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Protein

ATP-dependent Clp protease proteolytic subunit

Gene

clpP

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. Degrades antitoxin MazE (PubMed:24375411).UniRule annotation3 Publications

Catalytic activityi

Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec; and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).UniRule annotation

Enzyme regulationi

Inhibited by benzyloxycarbonyl leucyltyrosine chloromethylketone (Z-LY-CMK).1 Publication

Kineticsi

  1. KM=4.4 mM for N-succinyl-Leu-Tyr-7-amino-4-methyl-coumarin (N-succinyl-Leu-Tyr-AMC)2 Publications
  2. KM=1.0 mM for N-succinyl-Leu-Tyr-AMC2 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei111NucleophileCurated1
    Active sitei136Curated1
    Active sitei185Curated1

    GO - Molecular functioni

    • ATP-dependent peptidase activity Source: CACAO
    • identical protein binding Source: EcoCyc
    • serine-type endopeptidase activity Source: UniProtKB-HAMAP
    • serine-type peptidase activity Source: EcoCyc

    GO - Biological processi

    • misfolded or incompletely synthesized protein catabolic process Source: MGI
    • proteasomal protein catabolic process Source: CACAO
    • response to heat Source: EcoliWiki
    • response to temperature stimulus Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Stress response

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10158-MONOMER.
    ECOL316407:JW0427-MONOMER.
    MetaCyc:EG10158-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP-dependent Clp protease proteolytic subunitUniRule annotation (EC:3.4.21.92UniRule annotation)
    Alternative name(s):
    Caseinolytic protease
    Endopeptidase ClpUniRule annotation
    Heat shock protein F21.5
    Protease Ti
    Gene namesi
    Name:clpPUniRule annotation
    Synonyms:lopP
    Ordered Locus Names:b0437, JW0427
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10158. clpP.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: UniProtKB
    • membrane Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Cells undergo an apoptotic-like death upon DNA damage characterized by membrane depolarization (PubMed:22412352). Decreased persister cell formation upon antibotic challenge probably due to increased levels of MazF toxin (PubMed:24375411).2 Publications

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi17V → A: No ClpA-ClpP, little ClpX-ClpP complex forms. 1 Publication1
    Mutagenesisi18P → A: Reduced processing, no ClpA-ClpP complex forms. 1 Publication1
    Mutagenesisi19M → A: No ClpA-ClpP, little ClpX-ClpP complex forms. 1 Publication1
    Mutagenesisi20V → A: No ClpA-ClpP or ClpX-ClpP complex forms. 1 Publication1
    Mutagenesisi21I → A: No ClpA-ClpP or ClpX-ClpP complex forms. 1 Publication1
    Mutagenesisi24T → A: No ClpA-ClpP, little ClpX-ClpP complex forms. 1 Publication1
    Mutagenesisi27G → A: No ClpA-ClpP, little ClpX-ClpP complex forms. 1 Publication1
    Mutagenesisi32D → A: No ClpA-ClpP or ClpX-ClpP complex forms. 1 Publication1
    Mutagenesisi33I → A: No ClpA-ClpP or ClpX-ClpP complex forms. 1 Publication1
    Mutagenesisi34Y → A: No ClpA-ClpP or ClpX-ClpP complex forms. 1 Publication1
    Mutagenesisi126F → A: Little ClpA-ClpP or ClpX-ClpP complex forms. 1 Publication1
    Mutagenesisi185D → A: Loss of protease activity, forms ClpA-ClpP complex. 1 Publication1

    Chemistry databases

    ChEMBLiCHEMBL3341578.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    PropeptideiPRO_00002680121 – 141 PublicationAdd BLAST14
    ChainiPRO_000017955115 – 207ATP-dependent Clp protease proteolytic subunitAdd BLAST193

    Keywords - PTMi

    Zymogen

    Proteomic databases

    EPDiP0A6G7.
    PaxDbiP0A6G7.
    PRIDEiP0A6G7.

    2D gel databases

    SWISS-2DPAGEP0A6G7.

