TB Genome Annotation Portal

Rv1306 (atpF)

Amino Acid Sequence

MGEVSAIVLAASQAAEEGGESSNFLIPNGTFFVVLAIFLVVLAVIGTFVVPPILKVLRERDAMVAKTLADNKKSDEQFAAAQADYDEAMTEARVQASSLR
DNARADGRKVIEDARVRAEQQVASTLQTAHEQLKRERDAVELDLRAHVGTMSATLASRILGVDLTASAATR
(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
Too-Short Sodium Oleate H37RvMA Gumbel Subhalaxmi Nambi Probability of Essentiality: -1.000000;
3 non-insertions in a row out of 3 sites
Too-Short Lignoceric Acid H37RvMA Gumbel Subhalaxmi Nambi Probability of Essentiality: -1.000000;
3 non-insertions in a row out of 3 sites
Too-Short Phosphatidylcholine H37RvMA Gumbel Subhalaxmi Nambi Probability of Essentiality: -1.000000;
3 non-insertions in a row out of 3 sites
Uncertain minimal media + 0.1% glycerol H37RvMA Gumbel Griffin et al. (2011) Probability of Essentiality: 0.949300;
4 non-insertions in a row out of 4 sites
Uncertain minimal media + 0.01% cholesterol H37RvMA Gumbel Griffin et al. (2011) Probability of Essentiality: 0.950300;
4 non-insertions in a row out of 4 sites
Essential 7H10-glycerol H37RvMA TraSH Sassetti et al. (2003a)
Essential C57BL/6J mice (8 weeks) H37RvMA TraSH Sassetti et al. (2003b) Hybridization Ratio: 0.03
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

    RNA processing and modification
    Energy production and conversion
    Chromatin structure and dynamics
    Amino acid transport and metabolism
    Cell cycle control, cell division, chromosome partitioning
    Carbohydrate transport and metabolism
    Nucleotide transport and metabolism
    Lipid transport and metabolism
    Coenzyme transport and metabolism
    Transcription
    Translation, ribosomal structure and biogenesis
    Cell wall/membrane/envelope biogenesis
    Replication, recombination and repair
    Posttranslational modification, protein turnover, chaperones
    Cell motility
    Secondary metabolites biosynthesis, transport and catabolism
    Inorganic ion transport and metabolism
    Function unknown
    General function prediction only
    Intracellular trafficking, secretion, and vesicular transport
    Signal transduction mechanisms
    Extracellular structures
    Defense mechanisms
    Nuclear structure
    Cytoskeleton
  • BioCyc Co-regulated genes based on gene expression profiling (Systems Biology, Inferelator Network)
  • Differentially expressed as result of RNASeq in glycerol environment (Only top 20 genes shown sorted by log fold change with p_adj 0.05).
    Conditionally essential as result of TNSeq (Only top 20 genes shown sorted by log fold change with p_adj 0.05).
  • BioCyc Transcription factor binding based on ChIP-Seq (Systems Biology)
  • Interactions based on ChIPSeq data (Minch et al. 2014)

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



    TBCAP

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

    Rv1306 (atpF)

