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Escherichia coli K-12 substr. MG1655 Enzyme: serine endoprotease, periplasmic



Gene: degQ Accession Numbers: G7682 (EcoCyc), b3234, ECK3223

Synonyms: hhoA

Regulation Summary Diagram: ?

Summary:
DegQ is a serine endoprotease that may be involved in degrading transiently denatured proteins [Waller96, Kolmar96].

DegQ may function as a dodecamer (note, however, that the other protein identified as a dodecamer in this paper, DegP, appears to actually operate as a hexamer) [Kolmar96]. In vivo DegQ exists as a trimer when it is substrate-free and as a dodecamer when substrate is present [Bai11].

DegQ expression increases during anaerobic growth at pH 8.5 [Yohannes04].

DegQ is a multi-copy suppressor of prc deficiency [Bass96].

Locations: inner membrane, periplasmic space

Map Position: [3,378,765 -> 3,380,132] (72.82 centisomes)
Length: 1368 bp / 455 aa

Molecular Weight of Polypeptide: 47.205 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0010609 , DIP:DIP-9424N , EchoBASE:EB2496 , EcoGene:EG12612 , EcoliWiki:b3234 , Mint:MINT-1246722 , ModBase:P39099 , OU-Microarray:b3234 , PortEco:degQ , PR:PRO_000022426 , Pride:P39099 , Protein Model Portal:P39099 , RefSeq:NP_417701 , RegulonDB:G7682 , SMR:P39099 , String:511145.b3234 , Swiss-Model:P39099 , UniProt:P39099

Relationship Links: InterPro:IN-FAMILY:IPR001478 , InterPro:IN-FAMILY:IPR001940 , InterPro:IN-FAMILY:IPR009003 , InterPro:IN-FAMILY:IPR011782 , PDB:Structure:3STI , PDB:Structure:3STJ , PDB:Structure:4A8A , PDB:Structure:4A8B , PDB:Structure:4A8C , PDB:Structure:4A9G , Pfam:IN-FAMILY:PF00595 , Prints:IN-FAMILY:PR00834 , Prosite:IN-FAMILY:PS50106 , Smart:IN-FAMILY:SM00228

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0006508 - proteolysis Inferred from experiment Inferred by computational analysis [UniProtGOA11, GOA01, Waller96]
GO:0051603 - proteolysis involved in cellular protein catabolic process Inferred from experiment [Sawa11]
GO:0006950 - response to stress Inferred by computational analysis [UniProtGOA11]
Molecular Function: GO:0004252 - serine-type endopeptidase activity Inferred from experiment Inferred by computational analysis [GOA01, Sawa11, Waller96]
GO:0008233 - peptidase activity Inferred from experiment Inferred by computational analysis [UniProtGOA11, Kolmar96]
GO:0042802 - identical protein binding Inferred from experiment [Bai11]
GO:0003824 - catalytic activity Inferred by computational analysis [GOA01]
GO:0008236 - serine-type peptidase activity Inferred by computational analysis [UniProtGOA11]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0042597 - periplasmic space Inferred from experiment Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, Waller96]
GO:0030288 - outer membrane-bounded periplasmic space Inferred by computational analysis [Waller96]
GO:0071575 - integral component of external side of plasma membrane Inferred by computational analysis [Waller96]

MultiFun Terms: information transfer protein related turnover, degradation
metabolism degradation of macromolecules proteins/peptides/glycopeptides

Essentiality data for degQ knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 1]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 2]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 1]

Enzymatic reaction of: serine endoprotease

EC Number: 3.4.21.-

a polypeptide[periplasmic space] + H2O[periplasmic space] <=> 2 a polypeptide[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is physiologically favored in the direction shown.

T(opt): 55 °C [BRENDA14, SkorkoGlonek95]

pH(opt): 7.6 [BRENDA14, Jiang08]


Sequence Features

Feature Class Location Citations Comment
Signal-Sequence 1 -> 27
[Waller96]
 
Chain 28 -> 455
[UniProt09]
UniProt: Protease degQ;
Amino-Acid-Sites-That-Bind 59
[UniProt11a]
UniProt: Substrate; Non-Experimental Qualifier: by similarity.
Amino-Acid-Sites-That-Bind 109
[UniProt11a]
UniProt: Substrate; Non-Experimental Qualifier: by similarity.
Active-Site 109
[UniProt10]
UniProt: Charge relay system; Non-Experimental Qualifier: potential;
Amino-Acid-Sites-That-Bind 139
[UniProt11a]
UniProt: Substrate; Non-Experimental Qualifier: by similarity.
Active-Site 139
[UniProt10]
UniProt: Charge relay system; Non-Experimental Qualifier: potential;
Mutagenesis-Variant 187
[Sawa11, UniProt12b]
Alternate sequence: S → A; UniProt: Loss of peptidase activity.
Mutagenesis-Variant 191
[Sawa11, UniProt12b]
Alternate sequence: R → A; UniProt: Reduces the peptidase activity.
Amino-Acid-Sites-That-Bind 212
[UniProt11a]
UniProt: Substrate; via the backbone amide.
Protein-Segment 212 -> 214
[UniProt11a]
UniProt: Substrate binding; Sequence Annotation Type: region of interest.
Active-Site 214
[UniProt10]
UniProt: Charge relay system; Non-Experimental Qualifier: potential;
Protein-Segment 230 -> 234
[UniProt11a]
UniProt: Substrate binding; Sequence Annotation Type: region of interest.
Conserved-Region 258 -> 349
[UniProt09]
UniProt: PDZ 1;
Protein-Segment 269 -> 273
[UniProt11a]
UniProt: Substrate binding; Sequence Annotation Type: region of interest.
Mutagenesis-Variant 329
[Sawa11, UniProt12b]
Alternate sequence: R → A; UniProt: Reduces the peptidase activity.
Conserved-Region 355 -> 447
[UniProt09]
UniProt: PDZ 2;


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


References

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Bai11: Bai XC, Pan XJ, Wang XJ, Ye YY, Chang LF, Leng D, Lei J, Sui SF (2011). "Characterization of the Structure and Function of Escherichia coli DegQ as a Representative of the DegQ-like Proteases of Bacterial HtrA Family Proteins." Structure 19(9);1328-37. PMID: 21893291

Bass96: Bass S, Gu Q, Christen A (1996). "Multicopy suppressors of prc mutant Escherichia coli include two HtrA (DegP) protease homologs (HhoAB), DksA, and a truncated RlpA." J Bacteriol 178(4);1154-61. PMID: 8576052

BRENDA14: BRENDA team (2014). "Imported from BRENDA version existing on Aug 2014." http://www.brenda-enzymes.org.

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Jiang08: Jiang J, Zhang X, Chen Y, Wu Y, Zhou ZH, Chang Z, Sui SF (2008). "Activation of DegP chaperone-protease via formation of large cage-like oligomers upon binding to substrate proteins." Proc Natl Acad Sci U S A 105(33);11939-44. PMID: 18697939

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Kolmar96: Kolmar H, Waller PR, Sauer RT (1996). "The DegP and DegQ periplasmic endoproteases of Escherichia coli: specificity for cleavage sites and substrate conformation." J Bacteriol 178(20);5925-9. PMID: 8830688

Sawa11: Sawa J, Malet H, Krojer T, Canellas F, Ehrmann M, Clausen T (2011). "Molecular adaptation of the DegQ protease to exert protein quality control in the bacterial cell envelope." J Biol Chem 286(35);30680-90. PMID: 21685389

SkorkoGlonek95: Skorko-Glonek J, Krzewski K, Lipinska B, Bertoli E, Tanfani F (1995). "Comparison of the structure of wild-type HtrA heat shock protease and mutant HtrA proteins. A Fourier transform infrared spectroscopic study." J Biol Chem 270(19);11140-6. PMID: 7744744

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt11a: UniProt Consortium (2011). "UniProt version 2011-11 released on 2011-11-22 00:00:00." Database.

UniProt12b: UniProt Consortium (2012). "UniProt version 2012-02 released on 2012-02-29 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

Waller96: Waller PR, Sauer RT (1996). "Characterization of degQ and degS, Escherichia coli genes encoding homologs of the DegP protease." J Bacteriol 178(4);1146-53. PMID: 8576051

Yohannes04: Yohannes E, Barnhart DM, Slonczewski JL (2004). "pH-dependent catabolic protein expression during anaerobic growth of Escherichia coli K-12." J Bacteriol 186(1);192-9. PMID: 14679238

Other References Related to Gene Regulation

MendozaVargas09: Mendoza-Vargas A, Olvera L, Olvera M, Grande R, Vega-Alvarado L, Taboada B, Jimenez-Jacinto V, Salgado H, Juarez K, Contreras-Moreira B, Huerta AM, Collado-Vides J, Morett E (2009). "Genome-wide identification of transcription start sites, promoters and transcription factor binding sites in E. coli." PLoS One 4(10);e7526. PMID: 19838305

Viveiros07: Viveiros M, Dupont M, Rodrigues L, Couto I, Davin-Regli A, Martins M, Pages JM, Amaral L (2007). "Antibiotic stress, genetic response and altered permeability of E. coli." PLoS ONE 2;e365. PMID: 17426813


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Mon Dec 22, 2014, biocyc14.