ECOLI:DEGP

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	degP (synonyms: htrA, ptd)
Protein Name(s)	Periplasmic serine endoprotease DegP Heat shock protein DegP Protease Do
External Links
UniProt	P0C0V0
EMBL	M36536 X12457 U70214 U00096 AP009048 M29955 M31772
PIR	S45229
RefSeq	NP_414703.1 YP_488464.1
PDB	1KY9 2ZLE 3CS0 3MH4 3MH5 3MH6 3MH7 3OTP 3OU0 4A8D
PDBsum	1KY9 2ZLE 3CS0 3MH4 3MH5 3MH6 3MH7 3OTP 3OU0 4A8D
ProteinModelPortal	P0C0V0
SMR	P0C0V0
DIP	DIP-46256N
IntAct	P0C0V0
MINT	MINT-1302319
STRING	511145.b0161
MEROPS	S01.273
SWISS-2DPAGE	P0C0V0
PaxDb	P0C0V0
PRIDE	P0C0V0
EnsemblBacteria	AAC73272 BAB96738
GeneID	12932000 947139
KEGG	ecj:Y75_p0158 eco:b0161
PATRIC	32115431
EchoBASE	EB0458
EcoGene	EG10463
eggNOG	COG0265
HOGENOM	HOG000223642
InParanoid	P0C0V0
KO	K04771
OMA	ATKIQVQ
OrthoDB	EOG61ZTDN
PhylomeDB	P0C0V0
BioCyc	EcoCyc:EG10463-MONOMER ECOL316407:JW0157-MONOMER MetaCyc:EG10463-MONOMER RETL1328306-WGS:GSTH-1743-MONOMER
EvolutionaryTrace	P0C0V0
PRO	PR:P0C0V0
Proteomes	UP000000318 UP000000625
Genevestigator	P0C0V0
GO	GO:0030288 GO:0005886 GO:0042802 GO:0004252 GO:0006515 GO:0006457 GO:0006508 GO:0006979 GO:0009266
Gene3D	2.30.42.10
InterPro	IPR001478 IPR011782 IPR001940 IPR009003
Pfam	PF00595
PRINTS	PR00834
SMART	SM00228
SUPFAM	SSF50156 SSF50494
TIGRFAMs	TIGR02037
PROSITE	PS50106

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
enables	GO:0042802	identical protein binding	PMID:24373769^[1]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0C0V0	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:21893291^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0C0V0	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:21458668^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0C0V0	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:20581826^[4]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0C0V0	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:20581825^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0C0V0	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:18697939^[6]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0C0V0	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:18496527^[7]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0C0V0	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:11919638^[8]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0C0V0	F	Seeded From UniProt	complete
part_of	GO:0030288	outer membrane-bounded periplasmic space	PMID:10517331^[9]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0009266	response to temperature stimulus	PMID:10319814^[10]	ECO:0000270	expression pattern evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006979	response to oxidative stress	PMID:10517331^[9]	ECO:0000270	expression pattern evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006515	protein quality control for misfolded or incompletely synthesized proteins	PMID:10319814^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	PMID:2180903^[11]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006457	protein folding	PMID:10319814^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0004252	serine-type endopeptidase activity	PMID:19255437^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004252	serine-type endopeptidase activity	PMID:2180903^[11]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0061077	chaperone-mediated protein folding	PMID:18496527^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0061077	chaperone-mediated protein folding	PMID:10319814^[10]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:11919638^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0030288	outer membrane-bounded periplasmic space	PMID:9083020^[13]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0030288	outer membrane-bounded periplasmic space	PMID:10417648^[14]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0009408	response to heat	PMID:7557477^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0009408	response to heat	PMID:2537822^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0008236	serine-type peptidase activity	PMID:7557477^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008236	serine-type peptidase activity	PMID:9041651^[17]	ECO:0000255	match to sequence model evidence used in manual assertion		F	Seeded From UniProt	Missing: with/from
enables	GO:0008233	peptidase activity	PMID:19255437^[12]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008233	peptidase activity	PMID:18505836^[18]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006515	protein quality control for misfolded or incompletely synthesized proteins	PMID:18505836^[18]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006515	protein quality control for misfolded or incompletely synthesized proteins	PMID:10319814^[10]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	PMID:3278319^[19]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	PMID:18505836^[18]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:9083020^[13]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0004252	serine-type endopeptidase activity	PMID:2180903^[11]	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:IPR001940 InterPro:IPR011782	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:IPR001940 InterPro:IPR011782	P	Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000037 GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0997 UniProtKB-KW:KW-1003 UniProtKB-SubCell:SL-0037	C	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
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
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C	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
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
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Notes

References

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

↑ Thompson, NJ et al. (2014) Substrate occupancy at the onset of oligomeric transitions of DegP. Structure 22 281-90 PubMed GONUTS page
↑ Bai, XC et al. (2011) Characterization of the structure and function of Escherichia coli DegQ as a representative of the DegQ-like proteases of bacterial HtrA family proteins. Structure 19 1328-37 PubMed GONUTS page
↑ Kim, S et al. (2011) Covalent linkage of distinct substrate degrons controls assembly and disassembly of DegP proteolytic cages. Cell 145 67-78 PubMed GONUTS page
↑ Merdanovic, M et al. (2010) Determinants of structural and functional plasticity of a widely conserved protease chaperone complex. Nat. Struct. Mol. Biol. 17 837-43 PubMed GONUTS page
↑ Krojer, T et al. (2010) HtrA proteases have a conserved activation mechanism that can be triggered by distinct molecular cues. Nat. Struct. Mol. Biol. 17 844-52 PubMed GONUTS page
↑ Jiang, J et al. (2008) Activation of DegP chaperone-protease via formation of large cage-like oligomers upon binding to substrate proteins. Proc. Natl. Acad. Sci. U.S.A. 105 11939-44 PubMed GONUTS page
↑ ^7.0 ^7.1 Krojer, T et al. (2008) Structural basis for the regulated protease and chaperone function of DegP. Nature 453 885-90 PubMed GONUTS page
↑ ^8.0 ^8.1 Krojer, T et al. (2002) Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine. Nature 416 455-9 PubMed GONUTS page
↑ ^9.0 ^9.1 Skórko-Glonek, J et al. (1999) The Escherichia coli heat shock protease HtrA participates in defense against oxidative stress. Mol. Gen. Genet. 262 342-50 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 ^10.3 ^10.4 Spiess, C et al. (1999) A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein. Cell 97 339-47 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 Lipinska, B et al. (1990) The HtrA (DegP) protein, essential for Escherichia coli survival at high temperatures, is an endopeptidase. J. Bacteriol. 172 1791-7 PubMed GONUTS page
↑ ^12.0 ^12.1 Shen, QT et al. (2009) Bowl-shaped oligomeric structures on membranes as DegP's new functional forms in protein quality control. Proc. Natl. Acad. Sci. U.S.A. 106 4858-63 PubMed GONUTS page
↑ ^13.0 ^13.1 Skórko-Glonek, J et al. (1997) HtrA heat shock protease interacts with phospholipid membranes and undergoes conformational changes. J. Biol. Chem. 272 8974-82 PubMed GONUTS page
↑ Sassoon, N et al. (1999) PDZ domains determine the native oligomeric structure of the DegP (HtrA) protease. Mol. Microbiol. 33 583-9 PubMed GONUTS page
↑ ^15.0 ^15.1 Skórko-Glonek, J et al. (1995) Site-directed mutagenesis of the HtrA (DegP) serine protease, whose proteolytic activity is indispensable for Escherichia coli survival at elevated temperatures. Gene 163 47-52 PubMed GONUTS page
↑ Lipinska, B et al. (1989) Identification, characterization, and mapping of the Escherichia coli htrA gene, whose product is essential for bacterial growth only at elevated temperatures. J. Bacteriol. 171 1574-84 PubMed GONUTS page
↑ Ponting, CP (1997) Evidence for PDZ domains in bacteria, yeast, and plants. Protein Sci. 6 464-8 PubMed GONUTS page
↑ ^18.0 ^18.1 ^18.2 Krojer, T et al. (2008) Interplay of PDZ and protease domain of DegP ensures efficient elimination of misfolded proteins. Proc. Natl. Acad. Sci. U.S.A. 105 7702-7 PubMed GONUTS page
↑ Strauch, KL & Beckwith, J (1988) An Escherichia coli mutation preventing degradation of abnormal periplasmic proteins. Proc. Natl. Acad. Sci. U.S.A. 85 1576-80 PubMed GONUTS page

[PMID:24373769-1] Thompson, NJ et al. (2014) Substrate occupancy at the onset of oligomeric transitions of DegP. Structure 22 281-90 PubMed GONUTS page