    PropertyValueCreatorEvidencePMIDComment
    InteractionPhysicalInteraction Rv1304priti.prietyIDAstructural analysis
    MR. de Jonge, LH. Koymans et al. A computational model of the inhibition of Mycobacterium tuberculosis ATPase by a new drug candidate R207910. Proteins 2007
    InteractionPhysicalInteraction Rv1305priti.prietyIDAstructural analysis
    MR. de Jonge, LH. Koymans et al. A computational model of the inhibition of Mycobacterium tuberculosis ATPase by a new drug candidate R207910. Proteins 2007
    CitationDiarylquinolines are bactericidal for dormant mycobacteria as a result of disturbed ATP homeostasis. A. Koul,L. Vranckx,N. Dendouga,W. Balemans,I. Van den Wyngaert,K. Vergauwen,HW. Ghlmann,R. Willebrords,A. Poncelet,J. Guillemont,D. Bald,K. Andries J. Biol. Chem. 2008priti.prietyIDA18625705structural analysis
    InteractionPhysicalInteraction Rv1304priti.prietyIDAstructural analysis
    A. Koul,L. Vranckx,N. Dendouga,W. Balemans,I. Van den Wyngaert,K. Vergauwen,HW. Ghlmann,R. Willebrords,A. Poncelet,J. Guillemont,D. Bald,K. Andries Diarylquinolines are bactericidal for dormant mycobacteria as a result of disturbed ATP homeostasis. J. Biol. Chem. 2008
    InteractionPhysicalInteraction Rv1305priti.prietyIDAstructural analysis
    A. Koul,L. Vranckx,N. Dendouga,W. Balemans,I. Van den Wyngaert,K. Vergauwen,HW. Ghlmann,R. Willebrords,A. Poncelet,J. Guillemont,D. Bald,K. Andries Diarylquinolines are bactericidal for dormant mycobacteria as a result of disturbed ATP homeostasis. J. Biol. Chem. 2008
    InteractionPhysicalInteraction Rv1304priti.prietyIDAstructural analysis
    authors,M. Rappas,H. Niwa,X. Zhang Mechanisms of ATPases--a multi-disciplinary approach. Curr. Protein Pept. Sci. 2004
    InteractionPhysicalInteraction Rv1305priti.prietyIDAstructural analysis
    authors,M. Rappas,H. Niwa,X. Zhang Mechanisms of ATPases--a multi-disciplinary approach. Curr. Protein Pept. Sci. 2004
    CitationStructure of the F1-binding domain of the stator of bovine F1Fo-ATPase and how it binds an alpha-subunit. authors,RJ. Carbajo,FA. Kellas,MJ. Runswick,MG. Montgomery,JE. Walker,D. Neuhaus J. Mol. Biol. 2005priti.prietyIDA16045926structural analysis
    InteractionPhysicalInteraction Rv1304priti.prietyIDAstructural analysis
    authors,RJ. Carbajo,FA. Kellas,MJ. Runswick,MG. Montgomery,JE. Walker,D. Neuhaus Structure of the F1-binding domain of the stator of bovine F1Fo-ATPase and how it binds an alpha-subunit. J. Mol. Biol. 2005
    InteractionPhysicalInteraction Rv1305priti.prietyIDAstructural analysis
    authors,RJ. Carbajo,FA. Kellas,MJ. Runswick,MG. Montgomery,JE. Walker,D. Neuhaus Structure of the F1-binding domain of the stator of bovine F1Fo-ATPase and how it binds an alpha-subunit. J. Mol. Biol. 2005
    CitationDormancy phenotype displayed by extracellular Mycobacterium tuberculosis within artificial granulomas in mice. PC. Karakousis, T. Yoshimatsu et al. J. Exp. Med. 2004priti.prietyIDA15353557structural analysis
    InteractionPhysicalInteraction Rv1304priti.prietyIDAstructural analysis
    PC. Karakousis, T. Yoshimatsu et al. Dormancy phenotype displayed by extracellular Mycobacterium tuberculosis within artificial granulomas in mice. J. Exp. Med. 2004
    InteractionPhysicalInteraction Rv1305priti.prietyIDAstructural analysis
    PC. Karakousis, T. Yoshimatsu et al. Dormancy phenotype displayed by extracellular Mycobacterium tuberculosis within artificial granulomas in mice. J. Exp. Med. 2004
    CitationA computational model of the inhibition of Mycobacterium tuberculosis ATPase by a new drug candidate R207910. MR. de Jonge, LH. Koymans et al. Proteins 2007priti.prietyIDA17387738structural analysis
    InteractionPhysicalInteraction Rv1305priti.prietyIDAspectrophotometric assy
    PC. Karakousis, T. Yoshimatsu et al. Dormancy phenotype displayed by extracellular Mycobacterium tuberculosis within artificial granulomas in mice. J. Exp. Med. 2004
    CitationA computational model of the inhibition of Mycobacterium tuberculosis ATPase by a new drug candidate R207910. MR. de Jonge, LH. Koymans et al. Proteins 2007priti.prietyIDA17387738spectrophotometric assy
