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P0A6G7 (CLPP_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP-dependent Clp protease proteolytic subunit

EC=3.4.21.92
Alternative name(s):
Caseinolytic protease
Endopeptidase Clp
Heat shock protein F21.5
Protease Ti
Gene names
Name:clpP
Synonyms:lopP
Ordered Locus Names:b0437, JW0427
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length207 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.10

Catalytic activity

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). HAMAP-Rule MF_00444

Enzyme regulation

Inhibited by benzyloxycarbonyl leucyltyrosine chloromethylketone (Z-LY-CMK). Ref.14

Subunit structure

Component of the ClpAP and ClpX-ClpP complexes. 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. In the presence of ATP, binds to ClpA or ClpX subunits (a hexameric ring). Ref.12 Ref.13 Ref.14 Ref.15 Ref.16

Subcellular location

Cytoplasm HAMAP-Rule MF_00444.

Induction

By heat shock. Part of the clpP-clpX operon. Ref.7 Ref.14

Domain

The N-terminus (residues 17-34) interact with ClpA and ClpX. Ref.13

Miscellaneous

Acyldepsipeptide antibiotics bind in the ClpA or ClpX binding-sites, rendering the enzyme ATP-independent and indiscriminate, thus killing cells (Ref.15).

Sequence similarities

Belongs to the peptidase S14 family.

Biophysicochemical properties

Kinetic parameters:

KM=4.4 mM for N-succinyl-Leu-Tyr-7-amino-4-methyl-coumarin (N-succinyl-Leu-Tyr-AMC) (Ref.13) Ref.13 Ref.16

KM=1.0 mM for N-succinyl-Leu-Tyr-AMC (Ref.16)

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-370625,EBI-370625

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 1414 HAMAP-Rule MF_00444
PRO_0000268012
Chain15 – 207193ATP-dependent Clp protease proteolytic subunit HAMAP-Rule MF_00444
PRO_0000179551

Sites

Active site1111 Probable
Active site1361 Probable
Active site1851 Probable

Experimental info

Mutagenesis171V → A: No ClpA-ClpP, little ClpX-ClpP complex forms. Ref.13
Mutagenesis181P → A: Reduced processing, no ClpA-ClpP complex forms. Ref.13
Mutagenesis191M → A: No ClpA-ClpP, little ClpX-ClpP complex forms. Ref.13
Mutagenesis201V → A: No ClpA-ClpP or ClpX-ClpP complex forms. Ref.13
Mutagenesis211I → A: No ClpA-ClpP or ClpX-ClpP complex forms. Ref.13
Mutagenesis241T → A: No ClpA-ClpP, little ClpX-ClpP complex forms. Ref.13
Mutagenesis271G → A: No ClpA-ClpP, little ClpX-ClpP complex forms. Ref.13
Mutagenesis321D → A: No ClpA-ClpP or ClpX-ClpP complex forms. Ref.13
Mutagenesis331I → A: No ClpA-ClpP or ClpX-ClpP complex forms. Ref.13
Mutagenesis341Y → A: No ClpA-ClpP or ClpX-ClpP complex forms. Ref.13
Mutagenesis1261F → A: Little ClpA-ClpP or ClpX-ClpP complex forms. Ref.13
Mutagenesis1851D → A: Loss of protease activity, forms ClpA-ClpP complex. Ref.13

Secondary structure

.................................... 207
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A6G7 [UniParc].

Last modified March 29, 2005. Version 1.
Checksum: A7843D036C8CB3C2

FASTA20723,187
        10         20         30         40         50         60 
MSYSGERDNF APHMALVPMV IEQTSRGERS FDIYSRLLKE RVIFLTGQVE DHMANLIVAQ 

        70         80         90        100        110        120 
MLFLEAENPE KDIYLYINSP GGVITAGMSI YDTMQFIKPD VSTICMGQAA SMGAFLLTAG 

       130        140        150        160        170        180 
AKGKRFCLPN SRVMIHQPLG GYQGQATDIE IHAREILKVK GRMNELMALH TGQSLEQIER 

       190        200 
DTERDRFLSA PEAVEYGLVD SILTHRN 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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 1.9A 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05534 Genomic DNA. Translation: AAA23588.1.
U82664 Genomic DNA. Translation: AAB40193.1.
U00096 Genomic DNA. Translation: AAC73540.1.
AP009048 Genomic DNA. Translation: BAE76217.1.
PIRB36575.
RefSeqNP_414971.1. NC_000913.3.
YP_488729.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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/b15-207[»]
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[»]
ProteinModelPortalP0A6G7.
SMRP0A6G7. Positions 16-207.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-31838N.
IntActP0A6G7. 67 interactions.
STRING511145.b0437.

2D gel databases

SWISS-2DPAGEP0A6G7.

Proteomic databases

PaxDbP0A6G7.
PRIDEP0A6G7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73540; AAC73540; b0437.
BAE76217; BAE76217; BAE76217.
GeneID12931742.
945082.
KEGGecj:Y75_p0425.
eco:b0437.
PATRIC32116027. VBIEscCol129921_0455.

Organism-specific databases

EchoBASEEB0156.
EcoGeneEG10158. clpP.

Phylogenomic databases

eggNOGCOG0740.
HOGENOMHOG000285833.
KOK01358.
OMAANLIIAQ.
OrthoDBEOG6Z3KQ0.
PhylomeDBP0A6G7.
ProtClustDBPRK00277.

Enzyme and pathway databases

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

Gene expression databases

GenevestigatorP0A6G7.

Family and domain databases

HAMAPMF_00444. ClpP.
InterProIPR001907. ClpP.
IPR023562. ClpP/TepA.
IPR018215. ClpP_AS.
[Graphical view]
PANTHERPTHR10381. PTHR10381. 1 hit.
PfamPF00574. CLP_protease. 1 hit.
[Graphical view]
PRINTSPR00127. CLPPROTEASEP.
TIGRFAMsTIGR00493. clpP. 1 hit.
PROSITEPS00382. CLP_PROTEASE_HIS. 1 hit.
PS00381. CLP_PROTEASE_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A6G7.
PROP0A6G7.

Entry information

Entry nameCLPP_ECOLI
AccessionPrimary (citable) accession number: P0A6G7
Secondary accession number(s): P19245, Q2MBY9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 29, 2005
Last modified: April 16, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene