| Tag | Content |
|---|
| CPLM ID | CPLM-008475 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | mRNA endoribonuclease LS |
Protein Synonyms/Alias | RNase LS; Toxin LS |
Gene Name | rnlA |
Gene Synonyms/Alias | std; yfjN; b2630; JW2611 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 7 | *MTIRSYKNLNLVRA | acetylation | [1] | | 284 | GFGTYFDKPAAHYIL | acetylation | [1] |
|
Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | Toxic component of a toxin-antitoxin (TA) module. A stable (half-life 27.6 minutes) endoribonuclease that in the absence of cognate antitoxin RnlB causes generalized RNA degradation. Degrades late enterobacteria phage T4 mRNAs, protecting the host against T4 reproduction. Activity is inhibited by cognate antitoxin RnlB and by enterobacteria phage T4 protein Dmd. Targets cyaA mRNA. |
Sequence Annotation | |
Keyword | Complete proteome; Endonuclease; Hydrolase; Nuclease; Reference proteome; Toxin. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 357 AA |
Protein Sequence | MTIRSYKNLN LVRANIETES RQFIENKNYS IQSIGPMPGS RAGLRVVFTR PGVNLATVDI 60
FYNGDGSTTI QYLTGANRSL GQELADHLFE TINPAEFEQV NMVLQGFVET SVLPVLELSA 120
DESHIEFREH SRNAHTVVWK IISTSYQDEL TVSLHITTGK LQIQGRPLSC YRVFTFNLAA 180
LLDLQGLEKV LIRQEDGKAN IVQQEVARTY LQTVMADAYP HLHVTAEKLL VSGLCVKLAA 240
PDLPDYCMLL YPELRTIEGV LKSKMSGLGM PVQQPAGFGT YFDKPAAHYI LKPQFAATLR 300
PEQINIISTA YTFFNVERHS LFHMETVVDA SRMISDMARL MGKATRAWGI IKDLYIV 357 |
Gene Ontology | GO:0004521; F:endoribonuclease activity; IDA:EcoCyc. GO:0006402; P:mRNA catabolic process; IMP:EcoCyc. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |