protein

Recombinant Escherichia coli Periplasmic serine endoprotease DegP

MBS1198532

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Escherichia coli Periplasmic serine endoprotease DegP

Periplasmic serine endoprotease DegP

Heat shock protein DegP; Protease Do

serine endoprotease (protease Do), membrane-associated; Periplasmic serine endoprotease DegP; serine endoprotease (protease Do), membrane-associated; Heat shock protein DegP; Protease Do

degP

degP; degP; ECK0160; htrA; JW0157; ptd; htrA; ptd

DEGP_ECOLI

E Coli or Yeast or Baculovirus or Mammalian Cell

27-474

474

AETSSATTAQQMPSLAPMLEKVMPSVVSINVEGSTTVNT
PRMPRNFQQFFGDDSPFCQEGSPFQSSPFCQGGQGGNGG
GQQQKFMALGSGVIIDADKGYVVTNNHVVDNATVIKVQL
SDGRKFDAKMVGKDPRSDIALIQIQNPKNLTAIKMADSD
ALRVGDYTVAIGNPFGLGETVTSGIVSALGRSGLNAENY
ENFIQTDAAINRGNSGGALVNLNGELIGINTAILAPDGG
NIGIGFAIPSNMVKNLTSQMV

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. It degrades transiently denatured and unfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. Its proteolytic activity is essential for the survival of cells at elevated temperatures. It can degrade IciA, ada, casein, globin and PapA. DegP shares specificity with DegQ. DegP is also involved in the biogenesis of partially folded outer-membrane proteins (OMP).

