Rv0626 - conserved hypothetical protein


Protein Domains

Gene Information
LocusRv0626
Symbol
Gene Nameconserved hypothetical protein
Location718025 - 718285 (+)
SpeciesMycobacterium tuberculosis H37Rv complete genome.
LengthGene:261 bp
Protein:87 aa
External LinksTuberculist
Target Gene Information
String Protein-Protein Interactions
STITCH Chemical-Protein Interactions
Search Google Scholar
Orthologs
Orthogroup Number8441
Related GenesMAP2028c MT0654
Transcriptional Regulation
Operons View gene in operon browser
Regulatory Network
Search for regulators of Rv0626
Expression Correlation Genes with Correlated Expression
Scatterplot of Gene Expression

Sequence
Proteins
Genomic Sequence
Community Annotations Pending Curatorial Review
FieldValueStatusCreatorDate
InteractionInhibits Rv0627activeharsharohiratruefriend2012-10-05
Operon(Physical Interaction)
authors,J. Robson,JL. McKenzie,R. Cursons,GM. Cook,VL. Arcus The vapBC operon from Mycobacterium smegmatis is an autoregulated toxin-antitoxin module that controls growth via inhibition of translation. J. Mol. Biol. 2009
InteractionInhibits Rv0627activeharsharohiratruefriend2012-10-05
Operon(Physical Interaction)
authors,HR. Ramage,LE. Connolly,JS. Cox Comprehensive functional analysis of Mycobacterium tuberculosis toxin-antitoxin systems: implications for pathogenesis, stress responses, and evolution. PLoS Genet. 2009
InteractionInhibits Rv0627activeharsharohiratruefriend2012-10-05
Operon(Physical Interaction)
authors,A. Gupta Killing activity and rescue function of genome-wide toxin-antitoxin loci of Mycobacterium tuberculosis. FEMS Microbiol. Lett. 2009
InteractionInhibits Rv0627activeharsharohiratruefriend2012-10-05
Operon(Physical Interaction)
authors,L. Miallau,M. Faller,J. Chiang,M. Arbing,F. Guo,D. Cascio,D. Eisenberg Structure and proposed activity of a member of the VapBC family of toxin-antitoxin systems. VapBC-5 from Mycobacterium tuberculosis. J. Biol. Chem. 2009
InteractionInhibits Rv0627activeharsharohiratruefriend2012-10-05
Operon(Physical Interaction)
authors,J. Robson,JL. McKenzie,R. Cursons,GM. Cook,VL. Arcus The vapBC operon from Mycobacterium smegmatis is an autoregulated toxin-antitoxin module that controls growth via inhibition of translation. J. Mol. Biol. 2009
InteractionInhibits Rv0627activeharsharohiratruefriend2012-10-05
Operon(Physical Interaction)
authors,HR. Ramage,LE. Connolly,JS. Cox Comprehensive functional analysis of Mycobacterium tuberculosis toxin-antitoxin systems: implications for pathogenesis, stress responses, and evolution. PLoS Genet. 2009
InteractionInhibits Rv0627activeharsharohiratruefriend2012-10-05
Operon(Physical Interaction)
authors,A. Gupta Killing activity and rescue function of genome-wide toxin-antitoxin loci of Mycobacterium tuberculosis. FEMS Microbiol. Lett. 2009
InteractionInhibits Rv0627activeharsharohiratruefriend2012-10-05
Operon(Physical Interaction)
authors,L. Miallau,M. Faller,J. Chiang,M. Arbing,F. Guo,D. Cascio,D. Eisenberg Structure and proposed activity of a member of the VapBC family of toxin-antitoxin systems. VapBC-5 from Mycobacterium tuberculosis. J. Biol. Chem. 2009
InteractionInhibits Rv0627activeharsharohiratruefriend2012-10-05
Co-expression (Functional linkage)
authors,J. Robson,JL. McKenzie,R. Cursons,GM. Cook,VL. Arcus The vapBC operon from Mycobacterium smegmatis is an autoregulated toxin-antitoxin module that controls growth via inhibition of translation. J. Mol. Biol. 2009
InteractionInhibits Rv0627activeharsharohiratruefriend2012-10-05
Co-expression (Functional linkage)
authors,HR. Ramage,LE. Connolly,JS. Cox Comprehensive functional analysis of Mycobacterium tuberculosis toxin-antitoxin systems: implications for pathogenesis, stress responses, and evolution. PLoS Genet. 2009
InteractionInhibits Rv0627activeharsharohiratruefriend2012-10-05
Co-expression (Functional linkage)
authors,A. Gupta Killing activity and rescue function of genome-wide toxin-antitoxin loci of Mycobacterium tuberculosis. FEMS Microbiol. Lett. 2009
InteractionInhibits Rv0627activeharsharohiratruefriend2012-10-05
Co-expression (Functional linkage)
authors,L. Miallau,M. Faller,J. Chiang,M. Arbing,F. Guo,D. Cascio,D. Eisenberg Structure and proposed activity of a member of the VapBC family of toxin-antitoxin systems. VapBC-5 from Mycobacterium tuberculosis. J. Biol. Chem. 2009
InteractionInhibits Rv0627activeharsharohiratruefriend2012-10-05
Co-expression (Functional linkage)
authors,J. Robson,JL. McKenzie,R. Cursons,GM. Cook,VL. Arcus The vapBC operon from Mycobacterium smegmatis is an autoregulated toxin-antitoxin module that controls growth via inhibition of translation. J. Mol. Biol. 2009
InteractionInhibits Rv0627activeharsharohiratruefriend2012-10-05
Co-expression (Functional linkage)
authors,HR. Ramage,LE. Connolly,JS. Cox Comprehensive functional analysis of Mycobacterium tuberculosis toxin-antitoxin systems: implications for pathogenesis, stress responses, and evolution. PLoS Genet. 2009
InteractionInhibits Rv0627activeharsharohiratruefriend2012-10-05
Co-expression (Functional linkage)
authors,A. Gupta Killing activity and rescue function of genome-wide toxin-antitoxin loci of Mycobacterium tuberculosis. FEMS Microbiol. Lett. 2009
InteractionInhibits Rv0627activeharsharohiratruefriend2012-10-05
Co-expression (Functional linkage)
authors,L. Miallau,M. Faller,J. Chiang,M. Arbing,F. Guo,D. Cascio,D. Eisenberg Structure and proposed activity of a member of the VapBC family of toxin-antitoxin systems. VapBC-5 from Mycobacterium tuberculosis. J. Biol. Chem. 2009
InteractionInhibits Rv0627activeharsharohiratruefriend2012-10-05
Operon(Physical Interaction)
authors,J. Robson,JL. McKenzie,R. Cursons,GM. Cook,VL. Arcus The vapBC operon from Mycobacterium smegmatis is an autoregulated toxin-antitoxin module that controls growth via inhibition of translation. J. Mol. Biol. 2009
InteractionInhibits Rv0627activeharsharohiratruefriend2012-10-05
Operon(Physical Interaction)
authors,HR. Ramage,LE. Connolly,JS. Cox Comprehensive functional analysis of Mycobacterium tuberculosis toxin-antitoxin systems: implications for pathogenesis, stress responses, and evolution. PLoS Genet. 2009
InteractionInhibits Rv0627activeharsharohiratruefriend2012-10-05
Operon(Physical Interaction)
authors,A. Gupta Killing activity and rescue function of genome-wide toxin-antitoxin loci of Mycobacterium tuberculosis. FEMS Microbiol. Lett. 2009
InteractionInhibits Rv0627activeharsharohiratruefriend2012-10-05
Operon(Physical Interaction)
authors,L. Miallau,M. Faller,J. Chiang,M. Arbing,F. Guo,D. Cascio,D. Eisenberg Structure and proposed activity of a member of the VapBC family of toxin-antitoxin systems. VapBC-5 from Mycobacterium tuberculosis. J. Biol. Chem. 2009
InteractionInhibits Rv0627activeharsharohiratruefriend2012-10-05
Operon(Physical Interaction)
authors,J. Robson,JL. McKenzie,R. Cursons,GM. Cook,VL. Arcus The vapBC operon from Mycobacterium smegmatis is an autoregulated toxin-antitoxin module that controls growth via inhibition of translation. J. Mol. Biol. 2009
InteractionInhibits Rv0627activeharsharohiratruefriend2012-10-05
Operon(Physical Interaction)
authors,HR. Ramage,LE. Connolly,JS. Cox Comprehensive functional analysis of Mycobacterium tuberculosis toxin-antitoxin systems: implications for pathogenesis, stress responses, and evolution. PLoS Genet. 2009
InteractionInhibits Rv0627activeharsharohiratruefriend2012-10-05
Operon(Physical Interaction)
authors,A. Gupta Killing activity and rescue function of genome-wide toxin-antitoxin loci of Mycobacterium tuberculosis. FEMS Microbiol. Lett. 2009
InteractionInhibits Rv0627activeharsharohiratruefriend2012-10-05
Operon(Physical Interaction)
authors,L. Miallau,M. Faller,J. Chiang,M. Arbing,F. Guo,D. Cascio,D. Eisenberg Structure and proposed activity of a member of the VapBC family of toxin-antitoxin systems. VapBC-5 from Mycobacterium tuberculosis. J. Biol. Chem. 2009
InteractionInhibits Rv0627activeharsharohiratruefriend2012-10-05
Co-expression (Functional linkage)
authors,J. Robson,JL. McKenzie,R. Cursons,GM. Cook,VL. Arcus The vapBC operon from Mycobacterium smegmatis is an autoregulated toxin-antitoxin module that controls growth via inhibition of translation. J. Mol. Biol. 2009
InteractionInhibits Rv0627activeharsharohiratruefriend2012-10-05
Co-expression (Functional linkage)
authors,HR. Ramage,LE. Connolly,JS. Cox Comprehensive functional analysis of Mycobacterium tuberculosis toxin-antitoxin systems: implications for pathogenesis, stress responses, and evolution. PLoS Genet. 2009
InteractionInhibits Rv0627activeharsharohiratruefriend2012-10-05
Co-expression (Functional linkage)
authors,A. Gupta Killing activity and rescue function of genome-wide toxin-antitoxin loci of Mycobacterium tuberculosis. FEMS Microbiol. Lett. 2009
InteractionInhibits Rv0627activeharsharohiratruefriend2012-10-05
Co-expression (Functional linkage)
authors,L. Miallau,M. Faller,J. Chiang,M. Arbing,F. Guo,D. Cascio,D. Eisenberg Structure and proposed activity of a member of the VapBC family of toxin-antitoxin systems. VapBC-5 from Mycobacterium tuberculosis. J. Biol. Chem. 2009
InteractionInhibits Rv0627activeharsharohiratruefriend2012-10-05
Co-expression (Functional linkage)
authors,J. Robson,JL. McKenzie,R. Cursons,GM. Cook,VL. Arcus The vapBC operon from Mycobacterium smegmatis is an autoregulated toxin-antitoxin module that controls growth via inhibition of translation. J. Mol. Biol. 2009
InteractionInhibits Rv0627activeharsharohiratruefriend2012-10-05
Co-expression (Functional linkage)
authors,HR. Ramage,LE. Connolly,JS. Cox Comprehensive functional analysis of Mycobacterium tuberculosis toxin-antitoxin systems: implications for pathogenesis, stress responses, and evolution. PLoS Genet. 2009
InteractionInhibits Rv0627activeharsharohiratruefriend2012-10-05
Co-expression (Functional linkage)
authors,A. Gupta Killing activity and rescue function of genome-wide toxin-antitoxin loci of Mycobacterium tuberculosis. FEMS Microbiol. Lett. 2009
InteractionInhibits Rv0627activeharsharohiratruefriend2012-10-05
Co-expression (Functional linkage)
authors,L. Miallau,M. Faller,J. Chiang,M. Arbing,F. Guo,D. Cascio,D. Eisenberg Structure and proposed activity of a member of the VapBC family of toxin-antitoxin systems. VapBC-5 from Mycobacterium tuberculosis. J. Biol. Chem. 2009
SymbolVapBactivejlew2012-03-07

authors,BA. Ahidjo,D. Kuhnert,JL. McKenzie,EE. Machowski,BG. Gordhan,V. Arcus,GL. Abrahams,V. Mizrahi VapC toxins from Mycobacterium tuberculosis are ribonucleases that differentially inhibit growth and are neutralized by cognate VapB antitoxins. PLoS ONE 2011
SymbolvapB5activejlew2012-03-07
VapBC5 structure. Assay shows the toxin is an Mg-enabled endoribonuclease
authors,L. Miallau,M. Faller,J. Chiang,M. Arbing,F. Guo,D. Cascio,D. Eisenberg Structure and proposed activity of a member of the VapBC family of toxin-antitoxin systems. VapBC-5 from Mycobacterium tuberculosis. J. Biol. Chem. 2009
SymbolVapB5activejlew2012-03-07
We 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
Otherstrand:+activerslayden2012-03-05
Conserved hypothetical protein, similar to Mycobacterium tuberculosis hypothetical proteins e.g. Rv0596c, Rv3385c, Rv3407,Rv3181c, etc.
Otherstop:718285activerslayden2012-03-05
Conserved hypothetical protein, similar to Mycobacterium tuberculosis hypothetical proteins e.g. Rv0596c, Rv3385c, Rv3407,Rv3181c, etc.
Otherstart:718025activerslayden2012-03-05
Conserved hypothetical protein, similar to Mycobacterium tuberculosis hypothetical proteins e.g. Rv0596c, Rv3385c, Rv3407,Rv3181c, etc.
SymbolVap BC-5activerslayden2012-03-05
Conserved hypothetical protein, similar to Mycobacterium tuberculosis hypothetical proteins e.g. Rv0596c, Rv3385c, Rv3407,Rv3181c, etc.