[PMID:21893291-2] Bai, XC et al. (2011) Characterization of the structure and function of Escherichia coli DegQ as a representative of the DegQ-like proteases of bacterial HtrA family proteins. Structure 19 1328-37 PubMed GONUTS page

[PMID:21458668-3] Kim, S et al. (2011) Covalent linkage of distinct substrate degrons controls assembly and disassembly of DegP proteolytic cages. Cell 145 67-78 PubMed GONUTS page

[PMID:20581826-4] Merdanovic, M et al. (2010) Determinants of structural and functional plasticity of a widely conserved protease chaperone complex. Nat. Struct. Mol. Biol. 17 837-43 PubMed GONUTS page

[PMID:20581825-5] Krojer, T et al. (2010) HtrA proteases have a conserved activation mechanism that can be triggered by distinct molecular cues. Nat. Struct. Mol. Biol. 17 844-52 PubMed GONUTS page

[PMID:18697939-6] Jiang, J et al. (2008) Activation of DegP chaperone-protease via formation of large cage-like oligomers upon binding to substrate proteins. Proc. Natl. Acad. Sci. U.S.A. 105 11939-44 PubMed GONUTS page

[PMID:18496527-7] 7.0 ^7.1 Krojer, T et al. (2008) Structural basis for the regulated protease and chaperone function of DegP. Nature 453 885-90 PubMed GONUTS page

[PMID:11919638-8] 8.0 ^8.1 Krojer, T et al. (2002) Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine. Nature 416 455-9 PubMed GONUTS page

[PMID:10517331-9] 9.0 ^9.1 Skórko-Glonek, J et al. (1999) The Escherichia coli heat shock protease HtrA participates in defense against oxidative stress. Mol. Gen. Genet. 262 342-50 PubMed GONUTS page

[PMID:10319814-10] 10.0 ^10.1 ^10.2 ^10.3 ^10.4 Spiess, C et al. (1999) A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein. Cell 97 339-47 PubMed GONUTS page

[PMID:2180903-11] 11.0 ^11.1 ^11.2 Lipinska, B et al. (1990) The HtrA (DegP) protein, essential for Escherichia coli survival at high temperatures, is an endopeptidase. J. Bacteriol. 172 1791-7 PubMed GONUTS page

[PMID:19255437-12] 12.0 ^12.1 Shen, QT et al. (2009) Bowl-shaped oligomeric structures on membranes as DegP's new functional forms in protein quality control. Proc. Natl. Acad. Sci. U.S.A. 106 4858-63 PubMed GONUTS page

[PMID:9083020-13] 13.0 ^13.1 Skórko-Glonek, J et al. (1997) HtrA heat shock protease interacts with phospholipid membranes and undergoes conformational changes. J. Biol. Chem. 272 8974-82 PubMed GONUTS page

[PMID:10417648-14] Sassoon, N et al. (1999) PDZ domains determine the native oligomeric structure of the DegP (HtrA) protease. Mol. Microbiol. 33 583-9 PubMed GONUTS page

[PMID:7557477-15] 15.0 ^15.1 Skórko-Glonek, J et al. (1995) Site-directed mutagenesis of the HtrA (DegP) serine protease, whose proteolytic activity is indispensable for Escherichia coli survival at elevated temperatures. Gene 163 47-52 PubMed GONUTS page

[PMID:2537822-16] Lipinska, B et al. (1989) Identification, characterization, and mapping of the Escherichia coli htrA gene, whose product is essential for bacterial growth only at elevated temperatures. J. Bacteriol. 171 1574-84 PubMed GONUTS page

[PMID:9041651-17] Ponting, CP (1997) Evidence for PDZ domains in bacteria, yeast, and plants. Protein Sci. 6 464-8 PubMed GONUTS page

[PMID:18505836-18] 18.0 ^18.1 ^18.2 Krojer, T et al. (2008) Interplay of PDZ and protease domain of DegP ensures efficient elimination of misfolded proteins. Proc. Natl. Acad. Sci. U.S.A. 105 7702-7 PubMed GONUTS page

[PMID:3278319-19] Strauch, KL & Beckwith, J (1988) An Escherichia coli mutation preventing degradation of abnormal periplasmic proteins. Proc. Natl. Acad. Sci. U.S.A. 85 1576-80 PubMed GONUTS page

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ECOLI:DEGP

Contents

Annotations

Notes

References

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