DEGP_ECOLI
ID DEGP_ECOLI Reviewed; 474 AA.
AC P0C0V0; P09376; P15724;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Periplasmic serine endoprotease DegP;
DE EC=3.4.21.107 {ECO:0000269|PubMed:8830688};
DE AltName: Full=Heat shock protein DegP;
DE AltName: Full=Protease Do;
DE Flags: Precursor;
GN Name=degP; Synonyms=htrA, ptd; OrderedLocusNames=b0161, JW0157;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=K12;
RX PubMed=3057437; DOI=10.1093/nar/16.21.10053;
RA Lipinska B., Sharma S., Georgopoulos C.;
RT "Sequence analysis and regulation of the htrA gene of Escherichia coli: a
RT sigma 32-independent mechanism of heat-inducible transcription.";
RL Nucleic Acids Res. 16:10053-10067(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8202364; DOI=10.1093/nar/22.9.1637;
RA Fujita N., Mori H., Yura T., Ishihama A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-
RT 4.1 min (110,917-193,643 bp) region.";
RL Nucleic Acids Res. 22:1637-1639(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50.
RC STRAIN=K12;
RX PubMed=2165018; DOI=10.1016/0378-1119(90)90200-b;
RA Quirk S., Bhatnagar S.K., Bessman M.J.;
RT "Primary structure of the deoxyguanosine triphosphate triphosphohydrolase-
RT encoding gene (dgt) of Escherichia coli.";
RL Gene 89:13-18(1990).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
RX PubMed=2157212; DOI=10.1073/pnas.87.7.2740;
RA Wurgler S.M., Richardson C.C.;
RT "Structure and regulation of the gene for dGTP triphosphohydrolase from
RT Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:2740-2744(1990).
RN [8]
RP PROTEIN SEQUENCE OF 27-39, FUNCTION AS A SERINE PROTEASE, AND ACTIVITY
RP REGULATION.
RC STRAIN=K12;
RX PubMed=2180903; DOI=10.1128/jb.172.4.1791-1797.1990;
RA Lipinska B., Zylicz M., Georgopoulos C.;
RT "The HtrA (DegP) protein, essential for Escherichia coli survival at high
RT temperatures, is an endopeptidase.";
RL J. Bacteriol. 172:1791-1797(1990).
RN [9]
RP PROTEIN SEQUENCE OF 27-30.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9600841; DOI=10.1006/jmbi.1998.1726;
RA Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C.,
RA Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L.,
RA Hochstrasser D.F.;
RT "Protein identification with N and C-terminal sequence tags in proteome
RT projects.";
RL J. Mol. Biol. 278:599-608(1998).
RN [10]
RP IDENTITY OF HTRA AND PROTEASE DO.
RX PubMed=2025286; DOI=10.1016/s0006-291x(05)80245-1;
RA Seol J.H., Woo S.K., Jung E.M., Yoo S.J., Lee C.S., Kim K.J., Tanaka K.,
RA Ichihara A., Ha D.B., Chung C.H.;
RT "Protease Do is essential for survival of Escherichia coli at high
RT temperatures: its identity with the htrA gene product.";
RL Biochem. Biophys. Res. Commun. 176:730-736(1991).
RN [11]
RP FUNCTION, AND MUTAGENESIS OF HIS-131 AND SER-236.
RX PubMed=7557477; DOI=10.1016/0378-1119(95)00406-v;
RA Skorko-Glonek J., Wawrzynow A., Krzewski K., Kurpierz K., Lipinska B.;
RT "Site-directed mutagenesis of the HtrA (DegP) serine protease, whose
RT proteolytic activity is indispensable for Escherichia coli survival at
RT elevated temperatures (above 42 degrees Celsius).";
RL Gene 163:47-52(1995).
RN [12]
RP INDUCTION.
RC STRAIN=K12 / MC4100;
RX PubMed=7883164; DOI=10.1101/gad.9.4.387;
RA Danese P.N., Snyder W.B., Cosma C.L., Davis L.J., Silhavy T.J.;
RT "The Cpx two-component signal transduction pathway of Escherichia coli
RT regulates transcription of the gene specifying the stress-inducible
RT periplasmic protease, DegP.";
RL Genes Dev. 9:387-398(1995).
RN [13]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=7744744; DOI=10.1074/jbc.270.19.11140;
RA Skorko-Glonek J., Krzewski K., Lipinska B., Bertoli E., Tanfani F.;
RT "Comparison of the structure of wild-type HtrA heat shock protease and
RT mutant HtrA proteins. A Fourier transform infrared spectroscopic study.";
RL J. Biol. Chem. 270:11140-11146(1995).
RN [14]
RP FUNCTION AS A SERINE PROTEASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
RP AND SUBUNIT.
RX PubMed=8830688; DOI=10.1128/jb.178.20.5925-5929.1996;
RA Kolmar H., Waller P.R., Sauer R.T.;
RT "The DegP and DegQ periplasmic endoproteases of Escherichia coli:
RT specificity for cleavage sites and substrate conformation.";
RL J. Bacteriol. 178:5925-5929(1996).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=9083020; DOI=10.1074/jbc.272.14.8974;
RA Skorko-Glonek J., Lipinska B., Krzewski K., Zolese G., Bertoli E.,
RA Tanfani F.;
RT "HtrA heat shock protease interacts with phospholipid membranes and
RT undergoes conformational changes.";
RL J. Biol. Chem. 272:8974-8982(1997).
RN [16]
RP INDUCTION.
RX PubMed=9351822; DOI=10.1093/emboj/16.21.6394;
RA Jones C.H., Danese P.N., Pinkner J.S., Silhavy T.J., Hultgren S.J.;
RT "The chaperone-assisted membrane release and folding pathway is sensed by
RT two signal transduction systems.";
RL EMBO J. 16:6394-6406(1997).
RN [17]
RP FUNCTION AS A CHAPERONE AND AS A SERINE PROTEASE.
RX PubMed=10319814; DOI=10.1016/s0092-8674(00)80743-6;
RA Spiess C., Beil A., Ehrmann M.;
RT "A temperature-dependent switch from chaperone to protease in a widely
RT conserved heat shock protein.";
RL Cell 97:339-347(1999).
RN [18]
RP SUBSTRATE SPECIFICITY.
RX PubMed=12270835; DOI=10.1128/jb.184.20.5762-5771.2002;
RA Jones C.H., Dexter P., Evans A.K., Liu C., Hultgren S.J., Hruby D.E.;
RT "Escherichia coli DegP protease cleaves between paired hydrophobic residues
RT in a natural substrate: the PapA pilin.";
RL J. Bacteriol. 184:5762-5771(2002).
RN [19]
RP DISULFIDE BOND.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=12878036; DOI=10.1016/s1570-9639(03)00170-5;
RA Skorko-Glonek J., Zurawa D., Tanfani F., Scire A., Wawrzynow A.,
RA Narkiewicz J., Bertoli E., Lipinska B.;
RT "The N-terminal region of HtrA heat shock protease from Escherichia coli is
RT essential for stabilization of HtrA primary structure and maintaining of
RT its oligomeric structure.";
RL Biochim. Biophys. Acta 1649:171-182(2003).
RN [20]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100;
RX PubMed=16166523; DOI=10.1128/jb.187.19.6622-6630.2005;
RA Buelow D.R., Raivio T.L.;
RT "Cpx signal transduction is influenced by a conserved N-terminal domain in
RT the novel inhibitor CpxP and the periplasmic protease DegP.";
RL J. Bacteriol. 187:6622-6630(2005).
RN [21]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100;
RX PubMed=16303867; DOI=10.1073/pnas.0508936102;
RA Isaac D.D., Pinkner J.S., Hultgren S.J., Silhavy T.J.;
RT "The extracytoplasmic adaptor protein CpxP is degraded with substrate by
RT DegP.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:17775-17779(2005).
RN [22]
RP FUNCTION IN PREVENTION OF PROTEIN MISFOLDING.
RX PubMed=18505836; DOI=10.1073/pnas.0803392105;
RA Krojer T., Pangerl K., Kurt J., Sawa J., Stingl C., Mechtler K., Huber R.,
RA Ehrmann M., Clausen T.;
RT "Interplay of PDZ and protease domain of DegP ensures efficient elimination
RT of misfolded proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:7702-7707(2008).
