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Protein

Periplasmic serine endoprotease DegP

Gene

degP

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

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

Enzyme 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

  • serine-type endopeptidase activity Source: EcoliWiki

GO - Biological processi

  • misfolded or incompletely synthesized protein catabolic process Source: EcoliWiki
  • protein folding Source: EcoliWiki
  • proteolysis Source: EcoliWiki
  • response to oxidative stress Source: EcoliWiki
  • response to temperature stimulus Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Stress response

Enzyme and pathway databases

BioCyciEcoCyc:EG10463-MONOMER.
ECOL316407:JW0157-MONOMER.
MetaCyc:EG10463-MONOMER.
BRENDAi3.4.21.107. 2026.

Protein family/group databases

MEROPSiS01.273.

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

  • outer membrane-bounded periplasmic space Source: EcoliWiki
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

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-2DPAGEP0C0V0.

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

WithEntry#Exp.IntActNotes
itself2EBI-547165,EBI-547165
LYZP006988EBI-547165,EBI-1029543From a different organism.
ompAP0A9106EBI-547165,EBI-371347

Protein-protein interaction databases

BioGridi4260994. 924 interactors.
DIPiDIP-46256N.
IntActiP0C0V0. 17 interactors.
MINTiMINT-1302319.
STRINGi511145.b0161.

Structurei

Secondary structure

1474
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi42 – 48Combined sources7
Helixi49 – 51Combined sources3
Beta strandi52 – 63Combined sources12
Beta strandi106 – 120Combined sources15
Turni121 – 124Combined sources4
Beta strandi125 – 129Combined sources5
Helixi130 – 133Combined sources4
Beta strandi136 – 143Combined sources8
Beta strandi148 – 157Combined sources10
Turni158 – 161Combined sources4
Beta strandi162 – 169Combined sources8
Helixi181 – 183Combined sources3
Beta strandi189 – 194Combined sources6
Beta strandi198 – 200Combined sources3
Beta strandi202 – 213Combined sources12
Turni216 – 219Combined sources4
Beta strandi225 – 228Combined sources4
Beta strandi238 – 241Combined sources4
Beta strandi247 – 252Combined sources6
Helixi257 – 259Combined sources3
Beta strandi262 – 269Combined sources8
Helixi270 – 283Combined sources14
Beta strandi293 – 297Combined sources5
Helixi301 – 304Combined sources4
Beta strandi313 – 315Combined sources3
Beta strandi323 – 325Combined sources3
Turni326 – 329Combined sources4
Beta strandi338 – 343Combined sources6
Helixi348 – 353Combined sources6
Beta strandi356 – 358Combined sources3
Beta strandi364 – 371Combined sources8
Beta strandi373 – 375Combined sources3
Beta strandi382 – 384Combined sources3
Beta strandi388 – 393Combined sources6
Beta strandi401 – 403Combined sources3
Turni406 – 408Combined sources3
Beta strandi411 – 415Combined sources5
Beta strandi418 – 420Combined sources3
Helixi423 – 425Combined sources3
Beta strandi432 – 436Combined sources5
Helixi444 – 450Combined sources7
Turni451 – 453Combined sources3
Beta strandi460 – 466Combined sources7
Beta strandi468 – 471Combined sources4

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...

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
Contains 2 PDZ (DHR) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG4105C0H. Bacteria.
COG0265. LUCA.
HOGENOMiHOG000223642.
InParanoidiP0C0V0.
KOiK04771.
OMAiQPVENIG.
PhylomeDBiP0C0V0.

Family and domain databases

Gene3Di2.30.42.10. 2 hits.
InterProiIPR001478. PDZ.
IPR011782. Pept_S1C_Do.
IPR009003. Peptidase_S1_PA.
IPR001940. Peptidase_S1C.
[Graphical view]
PfamiPF00595. PDZ. 2 hits.
[Graphical view]
PRINTSiPR00834. PROTEASES2C.
SMARTiSM00228. PDZ. 2 hits.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 2 hits.
SSF50494. SSF50494. 2 hits.
TIGRFAMsiTIGR02037. degP_htrA_DO. 1 hit.
PROSITEiPS50106. PDZ. 2 hits.
[Graphical view]

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.
PATRICi32115431. VBIEscCol129921_0167.

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. 924 interactors.
DIPiDIP-46256N.
IntActiP0C0V0. 17 interactors.
MINTiMINT-1302319.
STRINGi511145.b0161.

Protein family/group databases

MEROPSiS01.273.

2D gel databases

SWISS-2DPAGEP0C0V0.

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.
PATRICi32115431. VBIEscCol129921_0167.

Organism-specific databases

EchoBASEiEB0458.
EcoGeneiEG10463. degP.

Phylogenomic databases

eggNOGiENOG4105C0H. Bacteria.
COG0265. LUCA.
HOGENOMiHOG000223642.
InParanoidiP0C0V0.
KOiK04771.
OMAiQPVENIG.
PhylomeDBiP0C0V0.

Enzyme and pathway databases

BioCyciEcoCyc:EG10463-MONOMER.
ECOL316407:JW0157-MONOMER.
MetaCyc:EG10463-MONOMER.
BRENDAi3.4.21.107. 2026.

Miscellaneous databases

EvolutionaryTraceiP0C0V0.
PROiP0C0V0.

Family and domain databases

Gene3Di2.30.42.10. 2 hits.
InterProiIPR001478. PDZ.
IPR011782. Pept_S1C_Do.
IPR009003. Peptidase_S1_PA.
IPR001940. Peptidase_S1C.
[Graphical view]
PfamiPF00595. PDZ. 2 hits.
[Graphical view]
PRINTSiPR00834. PROTEASES2C.
SMARTiSM00228. PDZ. 2 hits.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 2 hits.
SSF50494. SSF50494. 2 hits.
TIGRFAMsiTIGR02037. degP_htrA_DO. 1 hit.
PROSITEiPS50106. PDZ. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDEGP_ECOLI
AccessioniPrimary (citable) accession number: P0C0V0
Secondary accession number(s): P09376, P15724
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: November 2, 2016
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

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

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.