    Expressioni

    Inductioni

    By heat shock. Part of the clpP-clpX operon.1 Publication

    Interactioni

    Subunit structurei

    Fourteen ClpP subunits assemble into 2 heptameric rings which stack back to back to give a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes. Component of the ClpAP and ClpXP complexes.UniRule annotation5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-370625,EBI-370625
    clpAP0ABH93EBI-370625,EBI-546140

    GO - Molecular functioni

    • identical protein binding Source: EcoCyc

    Protein-protein interaction databases

    BioGridi4260736. 437 interactors.
    DIPiDIP-31838N.
    IntActiP0A6G7. 67 interactors.
    STRINGi511145.b0437.

    Chemistry databases

    BindingDBiP0A6G7.

    Structurei

    Secondary structure

    1207
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi19 – 21Combined sources3
    Beta strandi22 – 24Combined sources3
    Beta strandi27 – 29Combined sources3
    Beta strandi30 – 32Combined sources3
    Helixi33 – 38Combined sources6
    Turni39 – 41Combined sources3
    Beta strandi42 – 49Combined sources8
    Helixi51 – 67Combined sources17
    Beta strandi69 – 71Combined sources3
    Beta strandi73 – 79Combined sources7
    Helixi84 – 96Combined sources13
    Beta strandi97 – 99Combined sources3
    Beta strandi101 – 110Combined sources10
    Helixi112 – 118Combined sources7
    Beta strandi125 – 127Combined sources3
    Beta strandi132 – 135Combined sources4
    Beta strandi139 – 145Combined sources7
    Helixi146 – 171Combined sources26
    Helixi175 – 181Combined sources7
    Turni182 – 185Combined sources4
    Beta strandi186 – 189Combined sources4
    Helixi190 – 195Combined sources6
    Beta strandi198 – 202Combined sources5

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1TYFX-ray2.30A/B/C/D/E/F/G/H/I/J/K/L/M/N15-207[»]
    1YG6X-ray1.90A/B/C/D/E/F/G/H/I/J/K/L/M/N15-207[»]
    1YG8X-ray2.60A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b18-207[»]
    2FZSX-ray1.90A/B/C/D/E/F/G/H/I/J/K/L/M/N15-207[»]
    3HLNX-ray3.201/2/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z15-207[»]
    3MT6X-ray1.90A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b1-207[»]
    ProteinModelPortaliP0A6G7.
    SMRiP0A6G7.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A6G7.

    Family & Domainsi

    Domaini

    The N-terminus (residues 17-34) interact with ClpA and ClpX.1 Publication

    Sequence similaritiesi

    Belongs to the peptidase S14 family.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4105CCQ. Bacteria.
    COG0740. LUCA.
    HOGENOMiHOG000285833.
    InParanoidiP0A6G7.
    KOiK01358.
    OMAiARMNELM.
    PhylomeDBiP0A6G7.

    Family and domain databases

    Gene3Di3.90.226.10. 1 hit.
    HAMAPiMF_00444. ClpP. 1 hit.
    InterProiIPR001907. ClpP.
    IPR029045. ClpP/crotonase-like_dom.
    IPR023562. ClpP/TepA.
    IPR033135. ClpP_His_AS.
    IPR018215. ClpP_Ser_AS.
    [Graphical view]
    PANTHERiPTHR10381. PTHR10381. 1 hit.
    PfamiPF00574. CLP_protease. 1 hit.
    [Graphical view]
    PRINTSiPR00127. CLPPROTEASEP.
    SUPFAMiSSF52096. SSF52096. 1 hit.
    TIGRFAMsiTIGR00493. clpP. 1 hit.
    PROSITEiPS00382. CLP_PROTEASE_HIS. 1 hit.
    PS00381. CLP_PROTEASE_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0A6G7-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSYSGERDNF APHMALVPMV IEQTSRGERS FDIYSRLLKE RVIFLTGQVE
    60 70 80 90 100
    DHMANLIVAQ MLFLEAENPE KDIYLYINSP GGVITAGMSI YDTMQFIKPD
    110 120 130 140 150
    VSTICMGQAA SMGAFLLTAG AKGKRFCLPN SRVMIHQPLG GYQGQATDIE
    160 170 180 190 200
    IHAREILKVK GRMNELMALH TGQSLEQIER DTERDRFLSA PEAVEYGLVD