RN [23]
RP SUBUNIT.
RX PubMed=18697939; DOI=10.1073/pnas.0805464105;
RA Jiang J., Zhang X., Chen Y., Wu Y., Zhou Z.H., Chang Z., Sui S.F.;
RT "Activation of DegP chaperone-protease via formation of large cage-like
RT oligomers upon binding to substrate proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:11939-11944(2008).
RN [24]
RP ROLE IN HYDROXYUREA RESISTANCE, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=20005847; DOI=10.1016/j.molcel.2009.11.024;
RA Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J.,
RA Walker G.C.;
RT "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia
RT coli.";
RL Mol. Cell 36:845-860(2009).
RN [25]
RP MUTAGENESIS OF ILE-254; LEU-255; ASP-258; ASN-261; ILE-262 AND ILE-264.
RX PubMed=20515644; DOI=10.1016/j.abb.2010.05.028;
RA Sobiecka-Szkatula A., Gieldon A., Scire A., Tanfani F., Figaj D., Koper T.,
RA Ciarkowski J., Lipinska B., Skorko-Glonek J.;
RT "The role of the L2 loop in the regulation and maintaining the proteolytic
RT activity of HtrA (DegP) protein from Escherichia coli.";
RL Arch. Biochem. Biophys. 500:123-130(2010).
RN [26]
RP OLIGOMERIZATION, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RX PubMed=21526129; DOI=10.1371/journal.pone.0018944;
RA Iwanczyk J., Leong V., Ortega J.;
RT "Factors defining the functional oligomeric state of Escherichia coli DegP
RT protease.";
RL PLoS ONE 6:E18944-E18944(2011).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 27-474 OF MUTANT SER-236, AND
RP SUBUNIT.
RX PubMed=11919638; DOI=10.1038/416455a;
RA Krojer T., Garrido-Franco M., Huber R., Ehrmann M., Clausen T.;
RT "Crystal structure of DegP (HtrA) reveals a new protease-chaperone
RT machine.";
RL Nature 416:455-459(2002).
RN [28]
RP FUNCTION IN PREVENTION OF PROTEIN MISFOLDING, AND MUTAGENESIS OF SER-236.
RX PubMed=12730160; DOI=10.1128/jb.185.10.3020-3030.2003;
RA Pan K.L., Hsiao H.C., Weng C.L., Wu M.S., Chou C.P.;
RT "Roles of DegP in prevention of protein misfolding in the periplasm upon
RT overexpression of penicillin acylase in Escherichia coli.";
RL J. Bacteriol. 185:3020-3030(2003).
RN [29]
RP STRUCTURE BY ELECTRON MICROSCOPY (28.0 ANGSTROMS) OF 27-474 OF MUTANT
RP SER-236 IN COMPLEX WITH ANALOG SUBSTRATE, FUNCTION AS A CHAPERONE AND AS A
RP SERINE PROTEASE, OLIGOMERIZATION, AND SUBUNIT.
RX PubMed=18496527; DOI=10.1038/nature07004;
RA Krojer T., Sawa J., Schafer E., Saibil H.R., Ehrmann M., Clausen T.;
RT "Structural basis for the regulated protease and chaperone function of
RT DegP.";
RL Nature 453:885-890(2008).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 27-474 IN COMPLEX WITH ANALOG
RP SUBSTRATE, OLIGOMERIZATION, SUBUNIT, AND ACTIVE SITE.
RX PubMed=20581825; DOI=10.1038/nsmb.1840;
RA Krojer T., Sawa J., Huber R., Clausen T.;
RT "HtrA proteases have a conserved activation mechanism that can be triggered
RT by distinct molecular cues.";
RL Nat. Struct. Mol. Biol. 17:844-852(2010).
RN [31]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 27-474 IN COMPLEX WITH ANALOG
RP SUBSTRATE, OLIGOMERIZATION, AND SUBUNIT.
RX PubMed=21458668; DOI=10.1016/j.cell.2011.02.024;
RA Kim S., Grant R.A., Sauer R.T.;
RT "Covalent linkage of distinct substrate degrons controls assembly and
RT disassembly of DegP proteolytic cages.";
RL Cell 145:67-78(2011).
CC -!- FUNCTION: DegP acts as a chaperone at low temperatures but switches to
CC a peptidase (heat shock protein) at higher temperatures
CC (PubMed:10319814). Degrades transiently denatured and unfolded or
CC misfolded proteins which accumulate in the periplasm following heat
CC shock or other stress conditions (PubMed:16303867). DegP is efficient
CC with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for
CC beta-branched side chain amino acids (PubMed:8830688). Only unfolded
CC proteins devoid of disulfide bonds appear capable of being cleaved,
CC thereby preventing non-specific proteolysis of folded proteins
CC (PubMed:8830688). Its proteolytic activity is essential for the
CC survival of cells at elevated temperatures (PubMed:7557477). It can
CC degrade IciA, Ada, casein, globin and PapA. DegP shares specificity
CC with DegQ (PubMed:8830688). DegP is also involved in the biogenesis of
CC partially folded outer-membrane proteins (OMP).
CC {ECO:0000269|PubMed:10319814, ECO:0000269|PubMed:12730160,
CC ECO:0000269|PubMed:16303867, ECO:0000269|PubMed:18496527,
CC ECO:0000269|PubMed:18505836, ECO:0000269|PubMed:2180903,
CC ECO:0000269|PubMed:7557477, ECO:0000269|PubMed:8830688}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Acts on substrates that are at least partially unfolded. The
CC cleavage site P1 residue is normally between a pair of hydrophobic
CC residues, such as Val-|-Val.; EC=3.4.21.107;
CC Evidence={ECO:0000269|PubMed:8830688};
CC -!- ACTIVITY REGULATION: Inhibited by diisopropylfluorophosphate (DFP).
CC {ECO:0000269|PubMed:2180903}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is around 55 degrees Celsius. In the range from
CC 37 to 55 degrees Celsius, the proteolytic activity rapidly increases
CC with temperature. {ECO:0000269|PubMed:7744744};
CC -!- SUBUNIT: DegP can reversibly switch between different oligomeric forms
CC that represent inactive (6-mer) and active (12- and 24-mer) protease
CC states. Substrate binding triggers the conversion of the resting DegP
CC trimer and hexamer into catalytically active 12- and 24-mers. The
CC conversion of 6-mer (DegP6) into 12-mer (DegP12) or 24-mer (DegP24) is
CC crucial in regulating protease activity. {ECO:0000269|PubMed:11919638,
CC ECO:0000269|PubMed:18496527, ECO:0000269|PubMed:18697939,
CC ECO:0000269|PubMed:20581825, ECO:0000269|PubMed:21458668,
CC ECO:0000269|PubMed:21526129, ECO:0000269|PubMed:8830688}.
CC -!- INTERACTION:
CC P0C0V0; P0C0V0: degP; NbExp=16; IntAct=EBI-547165, EBI-547165;
CC P0C0V0; P0A910: ompA; NbExp=8; IntAct=EBI-547165, EBI-371347;
CC P0C0V0; P06996: ompC; NbExp=7; IntAct=EBI-547165, EBI-371155;
CC P0C0V0; P02666: CSN2; Xeno; NbExp=9; IntAct=EBI-547165, EBI-5260183;
CC P0C0V0; P00698: LYZ; Xeno; NbExp=11; IntAct=EBI-547165, EBI-1029543;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:9083020};
CC Peripheral membrane protein {ECO:0000269|PubMed:9083020}; Cytoplasmic
CC side {ECO:0000269|PubMed:9083020}.
CC -!- INDUCTION: By heat shock (PubMed:3057437). Transcriptionally up-
CC regulated by sigma-E factor and the Cpx two-component signal
CC transduction pathway (PubMed:7883164, PubMed:9351822).
CC {ECO:0000269|PubMed:3057437, ECO:0000269|PubMed:7883164,
CC ECO:0000269|PubMed:9351822}.
CC -!- DISRUPTION PHENOTYPE: Decreased induction of Cpx two-component
CC regulatory system (PubMed:16166523). Increased accumulation of
CC periplasmic accessory protein CpxP, increased accumulation and toxicity
CC of overexpressed, misfolded periplasmic proteins (PubMed:16303867).
CC Increased resistance to hydroxyurea, probably due to decreased
CC degradation of misfolded proteins which eventually leads to decreased
CC OH radical formation (PubMed:20005847). {ECO:0000269|PubMed:16166523,
CC ECO:0000269|PubMed:16303867, ECO:0000269|PubMed:20005847}.
CC -!- MISCELLANEOUS: DegP is indispensable for bacterial survival at
CC temperatures above 42 degrees Celsius, however is also able to digest
CC its natural substrates in a reducing environment at temperatures as low
CC as 20 degrees Celsius.
CC -!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
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DR EMBL; M36536; AAA23994.1; -; Genomic_DNA.
DR EMBL; X12457; CAA30997.1; -; Genomic_DNA.
DR EMBL; U70214; AAB08591.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73272.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96738.1; -; Genomic_DNA.
DR EMBL; M29955; AAA23717.1; -; Genomic_DNA.
DR EMBL; M31772; AAA23680.1; -; Genomic_DNA.
DR PIR; S45229; S45229.
DR RefSeq; NP_414703.1; NC_000913.3.
DR RefSeq; WP_000753946.1; NZ_SSZK01000004.1.
DR PDB; 1KY9; X-ray; 2.80 A; A/B=27-474.
DR PDB; 2ZLE; EM; 28.00 A; A/B/C/E/F/G/H/I/J/K/L/M=27-474.
DR PDB; 3CS0; X-ray; 3.00 A; A=27-474.
DR PDB; 3MH4; X-ray; 3.10 A; A/B=27-474.
DR PDB; 3MH5; X-ray; 3.00 A; A/B=27-474.
DR PDB; 3MH6; X-ray; 3.60 A; A=27-474.
DR PDB; 3MH7; X-ray; 2.96 A; A=27-474.
DR PDB; 3OTP; X-ray; 3.76 A; A/B/C/D/E/F=27-474.
DR PDB; 3OU0; X-ray; 3.00 A; A=27-474.
DR PDB; 4A8D; EM; 28.00 A; A/B/C/D/E/F/G/H/I/J/K/L=27-474.
DR PDB; 6JJK; X-ray; 3.60 A; A/B/C/D/E/F=35-474.
DR PDB; 6JJL; X-ray; 4.20 A; A/B/C/D/E/F=35-474.
DR PDB; 6JJO; X-ray; 4.16 A; A/B/C/D/E/F=27-474.
DR PDBsum; 1KY9; -.
DR PDBsum; 2ZLE; -.
DR PDBsum; 3CS0; -.
DR PDBsum; 3MH4; -.
DR PDBsum; 3MH5; -.
DR PDBsum; 3MH6; -.
DR PDBsum; 3MH7; -.
DR PDBsum; 3OTP; -.
DR PDBsum; 3OU0; -.
DR PDBsum; 4A8D; -.
DR PDBsum; 6JJK; -.
DR PDBsum; 6JJL; -.
DR PDBsum; 6JJO; -.
DR AlphaFoldDB; P0C0V0; -.
DR SMR; P0C0V0; -.
DR BioGRID; 4260994; 967.
DR DIP; DIP-46256N; -.
DR IntAct; P0C0V0; 20.
DR MINT; P0C0V0; -.
DR STRING; 511145.b0161; -.
DR MEROPS; S01.273; -.
DR MoonProt; P0C0V0; -.
DR SWISS-2DPAGE; P0C0V0; -.
DR jPOST; P0C0V0; -.
DR PaxDb; P0C0V0; -.
DR PRIDE; P0C0V0; -.
DR EnsemblBacteria; AAC73272; AAC73272; b0161.
DR EnsemblBacteria; BAB96738; BAB96738; BAB96738.
DR GeneID; 67416238; -.
DR GeneID; 947139; -.
DR KEGG; ecj:JW0157; -.
DR KEGG; eco:b0161; -.
DR PATRIC; fig|1411691.4.peg.2119; -.
DR EchoBASE; EB0458; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_1_1_6; -.
DR InParanoid; P0C0V0; -.
DR OMA; NRSVSMR; -.
DR PhylomeDB; P0C0V0; -.
DR BioCyc; EcoCyc:EG10463-MON; -.
DR BioCyc; MetaCyc:EG10463-MON; -.
DR BRENDA; 3.4.21.107; 2026.
DR EvolutionaryTrace; P0C0V0; -.
DR PRO; PR:P0C0V0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0042597; C:periplasmic space; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0008233; F:peptidase activity; IDA:EcoCyc.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:EcoCyc.
DR GO; GO:0008236; F:serine-type peptidase activity; IMP:EcoCyc.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:EcoCyc.
DR GO; GO:0006457; P:protein folding; IMP:EcoliWiki.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IDA:EcoCyc.
DR GO; GO:0006508; P:proteolysis; IDA:EcoCyc.
DR GO; GO:0009408; P:response to heat; IMP:EcoCyc.
DR GO; GO:0006979; P:response to oxidative stress; IEP:EcoliWiki.
DR GO; GO:0009266; P:response to temperature stimulus; IEP:EcoliWiki.
DR Gene3D; 2.30.42.10; -; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011782; Pept_S1C_Do.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR001940; Peptidase_S1C.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 2.
DR SUPFAM; SSF50156; SSF50156; 2.
DR SUPFAM; SSF50494; SSF50494; 1.
DR TIGRFAMs; TIGR02037; degP_htrA_DO; 1.
DR PROSITE; PS50106; PDZ; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Hydrolase; Membrane; Protease;
KW Reference proteome; Repeat; Serine protease; Signal; Stress response.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:2180903,
FT ECO:0000269|PubMed:9600841"
FT CHAIN 27..474
FT /note="Periplasmic serine endoprotease DegP"
FT /id="PRO_0000026921"
FT DOMAIN 280..371
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 377..466
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT ACT_SITE 131
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:20581825"
FT ACT_SITE 161
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:20581825"
FT ACT_SITE 236
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:20581825"
FT BINDING 58
FT /ligand="substrate"
FT BINDING 131
FT /ligand="substrate"
FT BINDING 161
FT /ligand="substrate"
FT BINDING 234..236
FT /ligand="substrate"
FT BINDING 252..256
FT /ligand="substrate"
FT BINDING 291..295
FT /ligand="substrate"
FT DISULFID 83..95
FT /evidence="ECO:0000269|PubMed:12878036"
FT MUTAGEN 131
FT /note="H->R: Loss of peptidase activity with no detectable
FT changes in secondary structure."
FT /evidence="ECO:0000269|PubMed:7557477"
FT MUTAGEN 236
FT /note="S->A: Loss of peptidase activity with no detectable
FT changes in secondary structure."
FT /evidence="ECO:0000269|PubMed:12730160,
FT ECO:0000269|PubMed:7557477"
FT MUTAGEN 254
FT /note="I->N: It does not affect the proteolytic activity."
FT /evidence="ECO:0000269|PubMed:20515644"
FT MUTAGEN 255
FT /note="L->N: Loss of proteolytic activity."
FT /evidence="ECO:0000269|PubMed:20515644"
FT MUTAGEN 258
FT /note="D->V: Increases the proteolytic activity."
FT /evidence="ECO:0000269|PubMed:20515644"
FT MUTAGEN 261
FT /note="N->I: Loss of proteolytic activity."
FT /evidence="ECO:0000269|PubMed:20515644"
FT MUTAGEN 262
FT /note="I->N: Stimulates the proteolytic activity at low
FT temperatures (20-30 degrees Celsius), whereas at higher
FT temperatures (above 35 degrees Celsius), the proteolytic
FT activity is less efficient."
FT /evidence="ECO:0000269|PubMed:20515644"
FT MUTAGEN 264
FT /note="I->N: Loss of proteolytic activity."
