TB Genome Annotation Portal

Rv3357 (relJ)

Amino Acid Sequence

MSISASEARQRLFPLIEQVNTDHQPVRITSRAGDAVLMSADDYDAWQETVYLLRSPENARRLMEAVARDKAGHSAFTKSVDELREMAGGEE
(Nucleotide sequence available on KEGG)

Additional Information



ESSENTIALITY

MtbTnDB - interactive tool for exploring a database of published TnSeq datasets for Mtb

TnSeqCorr - genes with correlated TnSeq profiles across >100 conditions *new*

Classification Condition Strain Method Reference Notes
Non-Essential Sodium Oleate H37RvMA Gumbel Subhalaxmi Nambi Probability of Essentiality: 0.000000;
0 non-insertions in a row out of 5 sites
Non-Essential Lignoceric Acid H37RvMA Gumbel Subhalaxmi Nambi Probability of Essentiality: 0.000000;
0 non-insertions in a row out of 5 sites
Non-Essential Phosphatidylcholine H37RvMA Gumbel Subhalaxmi Nambi Probability of Essentiality: 0.000000;
0 non-insertions in a row out of 5 sites
Non-Essential minimal media + 0.1% glycerol H37RvMA Gumbel Griffin et al. (2011) Probability of Essentiality: 0.000000;
0 non-insertions in a row out of 5 sites
Non-Essential minimal media + 0.01% cholesterol H37RvMA Gumbel Griffin et al. (2011) Probability of Essentiality: 0.000000;
0 non-insertions in a row out of 5 sites
Non-Essential 7H10-glycerol H37RvMA TraSH Sassetti et al. (2003a)
Non-Essential C57BL/6J mice (8 weeks) H37RvMA TraSH Sassetti et al. (2003b) Hybridization Ratio: 1.67
Non-Essential 7H09/7H10 + rich media H37RvMA MotifHMM DeJesus et al. (2017) Fully saturated (14 reps).

TnSeq Data No data currently available.
  • No TnSeq data currently available for this Target.
RNASeq Data No data currently available.
  • No RNA-Seq data currently available for this Target.
Metabolomic Profiles No data currently available.
  • No Metabolomic data currently available for this Target.
Proteomic Data No data currently available.
  • No Proteomic data currently available for this Target.

Regulatory Relationships from Systems Biology
  • BioCyc

    Gene interactions based on ChIPSeq and Transcription Factor Over-Expression (TFOE) (Systems Biology)

    NOTE: Green edges represent the connected genes being classified as differentially essential as a result of the middle gene being knocked out. These interactions are inferred based on RNASeq.

    Interactions based on ChIPSeq data

  • Interactions based on ChIPSeq data (Minch et al. 2014)

    Interactions based on TFOE data (Rustad et al. 2014)

    • Upregulates:

      • Does not upregulate other genes.
    • Upregulated by:

    • Downregulates:

      • Does not downregulate other genes.
    • Downregulated by:



    TBCAP

    Tubculosis Community Annotation Project (
    Slayden et al., 2013)

    Rv3357 (relJ)

    PropertyValueCreatorEvidencePMIDComment
    InteractionPhysicalInteraction Rv3358shahanup86IPIAffinity purification (Physical interaction)
    authors,R. Singh,CE. Barry,HI. Boshoff The three RelE homologs of Mycobacterium tuberculosis have individual, drug-specific effects on bacterial antibiotic tolerance. J. Bacteriol. 2010
    InteractionPhysicalInteraction Rv3358vashishtrvIPIAffinity purification (Physical interaction)
    authors,P. Kumar,B. Issac,EJ. Dodson,JP. Turkenburg,SC. Mande Crystal structure of Mycobacterium tuberculosis YefM antitoxin reveals that it is not an intrinsically unstructured protein. J. Mol. Biol. 2008
    InteractionPhysicalInteraction Rv3358vashishtrvIPIAffinity purification (Physical interaction)
    SB. Korch, H. Contreras et al. Three Mycobacterium tuberculosis Rel toxin:antitoxin modules inhibit mycobacterial growth and are expressed in human-infected macrophages. J. Bacteriol. 2008
    InteractionPhysicalInteraction Rv3358vashishtrvIPIAffinity purification (Physical interaction)
    authors,R. Singh,CE. Barry,HI. Boshoff The three RelE homologs of Mycobacterium tuberculosis have individual, drug-specific effects on bacterial antibiotic tolerance. J. Bacteriol. 2010
    CitationThree Mycobacterium tuberculosis Rel toxin:antitoxin modules inhibit mycobacterial growth and are expressed in human-infected macrophages. SB. Korch, H. Contreras et al. J. Bacteriol. 2008vashishtrvIPI19114484Affinity purification (Physical interaction)
    InteractionPhysicalInteraction Rv3358vashishtrvIPIAffinity purification (Physical interaction)
    SB. Korch, H. Contreras et al. Three Mycobacterium tuberculosis Rel toxin:antitoxin modules inhibit mycobacterial growth and are expressed in human-infected macrophages. J. Bacteriol. 2008
    CitationThe three RelE homologs of Mycobacterium tuberculosis have individual, drug-specific effects on bacterial antibiotic tolerance. authors,R. Singh,CE. Barry,HI. Boshoff J. Bacteriol. 2010vashishtrvIPI20061486Affinity purification (Physical interaction)
    InteractionPhysicalInteraction Rv3358vashishtrvIPIAffinity purification (Physical interaction)
    authors,R. Singh,CE. Barry,HI. Boshoff The three RelE homologs of Mycobacterium tuberculosis have individual, drug-specific effects on bacterial antibiotic tolerance. J. Bacteriol. 2010
    InteractionPhysicalInteraction Rv3358shahanup86IPIAffinity purification (Physical interaction)
    authors,P. Kumar,B. Issac,EJ. Dodson,JP. Turkenburg,SC. Mande Crystal structure of Mycobacterium tuberculosis YefM antitoxin reveals that it is not an intrinsically unstructured protein. J. Mol. Biol. 2008
    InteractionPhysicalInteraction Rv3358shahanup86IPIAffinity purification (Physical interaction)
    SB. Korch, H. Contreras et al. Three Mycobacterium tuberculosis Rel toxin:antitoxin modules inhibit mycobacterial growth and are expressed in human-infected macrophages. J. Bacteriol. 2008
    CitationCrystal structure of Mycobacterium tuberculosis YefM antitoxin reveals that it is not an intrinsically unstructured protein. authors,P. Kumar,B. Issac,EJ. Dodson,JP. Turkenburg,SC. Mande J. Mol. Biol. 2008shahanup86IPI18793646Affinity purification (Physical interaction)
    InteractionPhysicalInteraction Rv3358shahanup86IPIAffinity purification (Physical interaction)
    authors,P. Kumar,B. Issac,EJ. Dodson,JP. Turkenburg,SC. Mande Crystal structure of Mycobacterium tuberculosis YefM antitoxin reveals that it is not an intrinsically unstructured protein. J. Mol. Biol. 2008
    CitationThree Mycobacterium tuberculosis Rel toxin:antitoxin modules inhibit mycobacterial growth and are expressed in human-infected macrophages. SB. Korch, H. Contreras et al. J. Bacteriol. 2008shahanup86IPI19114484Affinity purification (Physical interaction)
    InteractionPhysicalInteraction Rv3358shahanup86IPIAffinity purification (Physical interaction)
    SB. Korch, H. Contreras et al. Three Mycobacterium tuberculosis Rel toxin:antitoxin modules inhibit mycobacterial growth and are expressed in human-infected macrophages. J. Bacteriol. 2008
    CitationThe three RelE homologs of Mycobacterium tuberculosis have individual, drug-specific effects on bacterial antibiotic tolerance. authors,R. Singh,CE. Barry,HI. Boshoff J. Bacteriol. 2010shahanup86IPI20061486Affinity purification (Physical interaction)
    InteractionPhysicalInteraction Rv3358shahanup86IPIAffinity purification (Physical interaction)
    authors,R. Singh,CE. Barry,HI. Boshoff The three RelE homologs of Mycobacterium tuberculosis have individual, drug-specific effects on bacterial antibiotic tolerance. J. Bacteriol. 2010
    CitationCrystal structure of Mycobacterium tuberculosis YefM antitoxin reveals that it is not an intrinsically unstructured protein. authors,P. Kumar,B. Issac,EJ. Dodson,JP. Turkenburg,SC. Mande J. Mol. Biol. 2008vashishtrvIPI18793646Affinity purification (Physical interaction)
    InteractionPhysicalInteraction Rv3358vashishtrvIPIAffinity purification (Physical interaction)
    authors,P. Kumar,B. Issac,EJ. Dodson,JP. Turkenburg,SC. Mande Crystal structure of Mycobacterium tuberculosis YefM antitoxin reveals that it is not an intrinsically unstructured protein. J. Mol. Biol. 2008
    SymbolrelJjlewEach pair shows interaction by two-hybrid and GST pulldown. F and B each interact with E, G, K, and itself.
    authors,M. Yang,C. Gao,Y. Wang,H. Zhang,ZG. He Characterization of the interaction and cross-regulation of three Mycobacterium tuberculosis RelBE modules. PLoS ONE 2010
    CitationCharacterization of the interaction and cross-regulation of three Mycobacterium tuberculosis RelBE modules. authors,M. Yang,C. Gao,Y. Wang,H. Zhang,ZG. He PLoS ONE 2010jlew20498855Each pair shows interaction by two-hybrid and GST pulldown. F and B each interact with E, G, K, and itself.
    SymbolrelB3jlewEach toxin individually arrests growth of both M. tuberculosis and E. coli, an effect that is neutralized by coexpression of the cognate antitoxin.
    authors,R. Singh,CE. Barry,HI. Boshoff The three RelE homologs of Mycobacterium tuberculosis have individual, drug-specific effects on bacterial antibiotic tolerance. J. Bacteriol. 2010
    CitationThe three RelE homologs of Mycobacterium tuberculosis have individual, drug-specific effects on bacterial antibiotic tolerance. authors,R. Singh,CE. Barry,HI. Boshoff J. Bacteriol. 2010jlew20061486Each toxin individually arrests growth of both M. tuberculosis and E. coli, an effect that is neutralized by coexpression of the cognate antitoxin.
    SymbolrelJjlewOverexpression of Mtb relE, relG and relK induces growth arrest in Msmeg; reversed by expression of relB, relF and relJ
    SB. Korch, H. Contreras et al. Three Mycobacterium tuberculosis Rel toxin:antitoxin modules inhibit mycobacterial growth and are expressed in human-infected macrophages. J. Bacteriol. 2008
    CitationThree Mycobacterium tuberculosis Rel toxin:antitoxin modules inhibit mycobacterial growth and are expressed in human-infected macrophages. SB. Korch, H. Contreras et al. J. Bacteriol. 2008jlew19114484Overexpression of Mtb relE, relG and relK induces growth arrest in Msmeg; reversed by expression of relB, relF and relJ
    SymbolRelB3jlewWe report the heterologous toxicity of these TA loci in Escherichia coli and show that only a few of the M. tuberculosis-encoded toxins can inhibit E. coli growth and have a killing effect. This killing effect can be suppressed by coexpression of the cognate antitoxin.
    authors,A. Gupta Killing activity and rescue function of genome-wide toxin-antitoxin loci of Mycobacterium tuberculosis. FEMS Microbiol. Lett. 2009
    CitationKilling activity and rescue function of genome-wide toxin-antitoxin loci of Mycobacterium tuberculosis. authors,A. Gupta FEMS Microbiol. Lett. 2009jlew19016878We report the heterologous toxicity of these TA loci in Escherichia coli and show that only a few of the M. tuberculosis-encoded toxins can inhibit E. coli growth and have a killing effect. This killing effect can be suppressed by coexpression of the cognate antitoxin.
    SymbolyefMjlewStructure
    authors,P. Kumar,B. Issac,EJ. Dodson,JP. Turkenburg,SC. Mande Crystal structure of Mycobacterium tuberculosis YefM antitoxin reveals that it is not an intrinsically unstructured protein. J. Mol. Biol. 2008
    CitationCrystal structure of Mycobacterium tuberculosis YefM antitoxin reveals that it is not an intrinsically unstructured protein. authors,P. Kumar,B. Issac,EJ. Dodson,JP. Turkenburg,SC. Mande J. Mol. Biol. 2008jlew18793646Structure
