ID   LSOA_ECO57              Reviewed;         346 AA.
AC   O82881;
DT   09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=mRNA endoribonuclease LsoA;
DE            EC=3.1.-.-;
DE   AltName: Full=Toxin LsoA;
GN   Name=lsoA;
OS   Escherichia coli O157:H7.
OG   Plasmid pOSAK1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=9628576; DOI=10.1093/dnares/5.1.1;
RA   Makino K., Ishii K., Yasunaga T., Hattori M., Yokoyama K., Yatsudo H.C.,
RA   Kubota Y., Yamaichi Y., Iida T., Yamamoto K., Honda T., Han C.G.,
RA   Ohtsubo A., Kasamatsu M., Hayashi T., Kuhara S., Shinagawa H.;
RT   "Complete nucleotide sequences of 93-kb and 3.3-kb plasmids of an
RT   enterohemorrhagic Escherichia coli O157:H7 derived from Sakai outbreak.";
RL   DNA Res. 5:1-9(1998).
RN   [2]
RP   FUNCTION AS A TOXIN, FUNCTION AS AN MRNA ENDORIBONUCLEASE, INTERACTION WITH
RP   LSOB, AND INTERACTION WITH ENTEROBACTERIA PHAGE T4 ANTITOXIN DMD.
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=22403819; DOI=10.1111/j.1365-2958.2012.07975.x;
RA   Otsuka Y., Yonesaki T.;
RT   "Dmd of bacteriophage T4 functions as an antitoxin against Escherichia coli
RT   LsoA and RnlA toxins.";
RL   Mol. Microbiol. 83:669-681(2012).
CC   -!- FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. A
CC       stable (half-life over 20 minutes) endoribonuclease that degrades mRNA.
CC       Degradation may be translation-stimulated. Overexpression in the
CC       absence of cognate antitoxin LsoB causes retarded growth and mRNA
CC       degradation, this effect is mitigated upon coexpression with antitoxin
CC       LsoB or enterobacteria phage T4 Dmd. Degrades late enterobacteria phage
CC       T4 mRNAs, protecting the host against T4 reproduction.
CC       {ECO:0000269|PubMed:22403819}.
CC   -!- SUBUNIT: Can form a complex with cognate antitoxin LsoB and with
CC       enterobacteria phage T4 antitoxin Dmd.
CC   -!- MISCELLANEOUS: This plasmid is only found in Sakai-derived strains of
CC       E.coli O157.
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DR   EMBL; AB011548; BAA31756.1; -; Genomic_DNA.
DR   RefSeq; NP_052606.1; NC_002127.1.
DR   RefSeq; WP_000068433.1; NZ_RWJR01000070.1.
DR   PDB; 5HY3; X-ray; 3.10 A; A=1-346.
DR   PDBsum; 5HY3; -.
DR   AlphaFoldDB; O82881; -.
DR   SMR; O82881; -.
DR   EnsemblBacteria; BAA31756; BAA31756; BAA31756.
DR   GeneID; 1789663; -.
DR   KEGG; ecs:pOSAK1_03; -.
DR   PATRIC; fig|386585.9.peg.3; -.
DR   HOGENOM; CLU_949108_0_0_6; -.
DR   Proteomes; UP000000558; Plasmid pOSAK1.
DR   GO; GO:0004521; F:endoribonuclease activity; IEA:InterPro.
DR   InterPro; IPR043994; RnlA/LsoA-toxin_DBD.
DR   InterPro; IPR045837; RnlA_toxin_N.
DR   InterPro; IPR031845; RnlA_toxin_NRD.
DR   Pfam; PF19034; RnlA-toxin_DBD; 1.
DR   Pfam; PF15935; RnlA_toxin; 1.
DR   Pfam; PF19417; RnlA_toxin_N; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Endonuclease; Hydrolase; Nuclease; Plasmid;
KW   Reference proteome; Toxin-antitoxin system.
FT   CHAIN           1..346
FT                   /note="mRNA endoribonuclease LsoA"
FT                   /id="PRO_0000420765"
FT   STRAND          92..98
FT                   /evidence="ECO:0007829|PDB:5HY3"
FT   HELIX           103..113
FT                   /evidence="ECO:0007829|PDB:5HY3"
FT   STRAND          117..121
FT                   /evidence="ECO:0007829|PDB:5HY3"
FT   STRAND          125..127
FT                   /evidence="ECO:0007829|PDB:5HY3"
FT   STRAND          131..135
FT                   /evidence="ECO:0007829|PDB:5HY3"
FT   STRAND          152..159
FT                   /evidence="ECO:0007829|PDB:5HY3"
FT   HELIX           160..172
FT                   /evidence="ECO:0007829|PDB:5HY3"
FT   HELIX           175..185
FT                   /evidence="ECO:0007829|PDB:5HY3"
FT   HELIX           192..202
FT                   /evidence="ECO:0007829|PDB:5HY3"
FT   TURN            204..208
FT                   /evidence="ECO:0007829|PDB:5HY3"
FT   HELIX           212..221
FT                   /evidence="ECO:0007829|PDB:5HY3"
FT   HELIX           223..226
FT                   /evidence="ECO:0007829|PDB:5HY3"
FT   HELIX           235..256
FT                   /evidence="ECO:0007829|PDB:5HY3"
FT   HELIX           265..268
FT                   /evidence="ECO:0007829|PDB:5HY3"
FT   STRAND          273..275
FT                   /evidence="ECO:0007829|PDB:5HY3"
FT   HELIX           280..282
FT                   /evidence="ECO:0007829|PDB:5HY3"
FT   TURN            283..285
FT                   /evidence="ECO:0007829|PDB:5HY3"
FT   HELIX           290..309
FT                   /evidence="ECO:0007829|PDB:5HY3"
FT   HELIX           323..343
FT                   /evidence="ECO:0007829|PDB:5HY3"
SQ   SEQUENCE   346 AA;  39574 MW;  F41A98E16FDF7B11 CRC64;
     MAQNPFKALN INIDKIESAL TQNGVTNYSS NVKNERETHI SGTYKGIDFL IKLMPSGGNT
     TIGRASGQNN TYFDEIALII KENCLYSDTK NFEYTIPKFS DDDRANLFEF LSEEGITITE
     DNNNDPNCKH QYIMTTSNGD RVRAKIYKRG SIQFQGKYLQ IASLINDFMC SILNMKEIVE
     QKNKEFNVDI KKETIESELH SKLPKSIDKI HEDIKKQLSC SLIMKKIDVE MEDYSTYCFS
     ALRAIEGFIY QILNDVCNPS SSKNLGEYFT ENKPKYIIRE IHQETINGEI AEVLCECYTY
     WHENRHGLFH MKPGIADTKT INKLESIAII DTVCQLIDGG VARLKL