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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei58 – 581Substrate
Active sitei131 – 1311Charge relay system1 Publication
Binding sitei131 – 1311Substrate
Active sitei161 – 1611Charge relay system1 Publication
Binding sitei161 – 1611Substrate
Active sitei236 – 2361Charge relay system1 Publication

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • 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.
RETL1328306-WGS:GSTH-1743-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi131 – 1311H → R: Loss of peptidase activity with no detectable changes in secondary structure. 1 Publication
Mutagenesisi236 – 2361S → A: Loss of peptidase activity with no detectable changes in secondary structure. 2 Publications
Mutagenesisi254 – 2541I → N: It does not affect the proteolytic activity. 1 Publication
Mutagenesisi255 – 2551L → N: Loss of proteolytic activity. 1 Publication
Mutagenesisi258 – 2581D → V: Increases the proteolytic activity. 1 Publication
Mutagenesisi261 – 2611N → I: Loss of proteolytic activity. 1 Publication
Mutagenesisi262 – 2621I → 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 Publication
Mutagenesisi264 – 2641I → N: Loss of proteolytic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26262 PublicationsAdd
BLAST
Chaini27 – 474448Periplasmic serine endoprotease DegPPRO_0000026921Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

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

Structurei

Secondary structure

1
474
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi42 – 487Combined sources
Helixi49 – 513Combined sources
Beta strandi52 – 6312Combined sources
Beta strandi106 – 12015Combined sources
Turni121 – 1244Combined sources
Beta strandi125 – 1295Combined sources
Helixi130 – 1334Combined sources
Beta strandi136 – 1438Combined sources
Beta strandi148 – 15710Combined sources
Turni158 – 1614Combined sources
Beta strandi162 – 1698Combined sources
Helixi181 – 1833Combined sources
Beta strandi189 – 1946Combined sources
Beta strandi198 – 2003Combined sources
Beta strandi202 – 21312Combined sources
Turni216 – 2194Combined sources
Beta strandi225 – 2284Combined sources
Beta strandi238 – 2414Combined sources
Beta strandi247 – 2526Combined sources
Helixi257 – 2593Combined sources
Beta strandi262 – 2698Combined sources
Helixi270 – 28314Combined sources
Beta strandi293 – 2975Combined sources
Helixi301 – 3044Combined sources
Beta strandi313 – 3153Combined sources
Beta strandi323 – 3253Combined sources
Turni326 – 3294Combined sources
Beta strandi338 – 3436Combined sources
Helixi348 – 3536Combined sources
Beta strandi356 – 3583Combined sources
Beta strandi364 – 3718Combined sources
Beta strandi373 – 3753Combined sources
Beta strandi382 – 3843Combined sources
Beta strandi388 – 3936Combined sources
Beta strandi401 – 4033Combined sources
Turni406 – 4083Combined sources
Beta strandi411 – 4155Combined sources
Beta strandi418 – 4203Combined sources
Helixi423 – 4253Combined sources
Beta strandi432 – 4365Combined sources
Helixi444 – 4507Combined sources
Turni451 – 4533Combined sources
Beta strandi460 – 4667Combined sources
Beta strandi468 – 4714Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 37-472.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C0V0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini280 – 37192PDZ 1PROSITE-ProRule annotationAdd
BLAST
Domaini377 – 46690PDZ 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni234 – 2363Substrate binding
Regioni252 – 2565Substrate binding
Regioni291 – 2955Substrate binding

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101A → R in AAA23994 (PubMed:3057437).Curated
Sequence conflicti10 – 101A → R in AAA23680 (PubMed:2157212).Curated
Sequence conflicti46 – 461E → Q in AAA23717 (PubMed:2165018).Curated
Sequence conflicti192 – 1921A → G in AAA23994 (PubMed:3057437).Curated
Sequence conflicti192 – 1921A → G in CAA30997 (PubMed:3057437).Curated
Sequence conflicti467 – 4748STIYLLMQ → RHLPVNAVISLNPFLKTGRG SPYNL in AAA23994 (PubMed:3057437).Curated
Sequence conflicti467 – 4748STIYLLMQ → RHLPVNAVISLNPFLKTGRG SPYNL in CAA30997 (PubMed:3057437).Curated

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
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. Positions 37-472.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260994. 924 interactions.
DIPiDIP-46256N.
IntActiP0C0V0. 17 interactions.
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.
RETL1328306-WGS:GSTH-1743-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: September 7, 2016
This is version 104 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.