SYME_SHIFL
ID SYME_SHIFL Reviewed; 113 AA.
AC Q83II5;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 95.
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};
GN OrderedLocusNames=SF4363, S4634;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN45779.1; -; Genomic_DNA.
DR EMBL; AE014073; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_710072.1; NC_004337.2.
DR RefSeq; WP_000132640.1; NZ_WPGW01000162.1.
DR AlphaFoldDB; Q83II5; -.
DR SMR; Q83II5; -.
DR STRING; 198214.SF4363; -.
DR EnsemblBacteria; AAN45779; AAN45779; SF4363.
DR GeneID; 1025495; -.
DR GeneID; 58391687; -.
DR KEGG; sfl:SF4363; -.
DR PATRIC; fig|198214.7.peg.5144; -.
DR HOGENOM; CLU_151239_0_0_6; -.
DR OMA; MRQHTRT; -.
DR OrthoDB; 1966690at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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;
KW Reference proteome; RNA-binding.
FT CHAIN 1..113
FT /note="Endoribonuclease SymE"
FT /id="PRO_0000297828"
FT DOMAIN 29..74
FT /note="SpoVT-AbrB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01076"
SQ SEQUENCE 113 AA; 12294 MW; 98166A3B8EB5447E CRC64;
MTDTHSIAQP LEAEVSPANN RQLTVSYASR YPDYSRIPAI TLKGQWLEAA GFATGTAVDV
KVMEGCIVLT AQPAAAEESE LMQSLRKVCK LSARKQRQVQ EFIGVITGKQ KVA