Sequence analysis and regulation of the htrA gene of Escherichia coli a sigma 32-independent mechanism of heat-inducible transcription.Lipinska B., Sharma S., Georgopoulos C.Nucleic Acids Res. 16:10053-10067(1988) Systematic sequencing of the Escherichia coli genome analysis of the 2.4-4.1 min (110,917-193,643 bp) region.Fujita N., Mori H., Yura T., Ishihama A.Nucleic Acids Res. 22:1637-1639(1994) Sequence of minutes 4-25 of Escherichia coli.Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. 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) 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) Primary structure of the deoxyguanosine triphosphate triphosphohydrolase-encoding gene (dgt) of Escherichia coli.Quirk S., Bhatnagar S.K., Bessman M.J.Gene 89:13-18(1990) Structure and regulation of the gene for dGTP triphosphohydrolase from Escherichia coli.Wurgler S.M., Richardson C.C.Proc. Natl. Acad. Sci. U.S.A. 87:2740-2744(1990) The HtrA (DegP) protein, essential for Escherichia coli survival at high temperatures, is an endopeptidase.Lipinska B., Zylicz M., Georgopoulos C.J. Bacteriol. 172:1791-1797(1990) Protein identification with N and C-terminal sequence tags in proteome projects.Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F.J. Mol. Biol. 278:599-608(1998) Protease Do is essential for survival of Escherichia coli at high temperatures its identity with the htrA gene product.Seol J.H., Woo S.K., Jung E.M., Yoo S.J., Lee C.S., Kim K.J., Tanaka K., Ichihara A., Ha D.B., Chung C.H.Biochem. Biophys. Res. Commun. 176:730-736(1991) Site-directed mutagenesis of the HtrA (DegP) serine protease, whose proteolytic activity is indispensable for Escherichia coli survival at elevated temperatures (above 42 degrees Celsius) .Skorko-Glonek J., Wawrzynow A., Krzewski K., Kurpierz K., Lipinska B.Gene 163:47-52(1995) The Cpx two-component signal transduction pathway of Escherichia coli regulates transcription of the gene specifying the stress-inducible periplasmic protease, DegP.Danese P.N., Snyder W.B., Cosma C.L., Davis L.J., Silhavy T.J.Genes Dev. 9:387-398(1995) Comparison of the structure of wild-type HtrA heat shock protease and mutant HtrA proteins. A Fourier transform infrared spectroscopic study.Skorko-Glonek J., Krzewski K., Lipinska B., Bertoli E., Tanfani F.J. Biol. Chem. 270:11140-11146(1995) 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) HtrA heat shock protease interacts with phospholipid membranes and undergoes conformational changes.Skorko-Glonek J., Lipinska B., Krzewski K., Zolese G., Bertoli E., Tanfani F.J. Biol. Chem. 272:8974-8982(1997) A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein.Spiess C., Beil A., Ehrmann M.Cell 97:339-347(1999) Escherichia coli DegP protease cleaves between paired hydrophobic residues in a natural substrate the PapA pilin.Jones C.H., Dexter P., Evans A.K., Liu C., Hultgren S.J., Hruby D.E.J. Bacteriol. 184:5762-5771(2002) The N-terminal region of HtrA heat shock protease from Escherichia coli is essential for stabilization of HtrA primary structure and maintaining of its oligomeric structure.Skorko-Glonek J., Zurawa D., Tanfani F., Scire A., Wawrzynow A., Narkiewicz J., Bertoli E., Lipinska B.Biochim. Biophys. Acta 1649:171-182(2003) Interplay of PDZ and protease domain of DegP ensures efficient elimination of misfolded proteins.Krojer T., Pangerl K., Kurt J., Sawa J., Stingl C., Mechtler K., Huber R., Ehrmann M., Clausen T.Proc. Natl. Acad. Sci. U.S.A. 105:7702-7707(2008) Activation of DegP chaperone-protease via formation of large cage-like oligomers upon binding to substrate proteins.Jiang J., Zhang X., Chen Y., Wu Y., Zhou Z.H., Chang Z., Sui S.F.Proc. Natl. Acad. Sci. U.S.A. 105:11939-11944(2008) The role of the L2 loop in the regulation and maintaining the proteolytic activity of HtrA (DegP) protein from Escherichia coli.Sobiecka-Szkatula A., Gieldon A., Scire A., Tanfani F., Figaj D., Koper T., Ciarkowski J., Lipinska B., Skorko-Glonek J.Arch. Biochem. Biophys. 500:123-130(2010) Factors defining the functional oligomeric state of Escherichia coli DegP protease.Iwanczyk J., Leong V., Ortega J.PLoS ONE 6:E18944-E18944(2011) Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine.Krojer T., Garrido-Franco M., Huber R., Ehrmann M., Clausen T.Nature 416:455-459(2002) Roles of DegP in prevention of protein misfolding in the periplasm upon overexpression of penicillin acylase in Escherichia coli.Pan K.L., Hsiao H.C., Weng C.L., Wu M.S., Chou C.P.J. Bacteriol. 185:3020-3030(2003) Structural basis for the regulated protease and chaperone function of DegP.Krojer T., Sawa J., Schafer E., Saibil H.R., Ehrmann M., Clausen T.Nature 453:885-890(2008) HtrA proteases have a conserved activation mechanism that can be triggered by distinct molecular cues.Krojer T., Sawa J., Huber R., Clausen T.Nat. Struct. Mol. Biol. 17:844-852(2010) Covalent linkage of distinct substrate degrons controls assembly and disassembly of DegP proteolytic cages.Kim S., Grant R.A., Sauer R.T.Cell 145:67-78(2011)

16128154

NP_414703.1

NC_000913.3

P0C0V0

62.8kD

Cationic Antimicrobial Peptide (CAMP) Resistance Pathway (1185584); Cationic Antimicrobial Peptide (CAMP) Resistance Pathway (1201183); Cationic Antimicrobial Peptide (CAMP) Resistance, Envelope Protein Folding And Degrading Factors DegP And DsbA Pathway (1201460); Cationic Antimicrobial Peptide (CAMP) Resistance, Envelope Protein Folding And Degrading Factors DegP And DsbA Pathway (1208953); Two-component System Pathway (1114); Two-component System Pathway (437)

Autocleavage occurs after Cys95(Cys69 of mature form) or Gln108 (Gln82 of mature form). [More information is available at EcoGene: EG10463]. Protease Do, or DegP, is a periplasmic serine protease required for survival at high temperatures . [More information is available at EcoCyc: EG10463].

0.05 mg (E-Coli)

190 USD

0.05 mg (Yeast)

190

0.2 mg (E-Coli)

460

0.2 mg (Yeast)

460

0.5 mg (Yeast)

750