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P39099

- DEGQ_ECOLI

UniProt

P39099 - DEGQ_ECOLI

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Protein

Periplasmic pH-dependent serine endoprotease DegQ

Gene

degQ

Organism
Escherichia coli (strain K12)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei59 – 591SubstrateBy similarity
Active sitei109 – 1091Charge relay systemSequence Analysis
Binding sitei109 – 1091SubstrateBy similarity
Active sitei139 – 1391Charge relay systemSequence Analysis
Binding sitei139 – 1391SubstrateBy similarity
Binding sitei212 – 2121Substrate; via amide nitrogen
Active sitei214 – 2141Charge relay systemSequence Analysis

GO - Molecular functioni

  1. identical protein binding Source: EcoCyc
  2. peptidase activity Source: EcoliWiki
  3. serine-type endopeptidase activity Source: UniProtKB

GO - Biological processi

  1. proteolysis Source: EcoCyc
  2. proteolysis involved in cellular protein catabolic process Source: UniProtKB
  3. response to stress Source: UniProtKB-KW
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG12612. degQ.

Subcellular locationi

Periplasm 1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi187 – 1871S → A: Loss of peptidase activity. 1 Publication
Mutagenesisi191 – 1911R → A: Reduces the peptidase activity. 1 Publication
Mutagenesisi329 – 3291R → A: Reduces the peptidase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 27271 PublicationAdd
BLAST
Chaini28 – 455428Periplasmic pH-dependent serine endoprotease DegQPRO_0000026937Add
BLAST

Proteomic databases

PaxDbiP39099.
PRIDEiP39099.

2D gel databases

SWISS-2DPAGEP39099.

Expressioni

Gene expression databases

GenevestigatoriP39099.

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

Protein-protein interaction databases

DIPiDIP-9424N.
IntActiP39099. 8 interactions.
MINTiMINT-1246722.
STRINGi511145.b3234.

Structurei

Secondary structure

1
455
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi43 – 497
Helixi50 – 523
Beta strandi53 – 553
Beta strandi93 – 986
Turni99 – 1024
Beta strandi103 – 1064
Helixi108 – 1103
Beta strandi117 – 1204
Beta strandi126 – 13510
Turni136 – 1394
Beta strandi140 – 1478
Helixi159 – 1613
Beta strandi166 – 1727
Helixi174 – 1763
Beta strandi180 – 1889
Beta strandi194 – 1996
Beta strandi203 – 2075
Turni211 – 2155
Beta strandi216 – 2194
Beta strandi225 – 2306
Beta strandi243 – 2475
Helixi248 – 26417
Beta strandi271 – 2755
Helixi278 – 2836
Beta strandi290 – 2978
Helixi302 – 3065
Helixi325 – 3339
Beta strandi340 – 3478
Beta strandi350 – 3578

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 38-455.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini258 – 34992PDZ 1PROSITE-ProRule annotationAdd
BLAST
Domaini355 – 44793PDZ 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni212 – 2143Substrate binding
Regioni230 – 2345Substrate binding
Regioni269 – 2735Substrate binding

Sequence similaritiesi

Belongs to the peptidase S1C family.Curated
Contains 2 PDZ (DHR) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiCOG0265.
HOGENOMiHOG000223642.
InParanoidiP39099.
KOiK04772.
OMAiMEMSADI.
OrthoDBiEOG61ZTDN.
PhylomeDBiP39099.

Family and domain databases

Gene3Di2.30.42.10. 2 hits.
InterProiIPR001478. PDZ.
IPR011782. Pept_S1C_Do.
IPR001940. Peptidase_S1C.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00595. PDZ. 2 hits.
[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:
EMBL
GenBank
DDBJ
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.
YP_491418.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76266; AAC76266; b3234.
BAE77277; BAE77277; BAE77277.
GeneIDi12932918.
947812.
KEGGiecj:Y75_p3154.
eco:b3234.
PATRICi32121894. VBIEscCol129921_3331.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi JC6051.
RefSeqi NP_417701.1. NC_000913.3.
YP_491418.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3STI X-ray 2.60 A/B/C 28-264 [» ]
3STJ X-ray 2.60 A/B/C/D/E/F/G/H/I/J/K/L 28-364 [» ]
4A8A electron microscopy 14.20 A/B/C/D/E/F/G/H/I/J/K/L 28-455 [» ]
4A8B electron microscopy 13.00 A/B/C/D/E/F/G/H/I/J/K/L 28-455 [» ]
4A8C electron microscopy 7.50 A/B/C/D/E/F/G/H/I/J/K/L 28-455 [» ]
4A9G electron microscopy 7.50 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/Y 28-455 [» ]
ProteinModelPortali P39099.
SMRi P39099. Positions 38-455.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-9424N.
IntActi P39099. 8 interactions.
MINTi MINT-1246722.
STRINGi 511145.b3234.

Protein family/group databases

MEROPSi S01.274.

2D gel databases

SWISS-2DPAGE P39099.

Proteomic databases

PaxDbi P39099.
PRIDEi P39099.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76266 ; AAC76266 ; b3234 .
BAE77277 ; BAE77277 ; BAE77277 .
GeneIDi 12932918.
947812.
KEGGi ecj:Y75_p3154.
eco:b3234.
PATRICi 32121894. VBIEscCol129921_3331.

Organism-specific databases

EchoBASEi EB2496.
EcoGenei EG12612. degQ.

Phylogenomic databases

eggNOGi COG0265.
HOGENOMi HOG000223642.
InParanoidi P39099.
KOi K04772.
OMAi MEMSADI.
OrthoDBi EOG61ZTDN.
PhylomeDBi P39099.

Enzyme and pathway databases

BioCyci EcoCyc:G7682-MONOMER.
ECOL316407:JW3203-MONOMER.
MetaCyc:G7682-MONOMER.

Miscellaneous databases

PROi P39099.

Gene expression databases

Genevestigatori P39099.

Family and domain databases

Gene3Di 2.30.42.10. 2 hits.
InterProi IPR001478. PDZ.
IPR011782. Pept_S1C_Do.
IPR001940. Peptidase_S1C.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF00595. PDZ. 2 hits.
[Graphical view ]
PRINTSi PR00834. PROTEASES2C.
SMARTi SM00228. PDZ. 2 hits.
[Graphical view ]
SUPFAMi SSF50156. SSF50156. 2 hits.
SSF50494. SSF50494. 1 hit.
TIGRFAMsi TIGR02037. degP_htrA_DO. 1 hit.
PROSITEi PS50106. PDZ. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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 SUBSTRATE ANALOGS, REACTION MECHANISM, MUTAGENESIS OF SER-187; ARG-191 AND ARG-329, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

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: October 29, 2014
This is version 130 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

External Data

Dasty 3