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Periplasmic serine endoprotease DegP (EC 3.4.21.107) (Heat shock protein DegP) (Protease Do)

 DEGP_ECOLI              Reviewed;         474 AA.
P0C0V0; P09376; P15724;
20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
20-DEC-2005, sequence version 1.
28-MAR-2018, entry version 118.
RecName: Full=Periplasmic serine endoprotease DegP;
EC=3.4.21.107 {ECO:0000269|PubMed:8830688};
AltName: Full=Heat shock protein DegP;
AltName: Full=Protease Do;
Flags: Precursor;
Name=degP; Synonyms=htrA, ptd; OrderedLocusNames=b0161, JW0157;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
STRAIN=K12;
PubMed=3057437; DOI=10.1093/nar/16.21.10053;
Lipinska B., Sharma S., Georgopoulos C.;
"Sequence analysis and regulation of the htrA gene of Escherichia
coli: a sigma 32-independent mechanism of heat-inducible
transcription.";
Nucleic Acids Res. 16:10053-10067(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=8202364; DOI=10.1093/nar/22.9.1637;
Fujita N., Mori H., Yura T., Ishihama A.;
"Systematic sequencing of the Escherichia coli genome: analysis of the
2.4-4.1 min (110,917-193,643 bp) region.";
Nucleic Acids Res. 22:1637-1639(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
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.;
"Sequence of minutes 4-25 of Escherichia coli.";
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
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.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50.
STRAIN=K12;
PubMed=2165018; DOI=10.1016/0378-1119(90)90200-B;
Quirk S., Bhatnagar S.K., Bessman M.J.;
"Primary structure of the deoxyguanosine triphosphate
triphosphohydrolase-encoding gene (dgt) of Escherichia coli.";
Gene 89:13-18(1990).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
PubMed=2157212; DOI=10.1073/pnas.87.7.2740;
Wurgler S.M., Richardson C.C.;
"Structure and regulation of the gene for dGTP triphosphohydrolase
from Escherichia coli.";
Proc. Natl. Acad. Sci. U.S.A. 87:2740-2744(1990).
[8]
PROTEIN SEQUENCE OF 27-39, FUNCTION AS A SERINE PROTEASE, AND ENZYME
REGULATION.
STRAIN=K12;
PubMed=2180903; DOI=10.1128/jb.172.4.1791-1797.1990;
Lipinska B., Zylicz M., Georgopoulos C.;
"The HtrA (DegP) protein, essential for Escherichia coli survival at
high temperatures, is an endopeptidase.";
J. Bacteriol. 172:1791-1797(1990).
[9]
PROTEIN SEQUENCE OF 27-30.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9600841; DOI=10.1006/jmbi.1998.1726;
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.;
"Protein identification with N and C-terminal sequence tags in
proteome projects.";
J. Mol. Biol. 278:599-608(1998).
[10]
IDENTITY OF HTRA AND PROTEASE DO.
PubMed=2025286; DOI=10.1016/S0006-291X(05)80245-1;
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.;
"Protease Do is essential for survival of Escherichia coli at high
temperatures: its identity with the htrA gene product.";
Biochem. Biophys. Res. Commun. 176:730-736(1991).
[11]
FUNCTION, AND MUTAGENESIS OF HIS-131 AND SER-236.
PubMed=7557477; DOI=10.1016/0378-1119(95)00406-V;
Skorko-Glonek J., Wawrzynow A., Krzewski K., Kurpierz K., Lipinska B.;
"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).";
Gene 163:47-52(1995).
[12]
INDUCTION.
STRAIN=K12 / MC4100;
PubMed=7883164; DOI=10.1101/gad.9.4.387;
Danese P.N., Snyder W.B., Cosma C.L., Davis L.J., Silhavy T.J.;
"The Cpx two-component signal transduction pathway of Escherichia coli
regulates transcription of the gene specifying the stress-inducible
periplasmic protease, DegP.";
Genes Dev. 9:387-398(1995).
