Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P39099 (DEGQ_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Periplasmic pH-dependent serine endoprotease DegQ

EC=3.4.21.107
Alternative name(s):
Protease Do
Gene names
Name:degQ
Synonyms:hhoA
Ordered Locus Names:b3234, JW3203
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length455 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.5

Catalytic activity

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 regulation

Inhibited by diisopropylfluorophosphate (DFP). Ref.2

Subunit structure

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. Ref.5 Ref.6

Subcellular location

Periplasm Ref.2.

Sequence similarities

Belongs to the peptidase S1B family.

Contains 2 PDZ (DHR) domains.

Biophysicochemical properties

pH dependence:

Optimum pH is 5.5. The degradation is efficient at pH values between 4.5 and 6. Ref.6

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Ref.2
Chain28 – 455428Periplasmic pH-dependent serine endoprotease DegQ
PRO_0000026937

Regions

Domain258 – 34992PDZ 1
Domain355 – 44793PDZ 2
Region212 – 2143Substrate binding
Region230 – 2345Substrate binding
Region269 – 2735Substrate binding

Sites

Active site1091Charge relay system Potential
Active site1391Charge relay system Potential
Active site2141Charge relay system Potential
Binding site591Substrate By similarity
Binding site1091Substrate By similarity
Binding site1391Substrate By similarity
Binding site2121Substrate; via amide nitrogen

Experimental info

Mutagenesis1871S → A: Loss of peptidase activity. Ref.6
Mutagenesis1911R → A: Reduces the peptidase activity. Ref.6
Mutagenesis3291R → A: Reduces the peptidase activity. Ref.6

Secondary structure

................................................... 455
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P39099 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 6A090F93AC021C83

FASTA45547,205
        10         20         30         40         50         60 
MKKQTQLLSA LALSVGLTLS ASFQAVASIP GQVADQAPLP SLAPMLEKVL PAVVSVRVEG 

        70         80         90        100        110        120 
TASQGQKIPE EFKKFFGDDL PDQPAQPFEG LGSGVIINAS KGYVLTNNHV INQAQKISIQ 

       130        140        150        160        170        180 
LNDGREFDAK LIGSDDQSDI ALLQIQNPSK LTQIAIADSD KLRVGDFAVA VGNPFGLGQT 

       190        200        210        220        230        240 
ATSGIVSALG RSGLNLEGLE NFIQTDASIN RGNSGGALLN LNGELIGINT AILAPGGGSV 

       250        260        270        280        290        300 
GIGFAIPSNM ARTLAQQLID FGEIKRGLLG IKGTEMSADI AKAFNLDVQR GAFVSEVLPG 

       310        320        330        340        350        360 
SGSAKAGVKA GDIITSLNGK PLNSFAELRS RIATTEPGTK VKLGLLRNGK PLEVEVTLDT 

       370        380        390        400        410        420 
STSSSASAEM ITPALEGATL SDGQLKDGGK GIKIDEVVKG SPAAQAGLQK DDVIIGVNRD 

       430        440        450 
RVNSIAEMRK VLAAKPAIIA LQIVRGNESI YLLMR 

« Hide

References

« Hide 'large scale' references
[1]Bass S., Gu Q., Goddard A.
Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]"Characterization of degQ and degS, Escherichia coli genes encoding homologs of the DegP protease."
Waller P.R., Sauer R.T.
J. Bacteriol. 178:1146-1153(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 28-32, FUNCTION AS A SERINE PROTEASE, SUBCELLULAR LOCATION, ENZYME REGULATION, NOMENCLATURE.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"The DegP and DegQ periplasmic endoproteases of Escherichia coli: specificity for cleavage sites and substrate conformation."
Kolmar H., Waller P.R., Sauer R.T.
J. Bacteriol. 178:5925-5929(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A SERINE PROTEASE, SUBSTRATE SPECIFICITY, SUBUNIT.
[6]"Molecular adaptation of the DegQ protease to exert protein quality control in the bacterial cell envelope."
Sawa J., Malet H., Krojer T., Canellas F., Ehrmann M., Clausen T.
J. Biol. Chem. 286:30680-30690(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 28-264 IN COMPLEX WITH ANALOGS SUBSTRATE, REACTION MECHANISM, MUTAGENESIS OF SER-187; ARG-191 AND ARG-329, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRJC6051.
RefSeqNP_417701.1. NC_000913.3.
YP_491418.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP39099.
SMRP39099. Positions 38-455.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9424N.
IntActP39099. 8 interactions.
MINTMINT-1246722.
STRING511145.b3234.

Protein family/group databases

MEROPSS01.274.

2D gel databases

SWISS-2DPAGEP39099.

Proteomic databases

PaxDbP39099.
PRIDEP39099.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76266; AAC76266; b3234.
BAE77277; BAE77277; BAE77277.
GeneID12932918.
947812.
KEGGecj:Y75_p3154.
eco:b3234.
PATRIC32121894. VBIEscCol129921_3331.

Organism-specific databases

EchoBASEEB2496.
EcoGeneEG12612. degQ.

Phylogenomic databases

eggNOGCOG0265.
HOGENOMHOG000223642.
KOK04772.
OMAMEMSADI.
OrthoDBEOG61ZTDN.
PhylomeDBP39099.
ProtClustDBPRK10139.

Enzyme and pathway databases

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

Gene expression databases

GenevestigatorP39099.

Family and domain databases

Gene3D2.30.42.10. 2 hits.
InterProIPR001478. PDZ.
IPR011782. Pept_S1C_Do.
IPR001940. Peptidase_S1C.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00595. PDZ. 2 hits.
[Graphical view]
PRINTSPR00834. PROTEASES2C.
SMARTSM00228. PDZ. 2 hits.
[Graphical view]
SUPFAMSSF50156. SSF50156. 2 hits.
SSF50494. SSF50494. 1 hit.
TIGRFAMsTIGR02037. degP_htrA_DO. 1 hit.
PROSITEPS50106. PDZ. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

PROP39099.

Entry information

Entry nameDEGQ_ECOLI
AccessionPrimary (citable) accession number: P39099
Secondary accession number(s): Q2M8X9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene