ID   SYME_ECOL6              Reviewed;         113 AA.
AC   Q8FA88;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Endoribonuclease SymE {ECO:0000255|HAMAP-Rule:MF_01193};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01193};
GN   Name=symE {ECO:0000255|HAMAP-Rule:MF_01193}; OrderedLocusNames=c5422;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Involved in the degradation and recycling of damaged RNA. It
CC       is itself a target for degradation by the ATP-dependent protease Lon.
CC       {ECO:0000255|HAMAP-Rule:MF_01193}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01193}.
CC   -!- SIMILARITY: Belongs to the SymE family. {ECO:0000255|HAMAP-
CC       Rule:MF_01193}.
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DR   EMBL; AE014075; AAN83842.1; -; Genomic_DNA.
DR   PIR; D86133; D86133.
DR   RefSeq; WP_000132630.1; NC_004431.1.
DR   AlphaFoldDB; Q8FA88; -.
DR   STRING; 199310.c5422; -.
DR   EnsemblBacteria; AAN83842; AAN83842; c5422.
DR   KEGG; ecc:c5422; -.
DR   eggNOG; ENOG5031VID; Bacteria.
DR   HOGENOM; CLU_151239_0_0_6; -.
DR   OMA; MRQHTRT; -.
DR   BioCyc; ECOL199310:C5422-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004521; F:endoribonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   HAMAP; MF_01193; Endoribonucl_SymE; 1.
DR   InterPro; IPR007159; SpoVT-AbrB_dom.
DR   InterPro; IPR014944; Toxin_SymE-like.
DR   InterPro; IPR020883; TypeI_TA_SymE.
DR   Pfam; PF08845; SymE_toxin; 1.
DR   PROSITE; PS51740; SPOVT_ABRB; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA-binding; Endonuclease; Hydrolase; Nuclease; RNA-binding.
FT   CHAIN           1..113
FT                   /note="Endoribonuclease SymE"
FT                   /id="PRO_0000297821"
FT   DOMAIN          29..74
FT                   /note="SpoVT-AbrB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01076"
SQ   SEQUENCE   113 AA;  12294 MW;  103D9607059B3CD5 CRC64;
     MTDTHSIAQP FEAEVSPANN RQLTVSYASR YPDYSRIPAI TLKGQWLEAA GFATGTVVDV
     KVMEGCIVLT AQPPAAAESE LMQSLRQVCK LSARKQRQVQ EFIGVIAGKQ KVA