[13]
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=7744744; DOI=10.1074/jbc.270.19.11140;
Skorko-Glonek J., Krzewski K., Lipinska B., Bertoli E., Tanfani F.;
"Comparison of the structure of wild-type HtrA heat shock protease and
mutant HtrA proteins. A Fourier transform infrared spectroscopic
study.";
J. Biol. Chem. 270:11140-11146(1995).
[14]
FUNCTION AS A SERINE PROTEASE, CATALYTIC ACTIVITY, SUBSTRATE
SPECIFICITY, AND SUBUNIT.
PubMed=8830688; DOI=10.1128/jb.178.20.5925-5929.1996;
Kolmar H., Waller P.R., Sauer R.T.;
"The DegP and DegQ periplasmic endoproteases of Escherichia coli:
specificity for cleavage sites and substrate conformation.";
J. Bacteriol. 178:5925-5929(1996).
[15]
SUBCELLULAR LOCATION.
PubMed=9083020;
Skorko-Glonek J., Lipinska B., Krzewski K., Zolese G., Bertoli E.,
Tanfani F.;
"HtrA heat shock protease interacts with phospholipid membranes and
undergoes conformational changes.";
J. Biol. Chem. 272:8974-8982(1997).
[16]
INDUCTION.
PubMed=9351822; DOI=10.1093/emboj/16.21.6394;
Jones C.H., Danese P.N., Pinkner J.S., Silhavy T.J., Hultgren S.J.;
"The chaperone-assisted membrane release and folding pathway is sensed
by two signal transduction systems.";
EMBO J. 16:6394-6406(1997).
[17]
FUNCTION AS A CHAPERONE AND AS A SERINE PROTEASE.
PubMed=10319814; DOI=10.1016/S0092-8674(00)80743-6;
Spiess C., Beil A., Ehrmann M.;
"A temperature-dependent switch from chaperone to protease in a widely
conserved heat shock protein.";
Cell 97:339-347(1999).
[18]
SUBSTRATE SPECIFICITY.
PubMed=12270835; DOI=10.1128/JB.184.20.5762-5771.2002;
Jones C.H., Dexter P., Evans A.K., Liu C., Hultgren S.J., Hruby D.E.;
"Escherichia coli DegP protease cleaves between paired hydrophobic
residues in a natural substrate: the PapA pilin.";
J. Bacteriol. 184:5762-5771(2002).
[19]
DISULFIDE BOND.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=12878036;
Skorko-Glonek J., Zurawa D., Tanfani F., Scire A., Wawrzynow A.,
Narkiewicz J., Bertoli E., Lipinska B.;
"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.";
Biochim. Biophys. Acta 1649:171-182(2003).
[20]
DISRUPTION PHENOTYPE.
STRAIN=K12 / MC4100;
PubMed=16166523; DOI=10.1128/JB.187.19.6622-6630.2005;
Buelow D.R., Raivio T.L.;
"Cpx signal transduction is influenced by a conserved N-terminal
domain in the novel inhibitor CpxP and the periplasmic protease
DegP.";
J. Bacteriol. 187:6622-6630(2005).
[21]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=K12 / MC4100;
PubMed=16303867; DOI=10.1073/pnas.0508936102;
Isaac D.D., Pinkner J.S., Hultgren S.J., Silhavy T.J.;
"The extracytoplasmic adaptor protein CpxP is degraded with substrate
by DegP.";
Proc. Natl. Acad. Sci. U.S.A. 102:17775-17779(2005).
[22]
FUNCTION IN PREVENTION OF PROTEIN MISFOLDING.
PubMed=18505836; DOI=10.1073/pnas.0803392105;
Krojer T., Pangerl K., Kurt J., Sawa J., Stingl C., Mechtler K.,
Huber R., Ehrmann M., Clausen T.;
"Interplay of PDZ and protease domain of DegP ensures efficient
elimination of misfolded proteins.";
Proc. Natl. Acad. Sci. U.S.A. 105:7702-7707(2008).
[23]
SUBUNIT.
PubMed=18697939; DOI=10.1073/pnas.0805464105;
Jiang J., Zhang X., Chen Y., Wu Y., Zhou Z.H., Chang Z., Sui S.F.;
"Activation of DegP chaperone-protease via formation of large cage-
like oligomers upon binding to substrate proteins.";
Proc. Natl. Acad. Sci. U.S.A. 105:11939-11944(2008).
