Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P0A6G7

- CLPP_ECOLI

UniProt

P0A6G7 - CLPP_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10158. clpP.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. membrane Source: UniProtKB
Complete GO annotation...

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
clpAP0ABH93EBI-370625,EBI-546140

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.
InParanoidiP0A6G7.
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

        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:
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.
InParanoidi P0A6G7.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 93 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