Rv3853 Ribonuclease E inhibitor RraA

Summary
Symbol Product Feature Type Start End Strand Length AA Length is TF
Rv3853 menG Ribonuclease E inhibitor RraA CDS 4325495 4325968 + 474 157 FALSE

Rv3853 (Ribonuclease E inhibitor RraA) is predicted to be co-regulated in modules bicluster_0281 with residual 0.48 and bicluster_0585 with residual 0.58.

This regulation is possibly mediated by two de-novo identified cis-regulatory motifs in each module with e-values , 140.00 and 1,200.00 for bicluster_0281 and 0.06 and 350.00 for bicluster_0585 respectively.

These modules are enriched for following go terms: acetate-CoA ligase activity cofactor biosynthetic process, coenzyme metabolic process, cofactor metabolic process.

This gene is found to be for growth on cholesterol.

Mutant available?:

Displaying 1 - 1 of 1
Gene Target Differential Expression Distance Expression pvalue Type
No results were found
Displaying 1 - 1 of 1
ChipSeq TF Differential Expression Distance Expression pvalue Type
Transcriptional regulator, AsnC family
No -133 0.11 0.923482 CDS
Motif 1 Motif 2 Residual
bicluster_0281
e.value: 
140
Motif Bicluster: 
e.value: 
1200
Motif Bicluster: 
0.48
bicluster_0585
e.value: 
0.055
Motif Bicluster: 
e.value: 
350
Motif Bicluster: 
0.58
Product (LegacyBRC) Product (RefSeq)
Regulator of ribonuclease activity A ribonuclease activity regulator protein RraA
Operon # Operon
2521 -
PATRIC Locus Tag Enzyme Name PATRIC Pathways Transcriptomics

PATRIC

Not assigned Not assigned
Locus Tuberculist Genome View

Tuberculist

Quickview
Locus Tag KEGG Pathways

KEGG

not assigned to any KEGG Pathway.
BioCyc Gene Page Cellular Overview Map
Link to STRING STRING Network

STRING

GI Number Protein ID Blast Conserved Domains
15610989 NP_218370.1 Run
GO:0070207

protein homotrimerization

protein homotrimerization

Details: 
The formation of a protein homotrimer, a macromolecular structure consisting of three noncovalently associated identical subunits.
GO Category: 
biological_process
6
Total items in this category:  
GO:0008757

S-adenosylmethionine-dependent methyltransferase activity

S-adenosylmethionine-dependent methyltransferase activity

Details: 
Catalysis of the transfer of a methyl group from S-adenosyl-L-methionine to a substrate.
GO Category: 
molecular_function
3
Total items in this category:  
Description:Expression data from transcription factor over expression experiments. TFOE are matched to the ChIP-seq experiment done simultaneously. This dataset is described in Rustad et al. 2014, Genome Biology.
Quantitative Proteomics Data
t-test p-value Cholesterol/Glycerol Ratio
0.390000 0.90

How essentiality calculations were done?

The relative representation of each mutant was determined by calculating the fold change (sequence reads/insertion in cholesterol divided by sequence reads/insertion in glycerol) for each gene. Statistical significance was determined by t-test. Each insertion site in each replicate sample was treated as a separate data point. The hyperbola used for defining genes specifically required for growth in cholesterol was defined by the formula, y = 3.8/x+0.7. Genes above this line are annotated as required for growth on cholesterol.

TRIP log2 fold abundance change

reports the log2 abundance fold change of each TFI strain, relative to no induction, in absence or presence of drug, averaged across experimental replicates. Also reported are the accompanying z-scores and two-sided t-test p-values for each TFI strain under each condition. Please refer to Ma et al., 2020, Nature Microbiology for more information.

p-value Untreated:
p-value INH: