TB Genome Annotation Portal

Rv2461c (clpP1)

Amino Acid Sequence

VSQVTDMRSNSQGLSLTDSVYERLLSERIIFLGSEVNDEIANRLCAQILLLAAEDASKDISLYINSPGGSISAGMAIYDTMVLAPCDIATYAMGMAASMG
EFLLAAGTKGKRYALPHARILMHQPLGGVTGSAADIAIQAEQFAVIKKEMFRLNAEFTGQPIERIEADSDRDRWFTAAEALEYGFVDHIITRAHVNGEAQ
(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
Uncertain Sodium Oleate H37RvMA Gumbel Subhalaxmi Nambi Probability of Essentiality: 0.991550;
10 non-insertions in a row out of 10 sites
Uncertain Lignoceric Acid H37RvMA Gumbel Subhalaxmi Nambi Probability of Essentiality: 0.978900;
7 non-insertions in a row out of 10 sites
Essential Phosphatidylcholine H37RvMA Gumbel Subhalaxmi Nambi Probability of Essentiality: 0.999450;
10 non-insertions in a row out of 10 sites
Essential minimal media + 0.1% glycerol H37RvMA Gumbel Griffin et al. (2011) Probability of Essentiality: 0.998950;
10 non-insertions in a row out of 10 sites
Essential minimal media + 0.01% cholesterol H37RvMA Gumbel Griffin et al. (2011) Probability of Essentiality: 0.999000;
10 non-insertions in a row out of 10 sites
No-Data 7H10-glycerol H37RvMA TraSH Sassetti et al. (2003a)
Too-Short C57BL/6J mice (8 weeks) H37RvMA TraSH Sassetti et al. (2003b) Hybridization Ratio: -1
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)

    Rv2461c (clpP1)

    PropertyValueCreatorEvidencePMIDComment
    CitationClgR regulation of chaperone and protease systems is essential for Mycobacterium tuberculosis parasitism of the macrophage. authors,M. Estorninho,H. Smith,J. Thole,J. Harders-Westerveen,A. Kierzek,RE. Butler,O. Neyrolles,GR. Stewart Microbiology (Reading, Engl.) 2010akankshajain.21IEP20688819Co-expression (Functional linkage)
    InteractionRegulatory Rv2475cakankshajain.21IEPCo-expression (Functional linkage)
    authors,M. Estorninho,H. Smith,J. Thole,J. Harders-Westerveen,A. Kierzek,RE. Butler,O. Neyrolles,GR. Stewart ClgR regulation of chaperone and protease systems is essential for Mycobacterium tuberculosis parasitism of the macrophage. Microbiology (Reading, Engl.) 2010
    InteractionPhysicalInteraction Rv2457cakankshajain.21IDAStructural analysis
    AK. Gupta, VM. Katoch et al. Microarray analysis of efflux pump genes in multidrug-resistant Mycobacterium tuberculosis during stress induced by common anti-tuberculous drugs. Microb. Drug Resist. 2010
    CitationInsights into the inter-ring plasticity of caseinolytic proteases from the X-ray structure of Mycobacterium tuberculosis ClpP1. H. Ingvarsson, MJ. Mat et al. Acta Crystallogr. D Biol. Crystallogr. 2007akankshajain.21IDA17242518Structural analysis
    InteractionPhysicalInteraction Rv2460cakankshajain.21IDAStructural analysis
    H. Ingvarsson, MJ. Mat et al. Insights into the inter-ring plasticity of caseinolytic proteases from the X-ray structure of Mycobacterium tuberculosis ClpP1. Acta Crystallogr. D Biol. Crystallogr. 2007
    InteractionPhysicalInteraction Rv2457cakankshajain.21IDAStructural analysis
    H. Ingvarsson, MJ. Mat et al. Insights into the inter-ring plasticity of caseinolytic proteases from the X-ray structure of Mycobacterium tuberculosis ClpP1. Acta Crystallogr. D Biol. Crystallogr. 2007
    CitationThe ClpP double ring tetradecameric protease exhibits plastic ring-ring interactions, and the N termini of its subunits form flexible loops that are essential for ClpXP and ClpAP complex formation. authors,A. Gribun,MS. Kimber,R. Ching,R. Sprangers,KM. Fiebig,WA. Houry J. Biol. Chem. 2005akankshajain.21IDA15701650Structural analysis
    InteractionPhysicalInteraction Rv2460cakankshajain.21IDAStructural analysis
    authors,A. Gribun,MS. Kimber,R. Ching,R. Sprangers,KM. Fiebig,WA. Houry The ClpP double ring tetradecameric protease exhibits plastic ring-ring interactions, and the N termini of its subunits form flexible loops that are essential for ClpXP and ClpAP complex formation. J. Biol. Chem. 2005
    InteractionPhysicalInteraction Rv2457cakankshajain.21IDAStructural analysis
    authors,A. Gribun,MS. Kimber,R. Ching,R. Sprangers,KM. Fiebig,WA. Houry The ClpP double ring tetradecameric protease exhibits plastic ring-ring interactions, and the N termini of its subunits form flexible loops that are essential for ClpXP and ClpAP complex formation. J. Biol. Chem. 2005
    CitationClpP: a distinctive family of cylindrical energy-dependent serine proteases. authors,AY. Yu,WA. Houry FEBS Lett. 2007richasinha4uIDA17499722Spectrophotometric Analysis
    InteractionRegulatory Rv2457crichasinha4uIDASpectrophotometric Analysis
    authors,AY. Yu,WA. Houry ClpP: a distinctive family of cylindrical energy-dependent serine proteases. FEBS Lett. 2007
    CitationSequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli. authors,MR. Maurizi,WP. Clark,Y. Katayama,S. Rudikoff,J. Pumphrey,B. Bowers,S. Gottesman J. Biol. Chem. 1990richasinha4uIDA2197275Structural Analysis
    InteractionRegulatory Rv2457crichasinha4uIDAStructural Analysis
    authors,MR. Maurizi,WP. Clark,Y. Katayama,S. Rudikoff,J. Pumphrey,B. Bowers,S. Gottesman Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli. J. Biol. Chem. 1990
    CitationThe ATP-dependent Clp protease of Escherichia coli. Sequence of clpA and identification of a Clp-specific substrate. authors,S. Gottesman,WP. Clark,MR. Maurizi J. Biol. Chem. 1990richasinha4uIDA2186030Structural Analysis
    InteractionRegulatory Rv2457crichasinha4uIDAStructural Analysis
    authors,S. Gottesman,WP. Clark,MR. Maurizi The ATP-dependent Clp protease of Escherichia coli. Sequence of clpA and identification of a Clp-specific substrate. J. Biol. Chem. 1990
    CitationClpP: a distinctive family of cylindrical energy-dependent serine proteases. authors,AY. Yu,WA. Houry FEBS Lett. 2007richasinha4uIDA17499722Structural Analysis