FT /evidence="ECO:0000269|PubMed:20515644"
FT CONFLICT 10
FT /note="A -> R (in Ref. 1; AAA23994 and 7; AAA23680)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="E -> Q (in Ref. 6; AAA23717)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="A -> G (in Ref. 1; AAA23994/CAA30997)"
FT /evidence="ECO:0000305"
FT CONFLICT 467..474
FT /note="STIYLLMQ -> RHLPVNAVISLNPFLKTGRGSPYNL (in Ref. 1;
FT AAA23994/CAA30997)"
FT /evidence="ECO:0000305"
FT HELIX 42..48
FT /evidence="ECO:0007829|PDB:1KY9"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:1KY9"
FT STRAND 52..63
FT /evidence="ECO:0007829|PDB:1KY9"
FT STRAND 106..120
FT /evidence="ECO:0007829|PDB:1KY9"
FT TURN 121..124
FT /evidence="ECO:0007829|PDB:1KY9"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:1KY9"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:1KY9"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:1KY9"
FT STRAND 148..157
FT /evidence="ECO:0007829|PDB:1KY9"
FT TURN 158..161
FT /evidence="ECO:0007829|PDB:1KY9"
FT STRAND 162..169
FT /evidence="ECO:0007829|PDB:1KY9"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:1KY9"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:1KY9"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:1KY9"
FT STRAND 202..213
FT /evidence="ECO:0007829|PDB:1KY9"
FT TURN 216..219
FT /evidence="ECO:0007829|PDB:3MH7"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:1KY9"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:1KY9"
FT STRAND 247..252
FT /evidence="ECO:0007829|PDB:1KY9"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:3MH7"
FT STRAND 262..269
FT /evidence="ECO:0007829|PDB:1KY9"
FT HELIX 270..283
FT /evidence="ECO:0007829|PDB:1KY9"
FT STRAND 293..297
FT /evidence="ECO:0007829|PDB:3MH7"
FT HELIX 301..304
FT /evidence="ECO:0007829|PDB:1KY9"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:1KY9"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:1KY9"
FT TURN 326..329
FT /evidence="ECO:0007829|PDB:1KY9"
FT STRAND 338..343
FT /evidence="ECO:0007829|PDB:1KY9"
FT HELIX 348..353
FT /evidence="ECO:0007829|PDB:1KY9"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:1KY9"
FT STRAND 364..371
FT /evidence="ECO:0007829|PDB:1KY9"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:1KY9"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:1KY9"
FT STRAND 388..393
FT /evidence="ECO:0007829|PDB:1KY9"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:3MH7"
FT TURN 406..408
FT /evidence="ECO:0007829|PDB:1KY9"
FT STRAND 411..415
FT /evidence="ECO:0007829|PDB:3MH7"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:3OU0"
FT HELIX 423..425
FT /evidence="ECO:0007829|PDB:1KY9"
FT STRAND 432..436
FT /evidence="ECO:0007829|PDB:1KY9"
FT HELIX 444..450
FT /evidence="ECO:0007829|PDB:1KY9"
FT TURN 451..453
FT /evidence="ECO:0007829|PDB:1KY9"
FT STRAND 460..466
FT /evidence="ECO:0007829|PDB:1KY9"
FT STRAND 468..471
FT /evidence="ECO:0007829|PDB:1KY9"
SQ SEQUENCE 474 AA; 49354 MW; 5482E596F74B6D5F CRC64;
MKKTTLALSA LALSLGLALS PLSATAAETS SATTAQQMPS LAPMLEKVMP SVVSINVEGS
TTVNTPRMPR NFQQFFGDDS PFCQEGSPFQ SSPFCQGGQG GNGGGQQQKF MALGSGVIID
ADKGYVVTNN HVVDNATVIK VQLSDGRKFD AKMVGKDPRS DIALIQIQNP KNLTAIKMAD
SDALRVGDYT VAIGNPFGLG ETVTSGIVSA LGRSGLNAEN YENFIQTDAA INRGNSGGAL
VNLNGELIGI NTAILAPDGG NIGIGFAIPS NMVKNLTSQM VEYGQVKRGE LGIMGTELNS
ELAKAMKVDA QRGAFVSQVL PNSSAAKAGI KAGDVITSLN GKPISSFAAL RAQVGTMPVG
SKLTLGLLRD GKQVNVNLEL QQSSQNQVDS SSIFNGIEGA EMSNKGKDQG VVVNNVKTGT
PAAQIGLKKG DVIIGANQQA VKNIAELRKV LDSKPSVLAL NIQRGDSTIY LLMQ
