMed:23267117"
FT MUTAGEN 57
FT /note="S->A: Overexpression no longer inhibits growth in
FT E.coli."
FT /evidence="ECO:0000269|PubMed:23267117"
FT MUTAGEN 58
FT /note="R->A: Overexpression no longer inhibits growth in
FT E.coli."
FT /evidence="ECO:0000269|PubMed:23267117"
FT MUTAGEN 110
FT /note="Y->A: Overexpression no longer inhibits growth in
FT E.coli."
FT /evidence="ECO:0000269|PubMed:23267117"
FT MUTAGEN 148
FT /note="K->A: Overexpression no longer inhibits growth in
FT E.coli."
FT /evidence="ECO:0000269|PubMed:23267117"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:4ATO"
FT HELIX 14..23
FT /evidence="ECO:0007829|PDB:4ATO"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:4ATO"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:4ATO"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:4ATO"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:4ATO"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:4ATO"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:4ATO"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:4ATO"
FT HELIX 100..106
FT /evidence="ECO:0007829|PDB:4ATO"
FT HELIX 108..139
FT /evidence="ECO:0007829|PDB:4ATO"
FT HELIX 147..155
FT /evidence="ECO:0007829|PDB:4ATO"
FT HELIX 159..169
FT /evidence="ECO:0007829|PDB:4ATO"
SQ SEQUENCE 194 AA; 22887 MW; A3A9E8E4823FB598 CRC64;
MTNKDNPKFH TISTEYIDYL READSKVPFN KDEQHSRPYV GVLEKINGHD YFVPLTSRND
KNFNSQVSVK LFDNDEKRIG VLLVNNMIPV PEKECKEIDI AEKTAADPQY GNLMLKQYLF
LKENMDRVTN KVEKVYKDVT VQGKPSHKQK FLKGVCCDFP KLEEKCQEYK ERDQAKERDK
ARRIAYMRQM GRER
