Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Periplasmic pH-dependent serine endoprotease DegQ

Gene

degQ

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

DegQ could degrade transiently denatured and unfolded proteins which accumulate in the periplasm following stress conditions. DegQ is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for a beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable to be cleaved, thereby preventing non-specific proteolysis of folded proteins. DegQ can substitute for the periplasmic protease DegP.2 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.

Enzyme regulationi

Inhibited by diisopropylfluorophosphate (DFP).1 Publication

pH dependencei

Optimum pH is 5.5. The degradation is efficient at pH values between 4.5 and 6.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei59SubstrateBy similarity1
Active sitei109Charge relay system1 Publication1
Binding sitei109SubstrateBy similarity1
Active sitei139Charge relay system1 Publication1
Binding sitei139SubstrateBy similarity1
Binding sitei212Substrate; via amide nitrogen1 Publication1
Active sitei214Charge relay system1 Publication1

GO - Molecular functioni

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

GO - Biological processi

  • proteolysis Source: EcoliWiki
  • proteolysis involved in cellular protein catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Stress response

Enzyme and pathway databases

BioCyciEcoCyc:G7682-MONOMER.
ECOL316407:JW3203-MONOMER.
MetaCyc:G7682-MONOMER.

Protein family/group databases

MEROPSiS01.274.

Names & Taxonomyi

Protein namesi
Recommended name:
Periplasmic pH-dependent serine endoprotease DegQ (EC:3.4.21.107)
Alternative name(s):
Protease Do
Gene namesi
Name:degQ
Synonyms:hhoA
Ordered Locus Names:b3234, JW3203
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12612. degQ.

Subcellular locationi

  • Periplasm 1 Publication

GO - Cellular componenti

  • integral component of external side of plasma membrane Source: EcoliWiki
  • periplasmic space Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi187S → A: Loss of peptidase activity. 1 Publication1
Mutagenesisi191R → A: Reduces the peptidase activity. 1 Publication1
Mutagenesisi329R → A: Reduces the peptidase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 271 PublicationAdd BLAST27
ChainiPRO_000002693728 – 455Periplasmic pH-dependent serine endoprotease DegQAdd BLAST428

Proteomic databases

EPDiP39099.
PaxDbiP39099.
PRIDEiP39099.

2D gel databases

SWISS-2DPAGEP39099.

Interactioni

Subunit structurei

DegQ 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 DegQ trimer and hexamer into catalytically active 12- and 24-mers. The conversion of 6-mer (DegQ6) into 12-mer (DegQ12) or 24-mer (DegQ24) is crucial in regulating protease activity.2 Publications

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4261912. 10 interactors.
DIPiDIP-9424N.
IntActiP39099. 8 interactors.
MINTiMINT-1246722.
STRINGi511145.b3234.

Structurei

Secondary structure

1455
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi43 – 49Combined sources7
Helixi50 – 52Combined sources3
Beta strandi53 – 55Combined sources3
Beta strandi93 – 98Combined sources6
Turni99 – 102Combined sources4
Beta strandi103 – 106Combined sources4
Helixi108 – 110Combined sources3
Beta strandi117 – 120Combined sources4
Beta strandi126 – 135Combined sources10
Turni136 – 139Combined sources4
Beta strandi140 – 147Combined sources8
Helixi159 – 161Combined sources3
Beta strandi166 – 172Combined sources7
Helixi174 – 176Combined sources3
Beta strandi180 – 188Combined sources9
Beta strandi194 – 199Combined sources6
Beta strandi203 – 207Combined sources5
Turni211 – 215Combined sources5
Beta strandi216 – 219Combined sources4
Beta strandi225 – 230Combined sources6
Beta strandi243 – 247Combined sources5
Helixi248 – 264Combined sources17
Beta strandi271 – 275Combined sources5
Helixi278 – 283Combined sources6
Beta strandi290 – 297Combined sources8
Helixi302 – 306Combined sources5
Helixi325 – 333Combined sources9
Beta strandi340 – 347Combined sources8
Beta strandi350 – 357Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3STIX-ray2.60A/B/C28-264[»]
3STJX-ray2.60A/B/C/D/E/F/G/H/I/J/K/L28-364[»]
4A8Aelectron microscopy14.20A/B/C/D/E/F/G/H/I/J/K/L28-455[»]
4A8Belectron microscopy13.00A/B/C/D/E/F/G/H/I/J/K/L28-455[»]
4A8Celectron microscopy7.50A/B/C/D/E/F/G/H/I/J/K/L28-455[»]
4A9Gelectron microscopy7.50A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/Y28-455[»]
ProteinModelPortaliP39099.
SMRiP39099.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini258 – 349PDZ 1PROSITE-ProRule annotationAdd BLAST92
Domaini355 – 447PDZ 2PROSITE-ProRule annotationAdd BLAST93

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni212 – 214Substrate binding3
Regioni230 – 234Substrate binding5
Regioni269 – 273Substrate 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.
InParanoidiP39099.
KOiK04772.
OMAiAFRYFFG.
PhylomeDBiP39099.

