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Entry version 147 (23 Feb 2022)
Sequence version 1 (29 Mar 2005)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

Miscellaneous

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>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 EC:3.4.21.92

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

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

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei111NucleophileCurated1
Active sitei136Curated1
Active sitei185Curated1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Protease, Serine protease
Biological processStress response

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG10158-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.4.21.92, 2026

Protein family/group databases

MEROPS protease database

More...
MEROPSi
S14.001

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:clpPUniRule annotation
Synonyms:lopP
Ordered Locus Names:b0437, JW0427
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3341578

Drug and drug target database

More...
DrugBanki
DB07571, N~2~-[(BENZYLOXY)CARBONYL]-N-[(1S,2S)-2-HYDROXY-1-(4-HYDROXYBENZYL)PROPYL]-L-LEUCINAMIDE

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_00002680121 – 141 PublicationAdd BLAST14
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000017955115 – 207ATP-dependent Clp protease proteolytic subunitAdd BLAST193

Keywords - PTMi

Zymogen

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0A6G7

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P0A6G7

PRoteomics IDEntifications database

More...
PRIDEi
P0A6G7

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...
SWISS-2DPAGEi
P0A6G7

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

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

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4260736, 465 interactors
849471, 1 interactor

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-3175, Endopeptidase ClpAP complex
CPX-3176, Endopeptidase ClpXP complex
CPX-3178, Endopeptidase ClpP complex

Database of interacting proteins

More...
DIPi
DIP-31838N

Protein interaction database and analysis system

More...
IntActi
P0A6G7, 68 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b0437

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P0A6G7

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1207
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P0A6G7

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P0A6G7

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peptidase S14 family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG0740, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_058707_3_2_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0A6G7

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0A6G7

Family and domain databases

Conserved Domains Database

More...
CDDi
cd07017, S14_ClpP_2, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00444, ClpP, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001907, ClpP
IPR029045, ClpP/crotonase-like_dom_sf
IPR023562, ClpP/TepA
IPR033135, ClpP_His_AS
IPR018215, ClpP_Ser_AS

The PANTHER Classification System

More...
PANTHERi
PTHR10381, PTHR10381, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00574, CLP_protease, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00127, CLPPROTEASEP

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52096, SSF52096, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00493, clpP, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00382, CLP_PROTEASE_HIS, 1 hit
PS00381, CLP_PROTEASE_SER, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iA7843D036C8CB3C2
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

Protein sequence database of the Protein Information Resource

More...
PIRi
B36575

NCBI Reference Sequences

More...
RefSeqi
NP_414971.1, NC_000913.3
WP_000122253.1, NZ_STEB01000007.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC73540; AAC73540; b0437
BAE76217; BAE76217; BAE76217

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
67416488
945082

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW0427
eco:b0437

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.1839

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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_STEB01000007.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
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[»]
6NB1X-ray1.90A/B/C/D/E/F/G/H/I/J/K/L/M/N1-207[»]
6PO1electron microscopy4.20H/I/J/K/L/M/N1-207[»]
6PO3electron microscopy4.28H/I/J/K/L/M/N1-207[»]
6PODelectron microscopy4.05H/I/J/K/L/M/N1-207[»]
6POSelectron microscopy4.12H/I/J/K/L/M/N1-207[»]
6PPEelectron microscopy3.19A/B/C/D/E/F/G/H/I/J/K/L/M/N16-207[»]
6UQEelectron microscopy3.00G/H/I/J/K/L/M/N/O/P/Q/R/S/T15-206[»]
6UQOelectron microscopy3.10G/H/I/J/K/L/M/N/O/P/Q/R/S/T15-206[»]
6W1Zelectron microscopy2.70G/H/I/J/K/L/M/N/O/P/Q/R/S/T1-207[»]
6W20electron microscopy3.00G/H/I/J/K/L/M/N/O/P/Q/R/S/T1-207[»]
6W21electron microscopy3.30G/H/I/J/K/L/M/N/O/P/Q/R/S/T1-207[»]
6WR2electron microscopy2.88H/I/J/K/L/M/N/h/i/j/k/l/m/n16-207[»]
6WRFelectron microscopy3.14H/I/J/K/L/M/N16-207[»]
6WSGelectron microscopy3.16H/I/J/K/L/M/N16-207[»]
SMRiP0A6G7
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4260736, 465 interactors
849471, 1 interactor
ComplexPortaliCPX-3175, Endopeptidase ClpAP complex
CPX-3176, Endopeptidase ClpXP complex
CPX-3178, Endopeptidase ClpP complex
DIPiDIP-31838N
IntActiP0A6G7, 68 interactors
STRINGi511145.b0437

Chemistry databases

BindingDBiP0A6G7
ChEMBLiCHEMBL3341578
DrugBankiDB07571, N~2~-[(BENZYLOXY)CARBONYL]-N-[(1S,2S)-2-HYDROXY-1-(4-HYDROXYBENZYL)PROPYL]-L-LEUCINAMIDE

Protein family/group databases

MEROPSiS14.001

2D gel databases

SWISS-2DPAGEiP0A6G7

Proteomic databases

jPOSTiP0A6G7
PaxDbiP0A6G7
PRIDEiP0A6G7

Genome annotation databases

EnsemblBacteriaiAAC73540; AAC73540; b0437
BAE76217; BAE76217; BAE76217
GeneIDi67416488
945082
KEGGiecj:JW0427
eco:b0437
PATRICifig|1411691.4.peg.1839

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

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EchoBASEi
EB0156

Phylogenomic databases

eggNOGiCOG0740, Bacteria
HOGENOMiCLU_058707_3_2_6
InParanoidiP0A6G7
PhylomeDBiP0A6G7

Enzyme and pathway databases

BioCyciEcoCyc:EG10158-MONOMER
BRENDAi3.4.21.92, 2026

Miscellaneous databases

EvolutionaryTraceiP0A6G7

Protein Ontology

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PROi
PR:P0A6G7

Family and domain databases

CDDicd07017, S14_ClpP_2, 1 hit
HAMAPiMF_00444, ClpP, 1 hit
InterProiView protein in InterPro
IPR001907, ClpP
IPR029045, ClpP/crotonase-like_dom_sf
IPR023562, ClpP/TepA
IPR033135, ClpP_His_AS
IPR018215, ClpP_Ser_AS
PANTHERiPTHR10381, PTHR10381, 1 hit
PfamiView protein in Pfam
PF00574, CLP_protease, 1 hit
PRINTSiPR00127, CLPPROTEASEP
SUPFAMiSSF52096, SSF52096, 1 hit
TIGRFAMsiTIGR00493, clpP, 1 hit
PROSITEiView protein in PROSITE
PS00382, CLP_PROTEASE_HIS, 1 hit
PS00381, CLP_PROTEASE_SER, 1 hit

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCLPP_ECOLI
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0A6G7
Secondary accession number(s): P19245, Q2MBY9
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 29, 2005
Last modified: February 23, 2022
This is version 147 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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