[24]
ROLE IN HYDROXYUREA RESISTANCE, AND DISRUPTION PHENOTYPE.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=20005847; DOI=10.1016/j.molcel.2009.11.024;
Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J.,
Walker G.C.;
"Hydroxyurea induces hydroxyl radical-mediated cell death in
Escherichia coli.";
Mol. Cell 36:845-860(2009).
[25]
MUTAGENESIS OF ILE-254; LEU-255; ASP-258; ASN-261; ILE-262 AND
ILE-264.
PubMed=20515644; DOI=10.1016/j.abb.2010.05.028;
Sobiecka-Szkatula A., Gieldon A., Scire A., Tanfani F., Figaj D.,
Koper T., Ciarkowski J., Lipinska B., Skorko-Glonek J.;
"The role of the L2 loop in the regulation and maintaining the
proteolytic activity of HtrA (DegP) protein from Escherichia coli.";
Arch. Biochem. Biophys. 500:123-130(2010).
[26]
OLIGOMERIZATION, SUBSTRATE SPECIFICITY, AND SUBUNIT.
PubMed=21526129; DOI=10.1371/journal.pone.0018944;
Iwanczyk J., Leong V., Ortega J.;
"Factors defining the functional oligomeric state of Escherichia coli
DegP protease.";
PLoS ONE 6:E18944-E18944(2011).
[27]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 27-474 OF MUTANT SER-236, AND
SUBUNIT.
PubMed=11919638; DOI=10.1038/416455a;
Krojer T., Garrido-Franco M., Huber R., Ehrmann M., Clausen T.;
"Crystal structure of DegP (HtrA) reveals a new protease-chaperone
machine.";
Nature 416:455-459(2002).
[28]
FUNCTION IN PREVENTION OF PROTEIN MISFOLDING, AND MUTAGENESIS OF
SER-236.
PubMed=12730160; DOI=10.1128/JB.185.10.3020-3030.2003;
Pan K.L., Hsiao H.C., Weng C.L., Wu M.S., Chou C.P.;
"Roles of DegP in prevention of protein misfolding in the periplasm
upon overexpression of penicillin acylase in Escherichia coli.";
J. Bacteriol. 185:3020-3030(2003).
[29]
STRUCTURE BY ELECTRON MICROSCOPY (28.0 ANGSTROMS) OF 27-474 OF MUTANT
SER-236 IN COMPLEX WITH ANALOG SUBSTRATE, FUNCTION AS A CHAPERONE AND
AS A SERINE PROTEASE, OLIGOMERIZATION, AND SUBUNIT.
PubMed=18496527; DOI=10.1038/nature07004;
Krojer T., Sawa J., Schafer E., Saibil H.R., Ehrmann M., Clausen T.;
"Structural basis for the regulated protease and chaperone function of
DegP.";
Nature 453:885-890(2008).
[30]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 27-474 IN COMPLEX WITH ANALOG
SUBSTRATE, OLIGOMERIZATION, SUBUNIT, AND ACTIVE SITE.
PubMed=20581825; DOI=10.1038/nsmb.1840;
Krojer T., Sawa J., Huber R., Clausen T.;
"HtrA proteases have a conserved activation mechanism that can be
triggered by distinct molecular cues.";
Nat. Struct. Mol. Biol. 17:844-852(2010).
[31]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 27-474 IN COMPLEX WITH ANALOG
SUBSTRATE, OLIGOMERIZATION, AND SUBUNIT.
PubMed=21458668; DOI=10.1016/j.cell.2011.02.024;
Kim S., Grant R.A., Sauer R.T.;
"Covalent linkage of distinct substrate degrons controls assembly and
disassembly of DegP proteolytic cages.";
Cell 145:67-78(2011).
-!- FUNCTION: DegP acts as a chaperone at low temperatures but
switches to a peptidase (heat shock protein) at higher
temperatures (PubMed:10319814). Degrades transiently denatured and
unfolded or misfolded proteins which accumulate in the periplasm
following heat shock or other stress conditions (PubMed:16303867).
DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds,
suggesting a preference for beta-branched side chain amino acids
(PubMed:8830688). Only unfolded proteins devoid of disulfide bonds
appear capable of being cleaved, thereby preventing non-specific
proteolysis of folded proteins (PubMed:8830688). Its proteolytic
activity is essential for the survival of cells at elevated
temperatures (PubMed:7557477). It can degrade IciA, Ada, casein,
globin and PapA. DegP shares specificity with DegQ
(PubMed:8830688). DegP is also involved in the biogenesis of
partially folded outer-membrane proteins (OMP).
{ECO:0000269|PubMed:10319814, ECO:0000269|PubMed:12730160,
ECO:0000269|PubMed:16303867, ECO:0000269|PubMed:18496527,
ECO:0000269|PubMed:18505836, ECO:0000269|PubMed:2180903,
ECO:0000269|PubMed:7557477, ECO:0000269|PubMed:8830688}.
-!- CATALYTIC ACTIVITY: 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.
{ECO:0000269|PubMed:8830688}.
-!- ENZYME REGULATION: Inhibited by diisopropylfluorophosphate (DFP).
{ECO:0000269|PubMed:2180903}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Temperature dependence:
Optimum temperature is around 55 degrees Celsius. In the range
from 37 to 55 degrees Celsius, the proteolytic activity rapidly
increases with temperature. {ECO:0000269|PubMed:7744744};
-!- SUBUNIT: DegP 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 DegP trimer and hexamer into catalytically active 12- and
24-mers. The conversion of 6-mer (DegP6) into 12-mer (DegP12) or
24-mer (DegP24) is crucial in regulating protease activity.
{ECO:0000269|PubMed:11919638, ECO:0000269|PubMed:18496527,
ECO:0000269|PubMed:18697939, ECO:0000269|PubMed:20581825,
ECO:0000269|PubMed:21458668, ECO:0000269|PubMed:21526129,
ECO:0000269|PubMed:8830688}.
-!- INTERACTION:
Self; NbExp=16; IntAct=EBI-547165, EBI-547165;
P02666:CSN2 (xeno); NbExp=8; IntAct=EBI-547165, EBI-5260183;
P00698:LYZ (xeno); NbExp=11; IntAct=EBI-547165, EBI-1029543;
P0A910:ompA; NbExp=9; IntAct=EBI-547165, EBI-371347;
P06996:ompC; NbExp=7; IntAct=EBI-547165, EBI-371155;
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000269|PubMed:9083020}; Peripheral membrane protein
{ECO:0000269|PubMed:9083020}; Cytoplasmic side
{ECO:0000269|PubMed:9083020}.
-!- INDUCTION: By heat shock (PubMed:3057437). Transcriptionally up-
regulated by sigma-E factor and the Cpx two-component signal
transduction pathway (PubMed:7883164, PubMed:9351822).
{ECO:0000269|PubMed:3057437, ECO:0000269|PubMed:7883164,
ECO:0000269|PubMed:9351822}.
-!- DISRUPTION PHENOTYPE: Decreased induction of Cpx two-component
regulatory system (PubMed:16166523). Increased accumulation of
periplasmic accessory protein CpxP, increased accumulation and
toxicity of overexpressed, misfolded periplasmic proteins
(PubMed:16303867). Increased resistance to hydroxyurea, probably
due to decreased degradation of misfolded proteins which
eventually leads to decreased OH radical formation
(PubMed:20005847). {ECO:0000269|PubMed:16166523,
ECO:0000269|PubMed:16303867, ECO:0000269|PubMed:20005847}.
-!- MISCELLANEOUS: DegP is indispensable for bacterial survival at
temperatures above 42 degrees Celsius, however is also able to
digest its natural substrates in a reducing environment at
temperatures as low as 20 degrees Celsius.
-!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
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EMBL; M36536; AAA23994.1; -; Genomic_DNA.
EMBL; X12457; CAA30997.1; -; Genomic_DNA.
EMBL; U70214; AAB08591.1; -; Genomic_DNA.
EMBL; U00096; AAC73272.1; -; Genomic_DNA.
EMBL; AP009048; BAB96738.1; -; Genomic_DNA.
EMBL; M29955; AAA23717.1; -; Genomic_DNA.
EMBL; M31772; AAA23680.1; -; Genomic_DNA.
PIR; S45229; S45229.
RefSeq; NP_414703.1; NC_000913.3.
RefSeq; WP_000753946.1; NZ_LN832404.1.
PDB; 1KY9; X-ray; 2.80 A; A/B=27-474.
PDB; 2ZLE; EM; 28.00 A; A/B/C/E/F/G/H/I/J/K/L/M=27-474.
PDB; 3CS0; X-ray; 3.00 A; A=27-474.
PDB; 3MH4; X-ray; 3.10 A; A/B=27-474.
PDB; 3MH5; X-ray; 3.00 A; A/B=27-474.
PDB; 3MH6; X-ray; 3.60 A; A=27-474.
PDB; 3MH7; X-ray; 2.96 A; A=27-474.
PDB; 3OTP; X-ray; 3.76 A; A/B/C/D/E/F=27-474.
PDB; 3OU0; X-ray; 3.00 A; A=27-474.
PDB; 4A8D; EM; 28.00 A; A/B/C/D/E/F/G/H/I/J/K/L=27-474.
PDBsum; 1KY9; -.
PDBsum; 2ZLE; -.
PDBsum; 3CS0; -.
PDBsum; 3MH4; -.
PDBsum; 3MH5; -.
PDBsum; 3MH6; -.
PDBsum; 3MH7; -.
PDBsum; 3OTP; -.
PDBsum; 3OU0; -.
PDBsum; 4A8D; -.
ProteinModelPortal; P0C0V0; -.
SMR; P0C0V0; -.
BioGrid; 4260994; 967.
DIP; DIP-46256N; -.
IntAct; P0C0V0; 20.
MINT; P0C0V0; -.
STRING; 316385.ECDH10B_0141; -.
MEROPS; S01.273; -.
SWISS-2DPAGE; P0C0V0; -.
EPD; P0C0V0; -.
PaxDb; P0C0V0; -.
PRIDE; P0C0V0; -.
EnsemblBacteria; AAC73272; AAC73272; b0161.
EnsemblBacteria; BAB96738; BAB96738; BAB96738.
GeneID; 947139; -.
KEGG; ecj:JW0157; -.
KEGG; eco:b0161; -.
PATRIC; fig|1411691.4.peg.2119; -.
EchoBASE; EB0458; -.
EcoGene; EG10463; degP.
eggNOG; ENOG4105C0H; Bacteria.
eggNOG; COG0265; LUCA.
HOGENOM; HOG000223642; -.
InParanoid; P0C0V0; -.
KO; K04771; -.
OMA; FAVPSKT; -.
PhylomeDB; P0C0V0; -.
BioCyc; EcoCyc:EG10463-MONOMER; -.
BioCyc; MetaCyc:EG10463-MONOMER; -.
BRENDA; 3.4.21.107; 2026.
EvolutionaryTrace; P0C0V0; -.
PRO; PR:P0C0V0; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoliWiki.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004252; F:serine-type endopeptidase activity; IDA:EcoliWiki.
GO; GO:0006457; P:protein folding; IMP:EcoliWiki.
GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IMP:EcoliWiki.
GO; GO:0006508; P:proteolysis; IDA:EcoliWiki.
GO; GO:0006979; P:response to oxidative stress; IEP:EcoliWiki.
GO; GO:0009266; P:response to temperature stimulus; IEP:EcoliWiki.
InterPro; IPR001478; PDZ.
InterPro; IPR036034; PDZ_sf.
InterPro; IPR011782; Pept_S1C_Do.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001940; Peptidase_S1C.
Pfam; PF00595; PDZ; 2.
PRINTS; PR00834; PROTEASES2C.
SMART; SM00228; PDZ; 2.
SUPFAM; SSF50156; SSF50156; 2.
SUPFAM; SSF50494; SSF50494; 2.