    Otherstrand:+rslaydenB2017 from Escherichia coli strain K12 (83 aa), FASTA scores: opt: 215, E(): 1.6e-08, (50.0% identity in 72 aa overlap); BAB58570
    Symbolrel BE-3rslaydenSAV2408 from Staphylococcus aureus subsp. aureus Mu50 (83 aa), FASTA scores: opt: 161, E(): 8.8e-05, (39.95% identity in 77 aa overlap); Q9Z5W8 PUTATIVE PHD PROTEIN from Francisella novicid (85 aa), FASTA scores: opt: 143, E(): 0.0016, (28.9% identity in 83 aa overlap); etc. Also similar to Rv1247c
    Otherstart:3770773rslaydenSAV2408 from Staphylococcus aureus subsp. aureus Mu50 (83 aa), FASTA scores: opt: 161, E(): 8.8e-05, (39.95% identity in 77 aa overlap); Q9Z5W8 PUTATIVE PHD PROTEIN from Francisella novicid (85 aa), FASTA scores: opt: 143, E(): 0.0016, (28.9% identity in 83 aa overlap); etc. Also similar to Rv1247c
    Otherstop:3771048rslaydenSAV2408 from Staphylococcus aureus subsp. aureus Mu50 (83 aa), FASTA scores: opt: 161, E(): 8.8e-05, (39.95% identity in 77 aa overlap); Q9Z5W8 PUTATIVE PHD PROTEIN from Francisella novicid (85 aa), FASTA scores: opt: 143, E(): 0.0016, (28.9% identity in 83 aa overlap); etc. Also similar to Rv1247c
    Otherstrand:+rslaydenSAV2408 from Staphylococcus aureus subsp. aureus Mu50 (83 aa), FASTA scores: opt: 161, E(): 8.8e-05, (39.95% identity in 77 aa overlap); Q9Z5W8 PUTATIVE PHD PROTEIN from Francisella novicid (85 aa), FASTA scores: opt: 143, E(): 0.0016, (28.9% identity in 83 aa overlap); etc. Also similar to Rv1247c
    Symbolrel BE-3rslaydenMTV006.19c (89 aa) (36.9% identity in 84 aa overlap). SEEMS TO BELONG TO THE PHD/YEFM FAMILY.
    Otherstart:3770773rslaydenMTV006.19c (89 aa) (36.9% identity in 84 aa overlap). SEEMS TO BELONG TO THE PHD/YEFM FAMILY.
    Otherstop:3771048rslaydenMTV006.19c (89 aa) (36.9% identity in 84 aa overlap). SEEMS TO BELONG TO THE PHD/YEFM FAMILY.
    Otherstrand:+rslaydenMTV006.19c (89 aa) (36.9% identity in 84 aa overlap). SEEMS TO BELONG TO THE PHD/YEFM FAMILY.
    Symbolrel BE-3rslaydenConserved hypothetical protein, highly similar to other hypothetical proteins e.g. Q9Z4V7
    Otherstart:3770773rslaydenConserved hypothetical protein, highly similar to other hypothetical proteins e.g. Q9Z4V7
    Otherstop:3771048rslaydenConserved hypothetical protein, highly similar to other hypothetical proteins e.g. Q9Z4V7
    Otherstrand:+rslaydenConserved hypothetical protein, highly similar to other hypothetical proteins e.g. Q9Z4V7
    Symbolrel BE-3rslaydenYU1E_STRCO (alias CAC37261
    Otherstart:3770773rslaydenYU1E_STRCO (alias CAC37261
    Otherstop:3771048rslaydenYU1E_STRCO (alias CAC37261
    Otherstrand:+rslaydenYU1E_STRCO (alias CAC37261
    Symbolrel BE-3rslaydenSCBAC17D6.02) ORFU1E (BELONGS TO THE PHD/YEFM FAMILY) from Streptomyces coelicolor (87 aa), FASTA scores: opt: 344, E(): 1.9e-17, (62.05% identity in 87 aa overlap); P46147
    Otherstart:3770773rslaydenSCBAC17D6.02) ORFU1E (BELONGS TO THE PHD/YEFM FAMILY) from Streptomyces coelicolor (87 aa), FASTA scores: opt: 344, E(): 1.9e-17, (62.05% identity in 87 aa overlap); P46147
    Otherstop:3771048rslaydenSCBAC17D6.02) ORFU1E (BELONGS TO THE PHD/YEFM FAMILY) from Streptomyces coelicolor (87 aa), FASTA scores: opt: 344, E(): 1.9e-17, (62.05% identity in 87 aa overlap); P46147
    Otherstrand:+rslaydenSCBAC17D6.02) ORFU1E (BELONGS TO THE PHD/YEFM FAMILY) from Streptomyces coelicolor (87 aa), FASTA scores: opt: 344, E(): 1.9e-17, (62.05% identity in 87 aa overlap); P46147
    Symbolrel BE-3rslaydenYEFM_ECOLI
    Otherstart:3770773rslaydenYEFM_ECOLI
    Otherstop:3771048rslaydenYEFM_ECOLI
    Otherstrand:+rslaydenYEFM_ECOLI
    Symbolrel BE-3rslaydenB2017 from Escherichia coli strain K12 (83 aa), FASTA scores: opt: 215, E(): 1.6e-08, (50.0% identity in 72 aa overlap); BAB58570
    Otherstart:3770773rslaydenB2017 from Escherichia coli strain K12 (83 aa), FASTA scores: opt: 215, E(): 1.6e-08, (50.0% identity in 72 aa overlap); BAB58570
    Otherstop:3771048rslaydenB2017 from Escherichia coli strain K12 (83 aa), FASTA scores: opt: 215, E(): 1.6e-08, (50.0% identity in 72 aa overlap); BAB58570

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