    SILTHRN
    Length:207
    Mass (Da):23,187
    Last modified:March 29, 2005 - v1
    Checksum:iA7843D036C8CB3C2
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J05534 Genomic DNA. Translation: AAA23588.1.
    U82664 Genomic DNA. Translation: AAB40193.1.
    U00096 Genomic DNA. Translation: AAC73540.1.
    AP009048 Genomic DNA. Translation: BAE76217.1.
    PIRiB36575.
    RefSeqiNP_414971.1. NC_000913.3.
    WP_000122253.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73540; AAC73540; b0437.
    BAE76217; BAE76217; BAE76217.
    GeneIDi945082.
    KEGGiecj:JW0427.
    eco:b0437.
    PATRICi32116027. VBIEscCol129921_0455.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J05534 Genomic DNA. Translation: AAA23588.1.
    U82664 Genomic DNA. Translation: AAB40193.1.
    U00096 Genomic DNA. Translation: AAC73540.1.
    AP009048 Genomic DNA. Translation: BAE76217.1.
    PIRiB36575.
    RefSeqiNP_414971.1. NC_000913.3.
    WP_000122253.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1TYFX-ray2.30A/B/C/D/E/F/G/H/I/J/K/L/M/N15-207[»]
    1YG6X-ray1.90A/B/C/D/E/F/G/H/I/J/K/L/M/N15-207[»]
    1YG8X-ray2.60A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b18-207[»]
    2FZSX-ray1.90A/B/C/D/E/F/G/H/I/J/K/L/M/N15-207[»]
    3HLNX-ray3.201/2/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z15-207[»]
    3MT6X-ray1.90A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b1-207[»]
    ProteinModelPortaliP0A6G7.
    SMRiP0A6G7.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4260736. 437 interactors.
    DIPiDIP-31838N.
    IntActiP0A6G7. 67 interactors.
    STRINGi511145.b0437.

    Chemistry databases

    BindingDBiP0A6G7.
    ChEMBLiCHEMBL3341578.

    2D gel databases

    SWISS-2DPAGEP0A6G7.

    Proteomic databases

    EPDiP0A6G7.
    PaxDbiP0A6G7.
    PRIDEiP0A6G7.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73540; AAC73540; b0437.
    BAE76217; BAE76217; BAE76217.
    GeneIDi945082.
    KEGGiecj:JW0427.
    eco:b0437.
    PATRICi32116027. VBIEscCol129921_0455.

    Organism-specific databases

    EchoBASEiEB0156.
    EcoGeneiEG10158. clpP.

    Phylogenomic databases

    eggNOGiENOG4105CCQ. Bacteria.
    COG0740. LUCA.
    HOGENOMiHOG000285833.
    InParanoidiP0A6G7.
    KOiK01358.
    OMAiARMNELM.
    PhylomeDBiP0A6G7.

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10158-MONOMER.
    ECOL316407:JW0427-MONOMER.
    MetaCyc:EG10158-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiP0A6G7.
    PROiP0A6G7.

    Family and domain databases

    Gene3Di3.90.226.10. 1 hit.
    HAMAPiMF_00444. ClpP. 1 hit.
    InterProiIPR001907. ClpP.
    IPR029045. ClpP/crotonase-like_dom.
    IPR023562. ClpP/TepA.
    IPR033135. ClpP_His_AS.
    IPR018215. ClpP_Ser_AS.
    [Graphical view]
    PANTHERiPTHR10381. PTHR10381. 1 hit.
    PfamiPF00574. CLP_protease. 1 hit.
    [Graphical view]
    PRINTSiPR00127. CLPPROTEASEP.
    SUPFAMiSSF52096. SSF52096. 1 hit.
    TIGRFAMsiTIGR00493. clpP. 1 hit.
    PROSITEiPS00382. CLP_PROTEASE_HIS. 1 hit.
    PS00381. CLP_PROTEASE_SER. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiCLPP_ECOLI
    AccessioniPrimary (citable) accession number: P0A6G7
    Secondary accession number(s): P19245, Q2MBY9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2005
    Last sequence update: March 29, 2005
    Last modified: November 2, 2016
    This is version 109 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Acyldepsipeptide antibiotics bind in the ClpA or ClpX binding-sites, rendering the enzyme ATP-independent and indiscriminate, thus killing cells.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Peptidase families
      Classification of peptidase families and list of entries
    4. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.