    InteractionPhysicalInteraction Rv1304priti.prietyIDAspectrophotometric assy
    MR. de Jonge, LH. Koymans et al. A computational model of the inhibition of Mycobacterium tuberculosis ATPase by a new drug candidate R207910. Proteins 2007
    InteractionPhysicalInteraction Rv1305priti.prietyIDAspectrophotometric assy
    MR. de Jonge, LH. Koymans et al. A computational model of the inhibition of Mycobacterium tuberculosis ATPase by a new drug candidate R207910. Proteins 2007
    CitationDiarylquinolines are bactericidal for dormant mycobacteria as a result of disturbed ATP homeostasis. A. Koul,L. Vranckx,N. Dendouga,W. Balemans,I. Van den Wyngaert,K. Vergauwen,HW. Ghlmann,R. Willebrords,A. Poncelet,J. Guillemont,D. Bald,K. Andries J. Biol. Chem. 2008priti.prietyIDA18625705spectrophotometric assy
    InteractionPhysicalInteraction Rv1304priti.prietyIDAspectrophotometric assy
    A. Koul,L. Vranckx,N. Dendouga,W. Balemans,I. Van den Wyngaert,K. Vergauwen,HW. Ghlmann,R. Willebrords,A. Poncelet,J. Guillemont,D. Bald,K. Andries Diarylquinolines are bactericidal for dormant mycobacteria as a result of disturbed ATP homeostasis. J. Biol. Chem. 2008
    InteractionPhysicalInteraction Rv1305priti.prietyIDAspectrophotometric assy
    A. Koul,L. Vranckx,N. Dendouga,W. Balemans,I. Van den Wyngaert,K. Vergauwen,HW. Ghlmann,R. Willebrords,A. Poncelet,J. Guillemont,D. Bald,K. Andries Diarylquinolines are bactericidal for dormant mycobacteria as a result of disturbed ATP homeostasis. J. Biol. Chem. 2008
    CitationMechanisms of ATPases--a multi-disciplinary approach. authors,M. Rappas,H. Niwa,X. Zhang Curr. Protein Pept. Sci. 2004priti.prietyIDA15078220structural analysis
    InteractionPhysicalInteraction Rv1305priti.prietyIDAstructural analysis
    A. Koul,L. Vranckx,N. Dendouga,W. Balemans,I. Van den Wyngaert,K. Vergauwen,HW. Ghlmann,R. Willebrords,A. Poncelet,J. Guillemont,D. Bald,K. Andries Diarylquinolines are bactericidal for dormant mycobacteria as a result of disturbed ATP homeostasis. J. Biol. Chem. 2008
    CitationMechanisms of ATPases--a multi-disciplinary approach. authors,M. Rappas,H. Niwa,X. Zhang Curr. Protein Pept. Sci. 2004priti.prietyIDA15078220spectrophotometric assy
    InteractionPhysicalInteraction Rv1304priti.prietyIDAspectrophotometric assy
    authors,M. Rappas,H. Niwa,X. Zhang Mechanisms of ATPases--a multi-disciplinary approach. Curr. Protein Pept. Sci. 2004
    InteractionPhysicalInteraction Rv1305priti.prietyIDAspectrophotometric assy
    authors,M. Rappas,H. Niwa,X. Zhang Mechanisms of ATPases--a multi-disciplinary approach. Curr. Protein Pept. Sci. 2004
    CitationStructure of the F1-binding domain of the stator of bovine F1Fo-ATPase and how it binds an alpha-subunit. authors,RJ. Carbajo,FA. Kellas,MJ. Runswick,MG. Montgomery,JE. Walker,D. Neuhaus J. Mol. Biol. 2005priti.prietyIDA16045926spectrophotometric assy
    InteractionPhysicalInteraction Rv1304priti.prietyIDAspectrophotometric assy
    authors,RJ. Carbajo,FA. Kellas,MJ. Runswick,MG. Montgomery,JE. Walker,D. Neuhaus Structure of the F1-binding domain of the stator of bovine F1Fo-ATPase and how it binds an alpha-subunit. J. Mol. Biol. 2005
    InteractionPhysicalInteraction Rv1305priti.prietyIDAspectrophotometric assy
    authors,RJ. Carbajo,FA. Kellas,MJ. Runswick,MG. Montgomery,JE. Walker,D. Neuhaus Structure of the F1-binding domain of the stator of bovine F1Fo-ATPase and how it binds an alpha-subunit. J. Mol. Biol. 2005
    CitationDormancy phenotype displayed by extracellular Mycobacterium tuberculosis within artificial granulomas in mice. PC. Karakousis, T. Yoshimatsu et al. J. Exp. Med. 2004priti.prietyIDA15353557spectrophotometric assy
    InteractionPhysicalInteraction Rv1304priti.prietyIDAspectrophotometric assy
    PC. Karakousis, T. Yoshimatsu et al. Dormancy phenotype displayed by extracellular Mycobacterium tuberculosis within artificial granulomas in mice. J. Exp. Med. 2004
    InteractionPhysicalInteraction Rv1305priti.prietyIDAstructural analysis
    authors,RJ. Carbajo,FA. Kellas,MJ. Runswick,MG. Montgomery,JE. Walker,D. Neuhaus Structure of the F1-binding domain of the stator of bovine F1Fo-ATPase and how it binds an alpha-subunit. J. Mol. Biol. 2005
