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P39099

- DEGQ_ECOLI

UniProt

P39099 - DEGQ_ECOLI

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
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    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

    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

    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.
    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 S1B family.Curated
    Contains 2 PDZ (DHR) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG0265.
    HOGENOMiHOG000223642.
    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

    MKKQTQLLSA LALSVGLTLS ASFQAVASIP GQVADQAPLP SLAPMLEKVL    50
    PAVVSVRVEG TASQGQKIPE EFKKFFGDDL PDQPAQPFEG LGSGVIINAS 100
    KGYVLTNNHV INQAQKISIQ LNDGREFDAK LIGSDDQSDI ALLQIQNPSK 150
    LTQIAIADSD KLRVGDFAVA VGNPFGLGQT ATSGIVSALG RSGLNLEGLE 200
    NFIQTDASIN RGNSGGALLN LNGELIGINT AILAPGGGSV GIGFAIPSNM 250
    ARTLAQQLID FGEIKRGLLG IKGTEMSADI AKAFNLDVQR GAFVSEVLPG 300
    SGSAKAGVKA GDIITSLNGK PLNSFAELRS RIATTEPGTK VKLGLLRNGK 350
    PLEVEVTLDT STSSSASAEM ITPALEGATL SDGQLKDGGK GIKIDEVVKG 400
    SPAAQAGLQK DDVIIGVNRD RVNSIAEMRK VLAAKPAIIA LQIVRGNESI 450
    YLLMR 455
    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.
    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.
    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

    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 1, 2014
    This is version 129 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