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. 1 hit.
PF13180. PDZ_2. 1 hit.
[Graphical view]
PRINTSiPR00834. PROTEASES2C.
SMARTiSM00228. PDZ. 2 hits.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 2 hits.
SSF50494. SSF50494. 1 hit.
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.

P39099-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKQTQLLSA LALSVGLTLS ASFQAVASIP GQVADQAPLP SLAPMLEKVL
60 70 80 90 100
PAVVSVRVEG TASQGQKIPE EFKKFFGDDL PDQPAQPFEG LGSGVIINAS
110 120 130 140 150
KGYVLTNNHV INQAQKISIQ LNDGREFDAK LIGSDDQSDI ALLQIQNPSK
160 170 180 190 200
LTQIAIADSD KLRVGDFAVA VGNPFGLGQT ATSGIVSALG RSGLNLEGLE
210 220 230 240 250
NFIQTDASIN RGNSGGALLN LNGELIGINT AILAPGGGSV GIGFAIPSNM
260 270 280 290 300
ARTLAQQLID FGEIKRGLLG IKGTEMSADI AKAFNLDVQR GAFVSEVLPG
310 320 330 340 350
SGSAKAGVKA GDIITSLNGK PLNSFAELRS RIATTEPGTK VKLGLLRNGK
360 370 380 390 400
PLEVEVTLDT STSSSASAEM ITPALEGATL SDGQLKDGGK GIKIDEVVKG
410 420 430 440 450
SPAAQAGLQK DDVIIGVNRD RVNSIAEMRK VLAAKPAIIA LQIVRGNESI

YLLMR
Length:455
Mass (Da):47,205
Last modified:February 1, 1995 - v1
Checksum:i6A090F93AC021C83
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U15661 Genomic DNA. Translation: AAC43992.1.
U32495 Genomic DNA. Translation: AAC44005.1.
U18997 Genomic DNA. Translation: AAA58036.1.
U00096 Genomic DNA. Translation: AAC76266.1.
AP009048 Genomic DNA. Translation: BAE77277.1.
PIRiJC6051.
RefSeqiNP_417701.1. NC_000913.3.
WP_001295271.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76266; AAC76266; b3234.
BAE77277; BAE77277; BAE77277.
GeneIDi947812.
KEGGiecj:JW3203.
eco:b3234.
PATRICi32121894. VBIEscCol129921_3331.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U15661 Genomic DNA. Translation: AAC43992.1.
U32495 Genomic DNA. Translation: AAC44005.1.
U18997 Genomic DNA. Translation: AAA58036.1.
U00096 Genomic DNA. Translation: AAC76266.1.
AP009048 Genomic DNA. Translation: BAE77277.1.
PIRiJC6051.
RefSeqiNP_417701.1. NC_000913.3.
WP_001295271.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3STIX-ray2.60A/B/C28-264[»]
3STJX-ray2.60A/B/C/D/E/F/G/H/I/J/K/L28-364[»]
4A8Aelectron microscopy14.20A/B/C/D/E/F/G/H/I/J/K/L28-455[»]
4A8Belectron microscopy13.00A/B/C/D/E/F/G/H/I/J/K/L28-455[»]
4A8Celectron microscopy7.50A/B/C/D/E/F/G/H/I/J/K/L28-455[»]
4A9Gelectron microscopy7.50A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/Y28-455[»]
ProteinModelPortaliP39099.
SMRiP39099.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261912. 10 interactors.
DIPiDIP-9424N.
IntActiP39099. 8 interactors.
MINTiMINT-1246722.
STRINGi511145.b3234.

Protein family/group databases

MEROPSiS01.274.

2D gel databases

SWISS-2DPAGEP39099.

Proteomic databases

EPDiP39099.
PaxDbiP39099.
PRIDEiP39099.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76266; AAC76266; b3234.
BAE77277; BAE77277; BAE77277.
GeneIDi947812.
KEGGiecj:JW3203.
eco:b3234.
PATRICi32121894. VBIEscCol129921_3331.

Organism-specific databases

EchoBASEiEB2496.
EcoGeneiEG12612. degQ.

Phylogenomic databases

eggNOGiENOG4105C0H. Bacteria.
COG0265. LUCA.
HOGENOMiHOG000223642.
InParanoidiP39099.
KOiK04772.
OMAiAFRYFFG.
PhylomeDBiP39099.

Enzyme and pathway databases

BioCyciEcoCyc:G7682-MONOMER.
ECOL316407:JW3203-MONOMER.
MetaCyc:G7682-MONOMER.

Miscellaneous databases

PROiP39099.

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. 1 hit.
PF13180. PDZ_2. 1 hit.
[Graphical view]
PRINTSiPR00834. PROTEASES2C.
SMARTiSM00228. PDZ. 2 hits.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 2 hits.
SSF50494. SSF50494. 1 hit.
TIGRFAMsiTIGR02037. degP_htrA_DO. 1 hit.
PROSITEiPS50106. PDZ. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDEGQ_ECOLI
AccessioniPrimary (citable) accession number: P39099
Secondary accession number(s): Q2M8X9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 2, 2016
This is version 144 of the entry and version 1 of the sequence. [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. 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.