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P0A6G7

- CLPP_ECOLI

UniProt

P0A6G7 - CLPP_ECOLI

Protein

ATP-dependent Clp protease proteolytic subunit

Gene

clpP

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (29 Mar 2005)
      Previous versions | rss
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    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.2 PublicationsUniRule annotation

    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)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei111 – 1111NucleophileCurated
    Active sitei136 – 1361Curated
    Active sitei185 – 1851Curated

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. serine-type endopeptidase activity Source: UniProtKB-HAMAP
    3. serine-type peptidase activity Source: EcoCyc

    GO - Biological processi

    1. misfolded or incompletely synthesized protein catabolic process Source: MGI
    2. response to heat Source: EcoliWiki
    3. response to temperature stimulus Source: EcoCyc

    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10158. clpP.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi17 – 171V → A: No ClpA-ClpP, little ClpX-ClpP complex forms. 1 Publication
    Mutagenesisi18 – 181P → A: Reduced processing, no ClpA-ClpP complex forms. 1 Publication
    Mutagenesisi19 – 191M → A: No ClpA-ClpP, little ClpX-ClpP complex forms. 1 Publication
    Mutagenesisi20 – 201V → A: No ClpA-ClpP or ClpX-ClpP complex forms. 1 Publication
    Mutagenesisi21 – 211I → A: No ClpA-ClpP or ClpX-ClpP complex forms. 1 Publication
    Mutagenesisi24 – 241T → A: No ClpA-ClpP, little ClpX-ClpP complex forms. 1 Publication
    Mutagenesisi27 – 271G → A: No ClpA-ClpP, little ClpX-ClpP complex forms. 1 Publication
    Mutagenesisi32 – 321D → A: No ClpA-ClpP or ClpX-ClpP complex forms. 1 Publication
    Mutagenesisi33 – 331I → A: No ClpA-ClpP or ClpX-ClpP complex forms. 1 Publication
    Mutagenesisi34 – 341Y → A: No ClpA-ClpP or ClpX-ClpP complex forms. 1 Publication
    Mutagenesisi126 – 1261F → A: Little ClpA-ClpP or ClpX-ClpP complex forms. 1 Publication
    Mutagenesisi185 – 1851D → A: Loss of protease activity, forms ClpA-ClpP complex. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 14141 PublicationPRO_0000268012Add
    BLAST
    Chaini15 – 207193ATP-dependent Clp protease proteolytic subunitPRO_0000179551Add
    BLAST

    Keywords - PTMi

    Zymogen

    Proteomic databases

    PaxDbiP0A6G7.
    PRIDEiP0A6G7.

    2D gel databases

    SWISS-2DPAGEP0A6G7.

    Expressioni

    Inductioni

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

    Gene expression databases

    GenevestigatoriP0A6G7.

    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.5 PublicationsUniRule annotation

    Binary interactionsi

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

    Protein-protein interaction databases

    DIPiDIP-31838N.
    IntActiP0A6G7. 67 interactions.
    STRINGi511145.b0437.

    Structurei

    Secondary structure

    1
    207
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi19 – 213
    Beta strandi22 – 243
    Beta strandi30 – 323
    Helixi33 – 386
    Turni39 – 413
    Beta strandi42 – 498
    Helixi51 – 6717
    Beta strandi69 – 713
    Beta strandi73 – 797
    Helixi84 – 9613
    Beta strandi97 – 993
    Beta strandi101 – 11010
    Helixi112 – 1187
    Beta strandi125 – 1273
    Beta strandi132 – 1354
    Beta strandi139 – 1457
    Helixi146 – 17126
    Helixi175 – 1817
    Turni182 – 1854
    Beta strandi186 – 1894
    Helixi190 – 1956
    Beta strandi198 – 2025

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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. Positions 16-207.
    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

    eggNOGiCOG0740.
    HOGENOMiHOG000285833.
    KOiK01358.
    OMAiKGERSFD.
    OrthoDBiEOG6Z3KQ0.
    PhylomeDBiP0A6G7.

    Family and domain databases

    Gene3Di3.90.226.10. 1 hit.
    HAMAPiMF_00444. ClpP.
    InterProiIPR001907. ClpP.
    IPR029045. ClpP/crotonase-like_dom.
    IPR023562. ClpP/TepA.
    IPR018215. ClpP_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

    MSYSGERDNF APHMALVPMV IEQTSRGERS FDIYSRLLKE RVIFLTGQVE    50
    DHMANLIVAQ MLFLEAENPE KDIYLYINSP GGVITAGMSI YDTMQFIKPD 100
    VSTICMGQAA SMGAFLLTAG AKGKRFCLPN SRVMIHQPLG GYQGQATDIE 150
    IHAREILKVK GRMNELMALH TGQSLEQIER DTERDRFLSA PEAVEYGLVD 200
    SILTHRN 207
    Length:207
    Mass (Da):23,187
    Last modified:March 29, 2005 - v1
    Checksum:iA7843D036C8CB3C2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    YP_488729.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73540; AAC73540; b0437.
    BAE76217; BAE76217; BAE76217.
    GeneIDi12931742.
    945082.
    KEGGiecj:Y75_p0425.
    eco:b0437.
    PATRICi32116027. VBIEscCol129921_0455.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi B36575.
    RefSeqi NP_414971.1. NC_000913.3.
    YP_488729.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1TYF X-ray 2.30 A/B/C/D/E/F/G/H/I/J/K/L/M/N 15-207 [» ]
    1YG6 X-ray 1.90 A/B/C/D/E/F/G/H/I/J/K/L/M/N 15-207 [» ]
    1YG8 X-ray 2.60 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/Z/a/b 18-207 [» ]
    2FZS X-ray 1.90 A/B/C/D/E/F/G/H/I/J/K/L/M/N 15-207 [» ]
    3HLN X-ray 3.20 1/2/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/Z 15-207 [» ]
    3MT6 X-ray 1.90 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/Z/a/b 1-207 [» ]
    ProteinModelPortali P0A6G7.
    SMRi P0A6G7. Positions 16-207.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-31838N.
    IntActi P0A6G7. 67 interactions.
    STRINGi 511145.b0437.