    InteractionRegulatory Rv2457crichasinha4uIDAStructural Analysis
    authors,AY. Yu,WA. Houry ClpP: a distinctive family of cylindrical energy-dependent serine proteases. FEBS Lett. 2007
    CitationMicroarray analysis of efflux pump genes in multidrug-resistant Mycobacterium tuberculosis during stress induced by common anti-tuberculous drugs. AK. Gupta, VM. Katoch et al. Microb. Drug Resist. 2010akankshajain.21IDA20001742Structural analysis
    InteractionPhysicalInteraction Rv2460cakankshajain.21IDAStructural analysis
    AK. Gupta, VM. Katoch et al. Microarray analysis of efflux pump genes in multidrug-resistant Mycobacterium tuberculosis during stress induced by common anti-tuberculous drugs. Microb. Drug Resist. 2010
    InteractionPhysicalInteraction Rv2460cakankshajain.21IDAStructural analysis
    authors,A. Gribun,MS. Kimber,R. Ching,R. Sprangers,KM. Fiebig,WA. Houry The ClpP double ring tetradecameric protease exhibits plastic ring-ring interactions, and the N termini of its subunits form flexible loops that are essential for ClpXP and ClpAP complex formation. J. Biol. Chem. 2005
    CitationSequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli. authors,MR. Maurizi,WP. Clark,Y. Katayama,S. Rudikoff,J. Pumphrey,B. Bowers,S. Gottesman J. Biol. Chem. 1990richasinha4uIDA2197275Spectrophotometric Analysis
    InteractionRegulatory Rv2457crichasinha4uIDASpectrophotometric Analysis
    authors,MR. Maurizi,WP. Clark,Y. Katayama,S. Rudikoff,J. Pumphrey,B. Bowers,S. Gottesman Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli. J. Biol. Chem. 1990
    CitationThe ATP-dependent Clp protease of Escherichia coli. Sequence of clpA and identification of a Clp-specific substrate. authors,S. Gottesman,WP. Clark,MR. Maurizi J. Biol. Chem. 1990richasinha4uIDA2186030Spectrophotometric Analysis
    InteractionRegulatory Rv2457crichasinha4uIDASpectrophotometric Analysis
    authors,S. Gottesman,WP. Clark,MR. Maurizi The ATP-dependent Clp protease of Escherichia coli. Sequence of clpA and identification of a Clp-specific substrate. J. Biol. Chem. 1990
    InteractionPhysicalInteraction Rv2457crichasinha4uIDAStructural Analysis
    authors,B. Banecki,A. Wawrzynow,J. Puzewicz,C. Georgopoulos,M. Zylicz Structure-function analysis of the zinc-binding region of the Clpx molecular chaperone. J. Biol. Chem. 2001
    InteractionPhysicalInteraction Rv2457crichasinha4uIDAStructural Analysis
    authors,LW. Donaldson,U. Wojtyra,WA. Houry Solution structure of the dimeric zinc binding domain of the chaperone ClpX. J. Biol. Chem. 2003
    InteractionPhysicalInteraction Rv2457crichasinha4uIDAStructural Analysis
    authors,AY. Yu,WA. Houry ClpP: a distinctive family of cylindrical energy-dependent serine proteases. FEBS Lett. 2007
    InteractionPhysicalInteraction Rv2460cakankshajain.21IDAStructural analysis
    AK. Gupta, VM. Katoch et al. Microarray analysis of efflux pump genes in multidrug-resistant Mycobacterium tuberculosis during stress induced by common anti-tuberculous drugs. Microb. Drug Resist. 2010
    InteractionPhysicalInteraction Rv2457cvmevada102ISOStructural analysis
    authors,A. Gribun,MS. Kimber,R. Ching,R. Sprangers,KM. Fiebig,WA. Houry The ClpP double ring tetradecameric protease exhibits plastic ring-ring interactions, and the N termini of its subunits form flexible loops that are essential for ClpXP and ClpAP complex formation. J. Biol. Chem. 2005
    InteractionPhysicalInteraction Rv2457crichasinha4uIDASpectrophotometric Analysis
    authors,B. Banecki,A. Wawrzynow,J. Puzewicz,C. Georgopoulos,M. Zylicz Structure-function analysis of the zinc-binding region of the Clpx molecular chaperone. J. Biol. Chem. 2001
    InteractionPhysicalInteraction Rv2457crichasinha4uIDASpectrophotometric Analysis
    authors,LW. Donaldson,U. Wojtyra,WA. Houry Solution structure of the dimeric zinc binding domain of the chaperone ClpX. J. Biol. Chem. 2003
    InteractionPhysicalInteraction Rv2457crichasinha4uIDASpectrophotometric Analysis
    authors,AY. Yu,WA. Houry ClpP: a distinctive family of cylindrical energy-dependent serine proteases. FEBS Lett. 2007
    InteractionPhysicalInteraction Rv2457cvmevada102ISOStructural analysis
    AK. Gupta, VM. Katoch et al. Microarray analysis of efflux pump genes in multidrug-resistant Mycobacterium tuberculosis during stress induced by common anti-tuberculous drugs. Microb. Drug Resist. 2010

    Comments