relK
- Type
- protein_coding
- Name
- relK
- Locus Name
-
Rv3358
- Product
-
Toxin RelK
- Functional Category
-
Virulence, detoxification, adaptation
- Location
- 3771045..3771302 (+ strand)
- Gene Length
- 257 bp
- Nucleotides
-
TGAGAAGCGTCAACTTCGATCCCGATGCCTGGGAGGACTTCTTGTTCTGGCTGGCCGCTGATCGCAAAACGGCCCGTCGGATCACCCGGTTGATCGGAGAAATTCAGCGTGATCCGTTCAGCGGGATCGGCAAACCCGAGCCGCTCCAAGGTGAGTTGTCGGGATACTGGTCGCGCCGGATCGACGACGAACACCGGCTGGTGTATCGAGCGGGCGACGACGAAGTCACGATGCTGAAGGCCCGATACCACTACTGA
- Drug Resistance
- Mutations
- Function
- Toxic component of a type II toxin-antitoxin (TA) system. Has RNase activity and preferentially cleaves at the 3'-end of purine ribonucleotides (By similarity). Overexpression in M.tuberculosis or M.smegmatis inhibits colony formation in a bacteriostatic rather than bacteriocidal fashion. Its toxic effect is neutralized by coexpression with antitoxin RelJ (shown only for M.smegmatis). Overexpression also increases the number of rifampcin-tolerant persister cells. {ECO:0000250, ECO:0000269|PubMed:19114484, ECO:0000269|PubMed:20011113, ECO:0000269|PubMed:20061486, ECO:0000269|PubMed:20498855}.; FUNCTION: In combination with RelJ represses its own promoter. Several DNA-protein complexes are formed in vitro depending on the RelJ:RelK ratio.
- Family
-
YoeB family
- GO
-
- transcription corepressor activity GO:0003714 molecular_function
- ribosomal small subunit binding GO:0043024 molecular_function
- endonuclease activity GO:0004519 molecular_function
- RNA catabolic process GO:0006401 biological_process
- endoribonuclease activity, producing 3'-phosphomonoesters GO:0016892 molecular_function
- negative regulation of translational initiation GO:0045947 biological_process
- negative regulation of transcription, DNA-templated GO:0045892 biological_process
- DNA binding GO:0003677 molecular_function
- InterPro
3OEI
- Name
- Toxin RelK (EC 3.1.-.-) (Endoribonuclease YoeB) (Putative mRNA interferase RelE3) (Putative mRNA interferase YoeB) (Toxin YoeB)
- Family
- YoeB family
- Protein Sequence
-
MRSVNFDPDAWEDFLFWLAADRKTARRITRLIGEIQRDPFSGIGKPEPLQGELSGYWSRRIDDEHRLVYRAGDDEVTMLKARYHY
- Mass
- 10,102 Da
- Length
- 85 Aa
Summary
Rv3358 doesn't seem to be a targeted by any drug.
Rv3358 doesn't seem to be involved in any pathway.
- Characterization of the interaction and cross-regulation of three Mycobacterium tuberculosis RelBE modules.
- PLoS One. 2010 May 17;5(5):e10672. doi: 10.1371/journal.pone.0010672.
- The three RelE homologs of Mycobacterium tuberculosis have individual, drug-specific effects on bacterial antibiotic tolerance.
- J Bacteriol. 2010 Mar;192(5):1279-91. doi: 10.1128/JB.01285-09. Epub 2010 Jan 8.
- Comprehensive functional analysis of Mycobacterium tuberculosis toxin-antitoxin systems: implications for pathogenesis, stress responses, and evolution.
- PLoS Genet. 2009 Dec;5(12):e1000767. doi: 10.1371/journal.pgen.1000767. Epub 2009 Dec 11.
- Three Mycobacterium tuberculosis Rel toxin-antitoxin modules inhibit mycobacterial growth and are expressed in infected human macrophages.
- J Bacteriol. 2009 Mar;191(5):1618-30. doi: 10.1128/JB.01318-08. Epub 2008 Dec 29.
- Crystal structure of Mycobacterium tuberculosis YefM antitoxin reveals that it is not an intrinsically unstructured protein.
- J Mol Biol. 2008 Nov 14;383(3):482-93. doi: 10.1016/j.jmb.2008.08.067. Epub 2008 Sep 4.
- Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence.
- Nature. 1998 Jun 11;393(6685):537-44. doi: 10.1038/31159.