ID   SYME_SALPA              Reviewed;         110 AA.
AC   Q5PIF2;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 2.
DT   25-MAY-2022, entry version 73.
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=SPA4344;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAV80070.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000026; AAV80070.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001520547.1; NC_006511.1.
DR   AlphaFoldDB; Q5PIF2; -.
DR   EnsemblBacteria; AAV80070; AAV80070; SPA4344.
DR   KEGG; spt:SPA4344; -.
DR   HOGENOM; CLU_151239_0_0_6; -.
DR   Proteomes; UP000008185; 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..110
FT                   /note="Endoribonuclease SymE"
FT                   /id="PRO_0000297824"
FT   DOMAIN          29..74
FT                   /note="SpoVT-AbrB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01076"
SQ   SEQUENCE   110 AA;  12154 MW;  9185B7F409CBA840 CRC64;
     MTTVHSIADP CDPEVSPTNN RHLTVSYASR YPDYTRIPAL TMKGQWLEAA GFATGTEVDV
     RVMNGCIVLT AQQPQPEESE LMQSLRQVSK LSARKQKQVQ AFIDVMAGSK