ID   TOX1_BACCR              Reviewed;         545 AA.
AC   Q813X6;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Toxin BC_0920 {ECO:0000303|PubMed:22200572};
DE   AltName: Full=Ribonuclease BC_0920;
DE            Short=RNase BC_0920 {ECO:0000303|PubMed:22200572};
DE            EC=3.1.-.-;
GN   OrderedLocusNames=BC_0920;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
RN   [2]
RP   FUNCTION AS AN RNASE, PROBABLE FUNCTION AS A TOXIN, AND EXPRESSION IN
RP   E.COLI.
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=22200572; DOI=10.1016/j.febslet.2011.12.020;
RA   Holberger L.E., Garza-Sanchez F., Lamoureux J., Low D.A., Hayes C.S.;
RT   "A novel family of toxin/antitoxin proteins in Bacillus species.";
RL   FEBS Lett. 586:132-136(2012).
RN   [3]
RP   FUNCTION.
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=29923643; DOI=10.1111/mmi.14007;
RA   Michalska K., Quan Nhan D., Willett J.L.E., Stols L.M., Eschenfeldt W.H.,
RA   Jones A.M., Nguyen J.Y., Koskiniemi S., Low D.A., Goulding C.W.,
RA   Joachimiak A., Hayes C.S.;
RT   "Functional plasticity of antibacterial EndoU toxins.";
RL   Mol. Microbiol. 109:509-527(2018).
CC   -!- FUNCTION: Toxic component of an LXG toxin-immunity module. The C-
CC       terminus (residues 322-545) has RNase activity in E.coli which is
CC       neutralized by cognate immunity protein BC_0921, but not by immunity
CC       proteins specific to other toxins with the LXG domain
CC       (PubMed:22200572). Degrades 5S rRNA and several tRNAs in vitro;
CC       cleavage is endonucleolytic within the anticodon loop for tRNA(GAU-Ile)
CC       and tRNA(UUC-Glu) but total for 5S rRNA and at least one other tRNA.
CC       RNase activity is suppressed by cognate immunity protein BC_0921
CC       (PubMed:29923643). {ECO:0000269|PubMed:22200572,
CC       ECO:0000269|PubMed:29923643}.
CC   -!- SUBUNIT: Probably interacts with cognate immunity protein BC_0921. The
CC       interaction inhibits the toxic activity of BC_0921 (Probable).
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Note=Delivery to target
CC       cells requires a type VII secretion system (T7SS). {ECO:0000305}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the LXG family.
CC       {ECO:0000303|PubMed:22200572}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the bacterial EndoU
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE016877; AAP07907.1; -; Genomic_DNA.
DR   RefSeq; NP_830706.1; NC_004722.1.
DR   RefSeq; WP_000056051.1; NZ_CP034551.1.
DR   AlphaFoldDB; Q813X6; -.
DR   PRIDE; Q813X6; -.
DR   EnsemblBacteria; AAP07907; AAP07907; BC_0920.
DR   KEGG; bce:BC0920; -.
DR   PATRIC; fig|226900.8.peg.868; -.
DR   HOGENOM; CLU_031023_2_0_9; -.
DR   OMA; EGEINWR; -.
DR   Proteomes; UP000001417; Chromosome.
DR   GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR   InterPro; IPR029501; EndoU_bac.
DR   InterPro; IPR006829; LXG_dom.
DR   Pfam; PF14436; EndoU_bacteria; 1.
DR   Pfam; PF04740; LXG; 1.
DR   PROSITE; PS51756; LXG; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Nuclease; Reference proteome; Secreted; Toxin.
FT   CHAIN           1..545
FT                   /note="Toxin BC_0920"
FT                   /id="PRO_0000424068"
FT   DOMAIN          1..217
FT                   /note="LXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01092"
SQ   SEQUENCE   545 AA;  59954 MW;  177452C51A0E14CD CRC64;
     MSLNMYLGEV QGQTQSMNAV CNATIQGMEQ VIQSIDAFAI DTVLQGQTYS SAKSFFVQTF
     RPLAQGIIYL CEELIRQNDA FPSQFQSQVA STDVIEQEIL EQIREIDRMK ASMEAISQAM
     PIPGMDAMAN LFTVMRKKLQ EKLDHLYQFN QTSSNNYSTA LQLAASIAAG LAEVQSGKGF
     SPASGTFSTQ GLNMEWTTSI QAITEERARQ AANSIEEGEM CGKLPEKSTG EKIWDGIVEG
     TGQAVSDTID GIKALGDWET WENMGNAALH PIDTLSTMYN TLSDSFINDV INGDAESRAK
     WGSYALTQVG LGLIGDKGLS KASKLGQAGK VTKLAKNKIP QAVSHITSNL QMGDRFAFAG
     GNSLRFRFDT PDFKKAEEKL STYQFARGES NYGGSNFVNE NHRSSLSNRE IISNLQHTEK
     FRPNTLKHIL EGEINWRGDA MGYHTEVLEN TPGKIISGTE EILNDQGIYK ARVEVNGTPK
     TGNRGFSTFF PKDWSPQKIV DNINEAYNNR TYEFGNTYSG IGSEGIRISM YIDGNGKIIS
     AFPAE