    InteractionPhysicalInteraction Rv1305priti.prietyIDAstructural analysis
    PC. Karakousis, T. Yoshimatsu et al. Dormancy phenotype displayed by extracellular Mycobacterium tuberculosis within artificial granulomas in mice. J. Exp. Med. 2004
    InteractionPhysicalInteraction Rv1305priti.prietyIDAstructural analysis
    MR. de Jonge, LH. Koymans et al. A computational model of the inhibition of Mycobacterium tuberculosis ATPase by a new drug candidate R207910. Proteins 2007
    InteractionPhysicalInteraction Rv1305priti.prietyIDAspectrophotometric assy
    MR. de Jonge, LH. Koymans et al. A computational model of the inhibition of Mycobacterium tuberculosis ATPase by a new drug candidate R207910. Proteins 2007
    InteractionPhysicalInteraction Rv1305priti.prietyIDAspectrophotometric assy
    A. Koul,L. Vranckx,N. Dendouga,W. Balemans,I. Van den Wyngaert,K. Vergauwen,HW. Ghlmann,R. Willebrords,A. Poncelet,J. Guillemont,D. Bald,K. Andries Diarylquinolines are bactericidal for dormant mycobacteria as a result of disturbed ATP homeostasis. J. Biol. Chem. 2008
    InteractionPhysicalInteraction Rv1304priti.prietyIDAstructural analysis
    MR. de Jonge, LH. Koymans et al. A computational model of the inhibition of Mycobacterium tuberculosis ATPase by a new drug candidate R207910. Proteins 2007
    InteractionPhysicalInteraction Rv1305priti.prietyIDAspectrophotometric assy
    authors,RJ. Carbajo,FA. Kellas,MJ. Runswick,MG. Montgomery,JE. Walker,D. Neuhaus Structure of the F1-binding domain of the stator of bovine F1Fo-ATPase and how it binds an alpha-subunit. J. Mol. Biol. 2005
    InteractionPhysicalInteraction Rv1305priti.prietyIDAspectrophotometric assy
    PC. Karakousis, T. Yoshimatsu et al. Dormancy phenotype displayed by extracellular Mycobacterium tuberculosis within artificial granulomas in mice. J. Exp. Med. 2004
    InteractionPhysicalInteraction Rv1304priti.prietyIDAspectrophotometric assy
    MR. de Jonge, LH. Koymans et al. A computational model of the inhibition of Mycobacterium tuberculosis ATPase by a new drug candidate R207910. Proteins 2007
    InteractionPhysicalInteraction Rv1304priti.prietyIDAstructural analysis
    authors,RJ. Carbajo,FA. Kellas,MJ. Runswick,MG. Montgomery,JE. Walker,D. Neuhaus Structure of the F1-binding domain of the stator of bovine F1Fo-ATPase and how it binds an alpha-subunit. J. Mol. Biol. 2005
    InteractionPhysicalInteraction Rv1304priti.prietyIDAstructural analysis
    PC. Karakousis, T. Yoshimatsu et al. Dormancy phenotype displayed by extracellular Mycobacterium tuberculosis within artificial granulomas in mice. J. Exp. Med. 2004
    InteractionPhysicalInteraction Rv1304priti.prietyIDAspectrophotometric assy
    authors,RJ. Carbajo,FA. Kellas,MJ. Runswick,MG. Montgomery,JE. Walker,D. Neuhaus Structure of the F1-binding domain of the stator of bovine F1Fo-ATPase and how it binds an alpha-subunit. J. Mol. Biol. 2005
    InteractionPhysicalInteraction Rv1304priti.prietyIDAspectrophotometric assy
    PC. Karakousis, T. Yoshimatsu et al. Dormancy phenotype displayed by extracellular Mycobacterium tuberculosis within artificial granulomas in mice. J. Exp. Med. 2004
    InteractionRegulatedBy Rv0981yamir.morenoIEPMicroarrays. mRNA levels of regulated element measured and compared between wild-type and trans-element mutation (knockout, over expression etc.) performed by using microarray (or macroarray) experiments..
    H. He, R. Hovey et al. MprAB is a stress-responsive two-component system that directly regulates expression of sigma factors SigB and SigE in Mycobacterium tuberculosis. J. Bacteriol. 2006
    InteractionRegulatedBy Rv1221yamir.morenoIEPMicroarrays. mRNA levels of regulated element measured and compared between wild-type and trans-element mutation (knockout, over expression etc.) performed by using microarray (or macroarray) experiments..
    R. Manganelli, MI. Voskuil et al. The Mycobacterium tuberculosis ECF sigma factor sigmaE: role in global gene expression and survival in macrophages. Mol. Microbiol. 2001

    Comments