ID A7MG71_CROS8 Unreviewed; 118 AA.
AC A7MG71;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 28-JAN-2026, entry version 75.
DE RecName: Full=Endoribonuclease SymE {ECO:0000256|HAMAP-Rule:MF_01193};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_01193};
GN Name=symE {ECO:0000256|HAMAP-Rule:MF_01193};
GN OrderedLocusNames=ESA_03423 {ECO:0000313|EMBL:ABU78641.1};
OS Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Enterobacterales; Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=290339 {ECO:0000313|EMBL:ABU78641.1, ECO:0000313|Proteomes:UP000000260};
RN [1] {ECO:0000313|EMBL:ABU78641.1, ECO:0000313|Proteomes:UP000000260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-894 {ECO:0000313|EMBL:ABU78641.1,
RC ECO:0000313|Proteomes:UP000000260};
RX PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA McClelland M., Forsythe S.J.;
RT "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT hybridization analysis with other Cronobacter species.";
RL PLoS ONE 5:E9556-E9556(2010).
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:0000256|HAMAP-Rule:MF_01193}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01193}.
CC -!- SIMILARITY: Belongs to the SymE family. {ECO:0000256|HAMAP-
CC Rule:MF_01193}.
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DR EMBL; CP000783; ABU78641.1; -; Genomic_DNA.
DR RefSeq; WP_012125874.1; NC_009778.1.
DR AlphaFoldDB; A7MG71; -.
DR KEGG; esa:ESA_03423; -.
DR PATRIC; fig|290339.8.peg.3042; -.
DR HOGENOM; CLU_151239_0_0_6; -.
DR Proteomes; UP000000260; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004521; F:RNA endonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016070; P:RNA metabolic process; IEA:InterPro.
DR HAMAP; MF_01193; Endoribonucl_SymE; 1.
DR InterPro; IPR014944; Toxin_SymE-like.
DR InterPro; IPR020883; TypeI_TA_SymE.
DR NCBIfam; NF010128; PRK13605.1; 1.
DR Pfam; PF08845; SymE_toxin; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01193};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Endonuclease {ECO:0000256|HAMAP-Rule:MF_01193};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01193};
KW Nuclease {ECO:0000256|HAMAP-Rule:MF_01193};
KW Reference proteome {ECO:0000313|Proteomes:UP000000260};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01193}.
FT DOMAIN 24..75
FT /note="Toxin SymE-like"
FT /evidence="ECO:0000259|Pfam:PF08845"
SQ SEQUENCE 118 AA; 13057 MW; 1C8658DD89D5FAC1 CRC64;
MSMLSVLPEV LPEALPAPAA LTEPRRIRVS YASRFHDGVS LAALTLRGKW LEEAGFPTGT
DADVRVMPGC IVITARAPEP EDPPLLKSLR RVCKLSVRKQ QQVQEFIEVI AGKRKKRV
//