    2D gel databases

    SWISS-2DPAGE P0A6G7.

    Proteomic databases

    PaxDbi P0A6G7.
    PRIDEi P0A6G7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73540 ; AAC73540 ; b0437 .
    BAE76217 ; BAE76217 ; BAE76217 .
    GeneIDi 12931742.
    945082.
    KEGGi ecj:Y75_p0425.
    eco:b0437.
    PATRICi 32116027. VBIEscCol129921_0455.

    Organism-specific databases

    EchoBASEi EB0156.
    EcoGenei EG10158. clpP.

    Phylogenomic databases

    eggNOGi COG0740.
    HOGENOMi HOG000285833.
    KOi K01358.
    OMAi KGERSFD.
    OrthoDBi EOG6Z3KQ0.
    PhylomeDBi P0A6G7.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10158-MONOMER.
    ECOL316407:JW0427-MONOMER.
    MetaCyc:EG10158-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A6G7.
    PROi P0A6G7.

    Gene expression databases

    Genevestigatori P0A6G7.

    Family and domain databases

    Gene3Di 3.90.226.10. 1 hit.
    HAMAPi MF_00444. ClpP.
    InterProi IPR001907. ClpP.
    IPR029045. ClpP/crotonase-like_dom.
    IPR023562. ClpP/TepA.
    IPR018215. ClpP_AS.
    [Graphical view ]
    PANTHERi PTHR10381. PTHR10381. 1 hit.
    Pfami PF00574. CLP_protease. 1 hit.
    [Graphical view ]
    PRINTSi PR00127. CLPPROTEASEP.
    SUPFAMi SSF52096. SSF52096. 1 hit.
    TIGRFAMsi TIGR00493. clpP. 1 hit.
    PROSITEi PS00382. CLP_PROTEASE_HIS. 1 hit.
    PS00381. CLP_PROTEASE_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli."
      Maurizi M.R., Clark W.P., Katayama Y., Rudikoff S., Pumphrey J., Bowers B., Gottesman S.
      J. Biol. Chem. 265:12536-12545(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 15-36.
    2. "Sequence of minutes 4-25 of Escherichia coli."
      Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "The ClpP component of Clp protease is the sigma 32-dependent heat shock protein F21.5."
      Kroh H.E., Simon L.D.
      J. Bacteriol. 172:6026-6034(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION AS A HEAT SHOCK PROTEIN.
    6. "A comparative study of the chymotrypsin-like activity of the rat liver multicatalytic proteinase and the ClpP from Escherichia coli."
      Arribas J., Castano J.G.
      J. Biol. Chem. 268:21165-21171(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    7. "clpX encoding an alternative ATP-binding subunit of protease Ti (Clp) can be expressed independently from clpP in Escherichia coli."
      Yoo S.J., Seol J.H., Kang M.S., Ha D.B., Chung C.H.
      Biochem. Biophys. Res. Commun. 203:798-804(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, OPERON.
    8. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    9. "Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine."
      Kenniston J.A., Baker T.A., Fernandez J.M., Sauer R.T.
      Cell 114:511-520(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Modulating substrate choice: the SspB adaptor delivers a regulator of the extracytoplasmic-stress response to the AAA+ protease ClpXP for degradation."
      Flynn J.M., Levchenko I., Sauer R.T., Baker T.A.
      Genes Dev. 18:2292-2301(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBSTRATE.
    11. "Molecular symmetry of the ClpP component of the ATP-dependent Clp protease, an Escherichia coli homolog of 20 S proteasome."
      Shin D.H., Lee C.S., Chung C.H., Suh S.W.
      J. Mol. Biol. 262:71-76(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    12. "The structure of ClpP at 2.3-A resolution suggests a model for ATP-dependent proteolysis."
      Wang J., Hartling J.A., Flanagan J.M.
      Cell 91:447-456(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 15-207, SUBUNIT.
    13. "The asymmetry in the mature amino-terminus of ClpP facilitates a local symmetry match in ClpAP and ClpXP complexes."
      Bewley M.C., Graziano V., Griffin K., Flanagan J.M.
      J. Struct. Biol. 153:113-128(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 15-207, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DOMAIN, MUTAGENESIS OF VAL-17; PRO-18; MET-19; VAL-20; ILE-21; THR-24; GLY-27; ASP-32; ILE-33; TYR-34; PHE-126 AND ASP-185.
    14. "Crystal structure at 1.9 A of E. coli ClpP with a peptide covalently bound at the active site."
      Szyk A., Maurizi M.R.
      J. Struct. Biol. 156:165-174(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 15-207 BOUND TO INHIBITOR, ENZYME REGULATION, SUBUNIT.
    15. "Acyldepsipeptide antibiotics induce the formation of a structured axial channel in ClpP: A model for the ClpX/ClpA-bound state of ClpP."
      Li D.H., Chung Y.S., Gloyd M., Joseph E., Ghirlando R., Wright G.D., Cheng Y.Q., Maurizi M.R., Guarne A., Ortega J.
      Chem. Biol. 17:959-969(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ANTIBIOTIC, SUBUNIT.
    16. "Structural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations."
      Kimber M.S., Yu A.Y., Borg M., Leung E., Chan H.S., Houry W.A.
      Structure 18:798-808(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 15-207, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

    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: October 1, 2014
    This is version 92 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

    External Data

    Dasty 3