ECOLI:CLPP

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	clpP (ECO:0000255 with HAMAP-Rule:MF_00444) (synonyms: lopP)
Protein Name(s)	ATP-dependent Clp protease proteolytic subunit (ECO:0000255 with HAMAP-Rule:MF_00444) Caseinolytic protease Endopeptidase Clp (ECO:0000255 with HAMAP-Rule:MF_00444) Heat shock protein F21.5 Protease Ti
External Links
UniProt	P0A6G7
EMBL	J05534 U82664 U00096 AP009048
PIR	B36575
RefSeq	NP_414971.1 YP_488729.1
PDB	1TYF 1YG6 1YG8 2FZS 3HLN 3MT6
PDBsum	1TYF 1YG6 1YG8 2FZS 3HLN 3MT6
ProteinModelPortal	P0A6G7
SMR	P0A6G7
DIP	DIP-31838N
IntAct	P0A6G7
STRING	511145.b0437
SWISS-2DPAGE	P0A6G7
PaxDb	P0A6G7
PRIDE	P0A6G7
EnsemblBacteria	AAC73540 BAE76217
GeneID	12931742 945082
KEGG	ecj:Y75_p0425 eco:b0437
PATRIC	32116027
EchoBASE	EB0156
EcoGene	EG10158
eggNOG	COG0740
HOGENOM	HOG000285833
InParanoid	P0A6G7
KO	K01358
OMA	ARMNELM
OrthoDB	EOG6Z3KQ0
PhylomeDB	P0A6G7
BioCyc	EcoCyc:EG10158-MONOMER ECOL316407:JW0427-MONOMER MetaCyc:EG10158-MONOMER
EvolutionaryTrace	P0A6G7
PRO	PR:P0A6G7
Proteomes	UP000000318 UP000000625
Genevestigator	P0A6G7
GO	GO:0005829 GO:0016020 GO:0042802 GO:0004252 GO:0008236 GO:0006515 GO:0009408 GO:0009266
Gene3D	3.90.226.10
HAMAP	MF_00444
InterPro	IPR001907 IPR029045 IPR023562 IPR018215
PANTHER	PTHR10381
Pfam	PF00574
PRINTS	PR00127
SUPFAM	SSF52096
TIGRFAMs	TIGR00493
PROSITE	PS00382 PS00381

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0009408	response to heat	PMID:21317324^[1]	ECO:0000315			P	Fig 1A deletion of clpP suppresses temperature-sensitive filamentation cells causing the cells to become elongated.	complete CACAO 4525
	GO:0004176	ATP-dependent peptidase activity	PMID:9573050^[2]	ECO:0000314			F	Figure 4 - ClpP complexes with both ClpA and ClpX to degrade SsrA-tagged proteins in vitro.	complete CACAO 9066
	GO:0010498	proteasomal protein catabolic process	PMID:9573050^[2]	ECO:0000315			P	Figure 5 - Shows ClpP(-) strains degrade the tagged proteins more slowly than wildtype, in vivo.	complete CACAO 9067
	GO:0043335	protein unfolding	PMID:21529717^[3]	ECO:0000314			P	Figure 4 - ClpP complexes with ClpX to unfold GFP during proteolysis.	complete CACAO 9070
	GO:0043068	positive regulation of programmed cell death	PMID:11222603^[4]	ECO:0000315			P	Fig (1a) shows that more E.coli cells with a disrupted clpP gene survived treatment with the antibiotics rifampin, chloramphenicol, and spectinomycin than wild type cells.	complete CACAO 13142
part_of	GO:0009376	HslUV protease complex	PMID:14536075^[5]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0051117	ATPase binding	PMID:14536075^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0A6H1	F	Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	PMID:14536075^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0004176	ATP-dependent peptidase activity	PMID:14536075^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0010498	proteasomal protein catabolic process	PMID:9573050^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0004176	ATP-dependent peptidase activity	PMID:9573050^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:16858726^[6]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:16858726^[6]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0051117	ATPase binding	PMID:21873635^[7]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10158 PANTHER:PTN000043558	F	Seeded From UniProt	complete
part_of	GO:0009368	endopeptidase Clp complex	PMID:21873635^[7]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000043558 TAIR:locus:2031070 TAIR:locus:2033344 TAIR:locus:2034625 TAIR:locus:2163538 TAIR:locus:2178282 TAIR:locus:2196120 UniProtKB:Q16740 UniProtKB:Q9SAA2	C	Seeded From UniProt	complete
involved_in	GO:0006515	protein quality control for misfolded or incompletely synthesized proteins	PMID:21873635^[7]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10158 PANTHER:PTN000043558	P	Seeded From UniProt	complete
enables	GO:0004252	serine-type endopeptidase activity	PMID:21873635^[7]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000043558 UniProtKB:Q16740 WB:WBGene00014172	F	Seeded From UniProt	complete
enables	GO:0004176	ATP-dependent peptidase activity	PMID:21873635^[7]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10158 PANTHER:PTN000043558 UniProtKB:P80244	F	Seeded From UniProt	complete
involved_in	GO:0006515	protein quality control for misfolded or incompletely synthesized proteins	PMID:10754102^[8]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:24627523^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0A6G7	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:24561554^[10]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0A6G7	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:20637416^[11]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0A6G7	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:19368884^[12]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0A6G7	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:16858726^[6]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0A6G7	F	Seeded From UniProt	complete
involved_in	GO:0009408	response to heat	PMID:8349564^[13]	ECO:0000270	expression pattern evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:7623377^[14]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0A6G7	F	Seeded From UniProt	complete
involved_in	GO:0009314	response to radiation	PMID:27718375^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0009266	response to temperature stimulus	PMID:2211522^[16]	ECO:0000269	experimental evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0008236	serine-type peptidase activity	PMID:8407953^[17]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004252	serine-type endopeptidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001907	F	Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001907	P	Seeded From UniProt	complete
enables	GO:0004252	serine-type endopeptidase activity	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000089051	F	Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000089051	P	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000089051	C	Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F	Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0645	P	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C	Seeded From UniProt	complete
enables	GO:0008236	serine-type peptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0720	F	Seeded From UniProt	complete
enables	GO:0008233	peptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0645	F	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Camberg, JL et al. (2011) The interplay of ClpXP with the cell division machinery in Escherichia coli. J. Bacteriol. 193 1911-8 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 Gottesman, S et al. (1998) The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system. Genes Dev. 12 1338-47 PubMed GONUTS page
↑ Maillard, RA et al. (2011) ClpX(P) generates mechanical force to unfold and translocate its protein substrates. Cell 145 459-69 PubMed GONUTS page
↑ Sat, B et al. (2001) Programmed cell death in Escherichia coli: some antibiotics can trigger mazEF lethality. J. Bacteriol. 183 2041-5 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 Wah, DA et al. (2003) Flexible linkers leash the substrate binding domain of SspB to a peptide module that stabilizes delivery complexes with the AAA+ ClpXP protease. Mol. Cell 12 355-63 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 ^7.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Andresen, BS et al. (2000) Characterization of mouse Clpp protease cDNA, gene, and protein. Mamm. Genome 11 275-80 PubMed GONUTS page
↑ Häuser, R et al. (2014) A second-generation protein-protein interaction network of Helicobacter pylori. Mol. Cell Proteomics 13 1318-29 PubMed GONUTS page
↑ Rajagopala, SV et al. (2014) The binary protein-protein interaction landscape of Escherichia coli. Nat. Biotechnol. 32 285-90 PubMed GONUTS page
↑ Kimber, MS et al. (2010) Structural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations. Structure 18 798-808 PubMed GONUTS page
↑ Maglica, Z et al. (2009) Optimal efficiency of ClpAP and ClpXP chaperone-proteases is achieved by architectural symmetry. Structure 17 508-16 PubMed GONUTS page
↑ Chuang, SE & Blattner, FR (1993) Characterization of twenty-six new heat shock genes of Escherichia coli. J. Bacteriol. 175 5242-52 PubMed GONUTS page
↑ Kessel, M et al. (1995) Homology in structural organization between E. coli ClpAP protease and the eukaryotic 26 S proteasome. J. Mol. Biol. 250 587-94 PubMed GONUTS page
↑ Sargentini, NJ et al. () Screen for genes involved in radiation survival of Escherichia coli and construction of a reference database. Mutat. Res. 793-794 1-14 PubMed GONUTS page
↑ Kroh, HE & Simon, LD (1990) The ClpP component of Clp protease is the sigma 32-dependent heat shock protein F21.5. J. Bacteriol. 172 6026-34 PubMed GONUTS page
↑ Arribas, J & Castaño, JG (1993) A comparative study of the chymotrypsin-like activity of the rat liver multicatalytic proteinase and the ClpP from Escherichia coli. J. Biol. Chem. 268 21165-71 PubMed GONUTS page

[PMID:21317324-1] Camberg, JL et al. (2011) The interplay of ClpXP with the cell division machinery in Escherichia coli. J. Bacteriol. 193 1911-8 PubMed GONUTS page

[PMID:9573050-2] 2.0 ^2.1 ^2.2 ^2.3 Gottesman, S et al. (1998) The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system. Genes Dev. 12 1338-47 PubMed GONUTS page

[PMID:21529717-3] Maillard, RA et al. (2011) ClpX(P) generates mechanical force to unfold and translocate its protein substrates. Cell 145 459-69 PubMed GONUTS page

[PMID:11222603-4] Sat, B et al. (2001) Programmed cell death in Escherichia coli: some antibiotics can trigger mazEF lethality. J. Bacteriol. 183 2041-5 PubMed GONUTS page

[PMID:14536075-5] 5.0 ^5.1 ^5.2 ^5.3 Wah, DA et al. (2003) Flexible linkers leash the substrate binding domain of SspB to a peptide module that stabilizes delivery complexes with the AAA+ ClpXP protease. Mol. Cell 12 355-63 PubMed GONUTS page

[PMID:16858726-6] 6.0 ^6.1 ^6.2 Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page

[PMID:21873635-7] 7.0 ^7.1 ^7.2 ^7.3 ^7.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:10754102-8] Andresen, BS et al. (2000) Characterization of mouse Clpp protease cDNA, gene, and protein. Mamm. Genome 11 275-80 PubMed GONUTS page

[PMID:24627523-9] Häuser, R et al. (2014) A second-generation protein-protein interaction network of Helicobacter pylori. Mol. Cell Proteomics 13 1318-29 PubMed GONUTS page

[PMID:24561554-10] Rajagopala, SV et al. (2014) The binary protein-protein interaction landscape of Escherichia coli. Nat. Biotechnol. 32 285-90 PubMed GONUTS page

[PMID:20637416-11] Kimber, MS et al. (2010) Structural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations. Structure 18 798-808 PubMed GONUTS page

[PMID:19368884-12] Maglica, Z et al. (2009) Optimal efficiency of ClpAP and ClpXP chaperone-proteases is achieved by architectural symmetry. Structure 17 508-16 PubMed GONUTS page

[PMID:8349564-13] Chuang, SE & Blattner, FR (1993) Characterization of twenty-six new heat shock genes of Escherichia coli. J. Bacteriol. 175 5242-52 PubMed GONUTS page

[PMID:7623377-14] Kessel, M et al. (1995) Homology in structural organization between E. coli ClpAP protease and the eukaryotic 26 S proteasome. J. Mol. Biol. 250 587-94 PubMed GONUTS page

[PMID:27718375-15] Sargentini, NJ et al. () Screen for genes involved in radiation survival of Escherichia coli and construction of a reference database. Mutat. Res. 793-794 1-14 PubMed GONUTS page

[PMID:2211522-16] Kroh, HE & Simon, LD (1990) The ClpP component of Clp protease is the sigma 32-dependent heat shock protein F21.5. J. Bacteriol. 172 6026-34 PubMed GONUTS page

[PMID:8407953-17] Arribas, J & Castaño, JG (1993) A comparative study of the chymotrypsin-like activity of the rat liver multicatalytic proteinase and the ClpP from Escherichia coli. J. Biol. Chem. 268 21165-71 PubMed GONUTS page

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ECOLI:CLPP

Contents

Annotations

Notes

References

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