ECOLI:CLPX

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	clpX (ECO:0000255 with HAMAP-Rule:MF_00175) (synonyms: lopC)
Protein Name(s)	ATP-dependent Clp protease ATP-binding subunit ClpX (ECO:0000255 with HAMAP-Rule:MF_00175) ATP-dependent unfoldase ClpX
External Links
UniProt	P0A6H1
EMBL	L18867 Z23278 U82664 U00096 AP009048
PIR	A48709
RefSeq	NP_414972.1 YP_488730.1
PDB	1OVX 2DS5 2DS6 2DS7 2DS8 3HTE 3HWS 4I34 4I4L 4I5O 4I63 4I81 4I9K
PDBsum	1OVX 2DS5 2DS6 2DS7 2DS8 3HTE 3HWS 4I34 4I4L 4I5O 4I63 4I81 4I9K
ProteinModelPortal	P0A6H1
SMR	P0A6H1
DIP	DIP-35907N
IntAct	P0A6H1
STRING	511145.b0438
PaxDb	P0A6H1
PRIDE	P0A6H1
EnsemblBacteria	AAC73541 BAE76218
GeneID	12931741 945083
KEGG	ecj:Y75_p0426 eco:b0438
PATRIC	32116029
EchoBASE	EB0157
EcoGene	EG10159
eggNOG	COG1219
HOGENOM	HOG000010093
InParanoid	P0A6H1
KO	K03544
OMA	ILLDIMY
OrthoDB	EOG625JZK
PhylomeDB	P0A6H1
BioCyc	EcoCyc:EG10159-MONOMER ECOL316407:JW0428-MONOMER MetaCyc:EG10159-MONOMER
EvolutionaryTrace	P0A6H1
PRO	PR:P0A6H1
Proteomes	UP000000318 UP000000625
Genevestigator	P0A6H1
GO	GO:0005524 GO:0004176 GO:0042802 GO:0008270 GO:0006200 GO:0051301 GO:0006457 GO:0006508 GO:0016032
Gene3D	3.40.50.300
HAMAP	MF_00175
InterPro	IPR003593 IPR003959 IPR019489 IPR004487 IPR027417 IPR010603
Pfam	PF07724 PF10431 PF06689
SMART	SM00382 SM01086 SM00994
SUPFAM	SSF52540
TIGRFAMs	TIGR00382

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0004176	ATP-dependent peptidase activity	PMID:8226769^[1]	ECO:0000314			F	Figure 7 and 9 show degradation of the lamba O protein by the ClpXP protease, being completely dependent on the presence of ATP, whereas table IV shows results for several nucleotides tested as energy source. The data demonstrated the ATP specificity of this protease.	complete CACAO 4150
	GO:0009408	response to heat	PMID:21317324^[2]	ECO:0000315			P	Fig 1A depletion of clpX surpresses temperature-sensitive filamentation in cells causing them to be shorter.	complete CACAO 4531
	GO:0051301	cell division	PMID:21317324^[2]	ECO:0000316		UniProtKB:P0A9A6	P	Fig 1	complete CACAO 6785
	GO:0043335	protein unfolding	PMID:21529717^[3]	ECO:0000314			P	Figure 4 - ClpX unfolds GFP.	complete CACAO 9068
	GO:0004176	ATP-dependent peptidase activity	PMID:9573050^[4]	ECO:0000314			F	Figure 4	complete CACAO 9069
	GO:0016887	ATPase activity	PMID:11278349^[5]	ECO:0000314			F	table 2	complete CACAO 9612
part_of	GO:0009376	HslUV protease complex	PMID:14536075^[6]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0002020	protease binding	PMID:14536075^[6]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0A6G7	F	Seeded From UniProt	complete
enables	GO:0097718	disordered domain specific binding	PMID:14536075^[6]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0AFZ3	F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:14536075^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0016887	ATPase activity	PMID:14536075^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0030164	protein denaturation	PMID:14536075^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0016887	ATPase activity	PMID:11278349^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004176	ATP-dependent peptidase activity	PMID:9573050^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0043335	protein unfolding	PMID:21529717^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0051301	cell division	PMID:21317324^[2]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P0A9A6	P	Seeded From UniProt	complete
involved_in	GO:0051301	cell division	PMID:21317324^[2]	ECO:0000316	genetic interaction evidence used in manual assertion		P	Seeded From UniProt	Missing: with/from
enables	GO:0004176	ATP-dependent peptidase activity	PMID:8226769^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0051301	cell division	PMID:21873635^[7]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10159 PANTHER:PTN000137358 UniProtKB:P9WPB9	P	Seeded From UniProt	complete
involved_in	GO:0030163	protein catabolic process	PMID:21873635^[7]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000137292 UniProtKB:P50866	P	Seeded From UniProt	complete
part_of	GO:0005759	mitochondrial matrix	PMID:21873635^[7]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000137292 SGD:S000000431 TAIR:locus:2154257 UniProtKB:O76031	C	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:21873635^[7]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10159 MGI:MGI:1346017 PANTHER:PTN000137292 SGD:S000000431	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:EG10159 PANTHER:PTN000137292 UniProtKB:O76031	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:25866879^[8]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0A6H1	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:24561554^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0A6H1	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:23622246^[10]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0A6H1	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:19914167^[11]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0A6H1	F	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:18304323^[12]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:15911532^[13]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:9575205^[14]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0004176	P	Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0004176	P	Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0004176	P	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR003959 InterPro:IPR004487	F	Seeded From UniProt	complete
involved_in	GO:0006457	protein folding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004487	P	Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR010603	F	Seeded From UniProt	complete
enables	GO:0046983	protein dimerization activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR010603	F	Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004487	F	Seeded From UniProt	complete
involved_in	GO:0006457	protein folding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000001454	P	Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000001454	F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000001454	F	Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F	Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F	Seeded From UniProt	complete
involved_in	GO:0016032	viral process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0945	P	Seeded From UniProt	complete
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Notes

References

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

↑ ^1.0 ^1.1 Wojtkowiak, D et al. (1993) Isolation and characterization of ClpX, a new ATP-dependent specificity component of the Clp protease of Escherichia coli. J. Biol. Chem. 268 22609-17 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 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
↑ ^3.0 ^3.1 Maillard, RA et al. (2011) ClpX(P) generates mechanical force to unfold and translocate its protein substrates. Cell 145 459-69 PubMed GONUTS page
↑ ^4.0 ^4.1 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
↑ ^5.0 ^5.1 Banecki, B et al. (2001) Structure-function analysis of the zinc-binding region of the Clpx molecular chaperone. J. Biol. Chem. 276 18843-8 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 ^6.3 ^6.4 ^6.5 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
↑ ^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
↑ Stinson, BM et al. (2015) Subunit asymmetry and roles of conformational switching in the hexameric AAA+ ring of ClpX. Nat. Struct. Mol. Biol. 22 411-6 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
↑ Stinson, BM et al. (2013) Nucleotide binding and conformational switching in the hexameric ring of a AAA+ machine. Cell 153 628-39 PubMed GONUTS page
↑ Glynn, SE et al. (2009) Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine. Cell 139 744-56 PubMed GONUTS page
↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
↑ Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page
↑ Grimaud, R et al. (1998) Enzymatic and structural similarities between the Escherichia coli ATP-dependent proteases, ClpXP and ClpAP. J. Biol. Chem. 273 12476-81 PubMed GONUTS page

[PMID:8226769-1] 1.0 ^1.1 Wojtkowiak, D et al. (1993) Isolation and characterization of ClpX, a new ATP-dependent specificity component of the Clp protease of Escherichia coli. J. Biol. Chem. 268 22609-17 PubMed GONUTS page

[PMID:21317324-2] 2.0 ^2.1 ^2.2 ^2.3 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:21529717-3] 3.0 ^3.1 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:9573050-4] 4.0 ^4.1 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:11278349-5] 5.0 ^5.1 Banecki, B et al. (2001) Structure-function analysis of the zinc-binding region of the Clpx molecular chaperone. J. Biol. Chem. 276 18843-8 PubMed GONUTS page

[PMID:14536075-6] 6.0 ^6.1 ^6.2 ^6.3 ^6.4 ^6.5 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: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:25866879-8] Stinson, BM et al. (2015) Subunit asymmetry and roles of conformational switching in the hexameric AAA+ ring of ClpX. Nat. Struct. Mol. Biol. 22 411-6 PubMed GONUTS page

[PMID:24561554-9] Rajagopala, SV et al. (2014) The binary protein-protein interaction landscape of Escherichia coli. Nat. Biotechnol. 32 285-90 PubMed GONUTS page

[PMID:23622246-10] Stinson, BM et al. (2013) Nucleotide binding and conformational switching in the hexameric ring of a AAA+ machine. Cell 153 628-39 PubMed GONUTS page

[PMID:19914167-11] Glynn, SE et al. (2009) Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine. Cell 139 744-56 PubMed GONUTS page

[PMID:18304323-12] Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page

[PMID:15911532-13] Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page

[PMID:9575205-14] Grimaud, R et al. (1998) Enzymatic and structural similarities between the Escherichia coli ATP-dependent proteases, ClpXP and ClpAP. J. Biol. Chem. 273 12476-81 PubMed GONUTS page

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ECOLI:CLPX

Contents

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