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Protein

Periplasmic serine endoprotease DegP

Gene

degP

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures (PubMed:10319814). Degrades transiently denatured and unfolded or misfolded proteins which accumulate in the periplasm following heat shock or other stress conditions (PubMed:16303867). DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids (PubMed:8830688). Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins (PubMed:8830688). Its proteolytic activity is essential for the survival of cells at elevated temperatures (PubMed:7557477). It can degrade IciA, Ada, casein, globin and PapA. DegP shares specificity with DegQ (PubMed:8830688). DegP is also involved in the biogenesis of partially folded outer-membrane proteins (OMP).8 Publications

Miscellaneous

DegP is indispensable for bacterial survival at temperatures above 42 degrees Celsius, however is also able to digest its natural substrates in a reducing environment at temperatures as low as 20 degrees Celsius.

Catalytic activityi

Acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-|-Val.1 Publication

Activity regulationi

Inhibited by diisopropylfluorophosphate (DFP).1 Publication

Temperature dependencei

Optimum temperature is around 55 degrees Celsius. In the range from 37 to 55 degrees Celsius, the proteolytic activity rapidly increases with temperature.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei58Substrate1
Active sitei131Charge relay system1 Publication1
Binding sitei131Substrate1
Active sitei161Charge relay system1 Publication1
Binding sitei161Substrate1
Active sitei236Charge relay system1 Publication1

GO - Molecular functioni

  • identical protein binding Source: EcoCyc
  • peptidase activity Source: EcoCyc
  • serine-type endopeptidase activity Source: EcoCyc
  • serine-type peptidase activity Source: EcoCyc

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Protease, Serine protease
Biological processStress response

Enzyme and pathway databases

BioCyciEcoCyc:EG10463-MONOMER
MetaCyc:EG10463-MONOMER
BRENDAi3.4.21.107 2026

Protein family/group databases

MEROPSiS01.273
MoonProtiP0C0V0

Names & Taxonomyi

Protein namesi
Recommended name:
Periplasmic serine endoprotease DegP (EC:3.4.21.1071 Publication)
Alternative name(s):
Heat shock protein DegP
Protease Do
Gene namesi
Name:degP
Synonyms:htrA, ptd
Ordered Locus Names:b0161, JW0157
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10463 degP

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Decreased induction of Cpx two-component regulatory system (PubMed:16166523). Increased accumulation of periplasmic accessory protein CpxP, increased accumulation and toxicity of overexpressed, misfolded periplasmic proteins (PubMed:16303867). Increased resistance to hydroxyurea, probably due to decreased degradation of misfolded proteins which eventually leads to decreased OH radical formation (PubMed:20005847).3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi131H → R: Loss of peptidase activity with no detectable changes in secondary structure. 1 Publication1
Mutagenesisi236S → A: Loss of peptidase activity with no detectable changes in secondary structure. 2 Publications1
Mutagenesisi254I → N: It does not affect the proteolytic activity. 1 Publication1
Mutagenesisi255L → N: Loss of proteolytic activity. 1 Publication1
Mutagenesisi258D → V: Increases the proteolytic activity. 1 Publication1
Mutagenesisi261N → I: Loss of proteolytic activity. 1 Publication1
Mutagenesisi262I → N: Stimulates the proteolytic activity at low temperatures (20-30 degrees Celsius), whereas at higher temperatures (above 35 degrees Celsius), the proteolytic activity is less efficient. 1 Publication1
Mutagenesisi264I → N: Loss of proteolytic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 262 PublicationsAdd BLAST26
ChainiPRO_000002692127 – 474Periplasmic serine endoprotease DegPAdd BLAST448

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi83 ↔ 951 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

EPDiP0C0V0
PaxDbiP0C0V0
PRIDEiP0C0V0

2D gel databases

SWISS-2DPAGEiP0C0V0

Expressioni

Inductioni

By heat shock (PubMed:3057437). Transcriptionally up-regulated by sigma-E factor and the Cpx two-component signal transduction pathway (PubMed:7883164, PubMed:9351822).3 Publications

Interactioni

Subunit structurei

DegP can reversibly switch between different oligomeric forms that represent inactive (6-mer) and active (12-and 24-mer) protease states. Substrate binding triggers the conversion of the resting DegP trimer and hexamer into catalytically active 12- and 24-mers. The conversion of 6-mer (DegP6) into 12-mer (DegP12) or 24-mer (DegP24) is crucial in regulating protease activity.7 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi4260994, 967 interactors
DIPiDIP-46256N
IntActiP0C0V0, 20 interactors
MINTiP0C0V0
STRINGi316385.ECDH10B_0141

Structurei

Secondary structure

1474
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP0C0V0
SMRiP0C0V0
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C0V0

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini280 – 371PDZ 1PROSITE-ProRule annotationAdd BLAST92
Domaini377 – 466PDZ 2PROSITE-ProRule annotationAdd BLAST90

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni234 – 236Substrate binding3
Regioni252 – 256Substrate binding5
Regioni291 – 295Substrate binding5

Sequence similaritiesi

Belongs to the peptidase S1C family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG4105C0H Bacteria
COG0265 LUCA
HOGENOMiHOG000223642
InParanoidiP0C0V0
KOiK04771
PhylomeDBiP0C0V0

Family and domain databases

InterProiView protein in InterPro
IPR001478 PDZ
IPR036034 PDZ_sf
IPR011782 Pept_S1C_Do
IPR009003 Peptidase_S1_PA
IPR001940 Peptidase_S1C
PfamiView protein in Pfam
PF00595 PDZ, 2 hits
PRINTSiPR00834 PROTEASES2C
SMARTiView protein in SMART
SM00228 PDZ, 2 hits
SUPFAMiSSF50156 SSF50156, 2 hits
SSF50494 SSF50494, 1 hit
TIGRFAMsiTIGR02037 degP_htrA_DO, 1 hit
PROSITEiView protein in PROSITE
PS50106 PDZ, 2 hits

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0C0V0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKKTTLALSA LALSLGLALS PLSATAAETS SATTAQQMPS LAPMLEKVMP
60 70 80 90 100
SVVSINVEGS TTVNTPRMPR NFQQFFGDDS PFCQEGSPFQ SSPFCQGGQG
110 120 130 140 150
GNGGGQQQKF MALGSGVIID ADKGYVVTNN HVVDNATVIK VQLSDGRKFD
160 170 180 190 200
AKMVGKDPRS DIALIQIQNP KNLTAIKMAD SDALRVGDYT VAIGNPFGLG
210 220 230 240 250
ETVTSGIVSA LGRSGLNAEN YENFIQTDAA INRGNSGGAL VNLNGELIGI
260 270 280 290 300
NTAILAPDGG NIGIGFAIPS NMVKNLTSQM VEYGQVKRGE LGIMGTELNS
310 320 330 340 350
ELAKAMKVDA QRGAFVSQVL PNSSAAKAGI KAGDVITSLN GKPISSFAAL
360 370 380 390 400
RAQVGTMPVG SKLTLGLLRD GKQVNVNLEL QQSSQNQVDS SSIFNGIEGA
410 420 430 440 450
EMSNKGKDQG VVVNNVKTGT PAAQIGLKKG DVIIGANQQA VKNIAELRKV
460 470
LDSKPSVLAL NIQRGDSTIY LLMQ
Length:474
Mass (Da):49,354
Last modified:December 20, 2005 - v1
Checksum:i5482E596F74B6D5F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti10A → R in AAA23994 (PubMed:3057437).Curated1
Sequence conflicti10A → R in AAA23680 (PubMed:2157212).Curated1
Sequence conflicti46E → Q in AAA23717 (PubMed:2165018).Curated1
Sequence conflicti192A → G in AAA23994 (PubMed:3057437).Curated1
Sequence conflicti192A → G in CAA30997 (PubMed:3057437).Curated1
Sequence conflicti467 – 474STIYLLMQ → RHLPVNAVISLNPFLKTGRG SPYNL in AAA23994 (PubMed:3057437).Curated8
Sequence conflicti467 – 474STIYLLMQ → RHLPVNAVISLNPFLKTGRG SPYNL in CAA30997 (PubMed:3057437).Curated8

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36536 Genomic DNA Translation: AAA23994.1
X12457 Genomic DNA Translation: CAA30997.1
U70214 Genomic DNA Translation: AAB08591.1
U00096 Genomic DNA Translation: AAC73272.1
AP009048 Genomic DNA Translation: BAB96738.1
M29955 Genomic DNA Translation: AAA23717.1
M31772 Genomic DNA Translation: AAA23680.1
PIRiS45229
RefSeqiNP_414703.1, NC_000913.3
WP_000753946.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC73272; AAC73272; b0161
BAB96738; BAB96738; BAB96738
GeneIDi947139
KEGGiecj:JW0157
eco:b0161
PATRICifig|1411691.4.peg.2119

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36536 Genomic DNA Translation: AAA23994.1
X12457 Genomic DNA Translation: CAA30997.1
U70214 Genomic DNA Translation: AAB08591.1
U00096 Genomic DNA Translation: AAC73272.1
AP009048 Genomic DNA Translation: BAB96738.1
M29955 Genomic DNA Translation: AAA23717.1
M31772 Genomic DNA Translation: AAA23680.1
PIRiS45229
RefSeqiNP_414703.1, NC_000913.3
WP_000753946.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KY9X-ray2.80A/B27-474[»]
2ZLEelectron microscopy28.00A/B/C/E/F/G/H/I/J/K/L/M27-474[»]
3CS0X-ray3.00A27-474[»]
3MH4X-ray3.10A/B27-474[»]
3MH5X-ray3.00A/B27-474[»]
3MH6X-ray3.60A27-474[»]
3MH7X-ray2.96A27-474[»]
3OTPX-ray3.76A/B/C/D/E/F27-474[»]
3OU0X-ray3.00A27-474[»]
4A8Delectron microscopy28.00A/B/C/D/E/F/G/H/I/J/K/L27-474[»]
ProteinModelPortaliP0C0V0
SMRiP0C0V0
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260994, 967 interactors
DIPiDIP-46256N
IntActiP0C0V0, 20 interactors
MINTiP0C0V0
STRINGi316385.ECDH10B_0141

Protein family/group databases

MEROPSiS01.273
MoonProtiP0C0V0

2D gel databases

SWISS-2DPAGEiP0C0V0

Proteomic databases

EPDiP0C0V0
PaxDbiP0C0V0
PRIDEiP0C0V0

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73272; AAC73272; b0161
BAB96738; BAB96738; BAB96738
GeneIDi947139
KEGGiecj:JW0157
eco:b0161
PATRICifig|1411691.4.peg.2119

Organism-specific databases

EchoBASEiEB0458
EcoGeneiEG10463 degP

Phylogenomic databases

eggNOGiENOG4105C0H Bacteria
COG0265 LUCA
HOGENOMiHOG000223642
InParanoidiP0C0V0
KOiK04771
PhylomeDBiP0C0V0

Enzyme and pathway databases

BioCyciEcoCyc:EG10463-MONOMER
MetaCyc:EG10463-MONOMER
BRENDAi3.4.21.107 2026

Miscellaneous databases

EvolutionaryTraceiP0C0V0
PROiPR:P0C0V0

Family and domain databases

InterProiView protein in InterPro
IPR001478 PDZ
IPR036034 PDZ_sf
IPR011782 Pept_S1C_Do
IPR009003 Peptidase_S1_PA
IPR001940 Peptidase_S1C
PfamiView protein in Pfam
PF00595 PDZ, 2 hits
PRINTSiPR00834 PROTEASES2C
SMARTiView protein in SMART
SM00228 PDZ, 2 hits
SUPFAMiSSF50156 SSF50156, 2 hits
SSF50494 SSF50494, 1 hit
TIGRFAMsiTIGR02037 degP_htrA_DO, 1 hit
PROSITEiView protein in PROSITE
PS50106 PDZ, 2 hits
ProtoNetiSearch...

Entry informationi

Entry nameiDEGP_ECOLI
AccessioniPrimary (citable) accession number: P0C0V0
Secondary accession number(s): P09376, P15724
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: November 7, 2018
This is version 122 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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Main funding by: National Institutes of Health

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