TIGRFAMs; TIGR02037; degP_htrA_DO; 1.
PROSITE; PS50106; PDZ; 2.
1: Evidence at protein level;
3D-structure; Cell inner membrane; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Hydrolase; Membrane;
Protease; Reference proteome; Repeat; Serine protease; Signal;
Stress response.
SIGNAL 1 26 {ECO:0000269|PubMed:2180903,
ECO:0000269|PubMed:9600841}.
CHAIN 27 474 Periplasmic serine endoprotease DegP.
/FTId=PRO_0000026921.
DOMAIN 280 371 PDZ 1. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 377 466 PDZ 2. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
REGION 234 236 Substrate binding.
REGION 252 256 Substrate binding.
REGION 291 295 Substrate binding.
ACT_SITE 131 131 Charge relay system.
{ECO:0000269|PubMed:20581825}.
ACT_SITE 161 161 Charge relay system.
{ECO:0000269|PubMed:20581825}.
ACT_SITE 236 236 Charge relay system.
{ECO:0000269|PubMed:20581825}.
BINDING 58 58 Substrate.
BINDING 131 131 Substrate.
BINDING 161 161 Substrate.
DISULFID 83 95 {ECO:0000269|PubMed:12878036}.
MUTAGEN 131 131 H->R: Loss of peptidase activity with no
detectable changes in secondary
structure. {ECO:0000269|PubMed:7557477}.
MUTAGEN 236 236 S->A: Loss of peptidase activity with no
detectable changes in secondary
structure. {ECO:0000269|PubMed:12730160,
ECO:0000269|PubMed:7557477}.
MUTAGEN 254 254 I->N: It does not affect the proteolytic
activity. {ECO:0000269|PubMed:20515644}.
MUTAGEN 255 255 L->N: Loss of proteolytic activity.
{ECO:0000269|PubMed:20515644}.
MUTAGEN 258 258 D->V: Increases the proteolytic activity.
{ECO:0000269|PubMed:20515644}.
MUTAGEN 261 261 N->I: Loss of proteolytic activity.
{ECO:0000269|PubMed:20515644}.
MUTAGEN 262 262 I->N: Stimulates the proteolytic activity
at low temperatures (20-30 degrees
Celsius), whereas at higher temperatures
(above 35 degrees Celsius), the
proteolytic activity is less efficient.
{ECO:0000269|PubMed:20515644}.
MUTAGEN 264 264 I->N: Loss of proteolytic activity.
{ECO:0000269|PubMed:20515644}.
CONFLICT 10 10 A -> R (in Ref. 1; AAA23994 and 7;
AAA23680). {ECO:0000305}.
CONFLICT 46 46 E -> Q (in Ref. 6; AAA23717).
{ECO:0000305}.
CONFLICT 192 192 A -> G (in Ref. 1; AAA23994/CAA30997).
{ECO:0000305}.
CONFLICT 467 474 STIYLLMQ -> RHLPVNAVISLNPFLKTGRGSPYNL (in
Ref. 1; AAA23994/CAA30997).
{ECO:0000305}.
HELIX 42 48 {ECO:0000244|PDB:1KY9}.
HELIX 49 51 {ECO:0000244|PDB:1KY9}.
STRAND 52 63 {ECO:0000244|PDB:1KY9}.
STRAND 106 120 {ECO:0000244|PDB:1KY9}.
TURN 121 124 {ECO:0000244|PDB:1KY9}.
STRAND 125 129 {ECO:0000244|PDB:1KY9}.
HELIX 130 133 {ECO:0000244|PDB:1KY9}.
STRAND 136 143 {ECO:0000244|PDB:1KY9}.
STRAND 148 157 {ECO:0000244|PDB:1KY9}.
TURN 158 161 {ECO:0000244|PDB:1KY9}.
STRAND 162 169 {ECO:0000244|PDB:1KY9}.
HELIX 181 183 {ECO:0000244|PDB:1KY9}.
STRAND 189 194 {ECO:0000244|PDB:1KY9}.
STRAND 198 200 {ECO:0000244|PDB:1KY9}.
STRAND 202 213 {ECO:0000244|PDB:1KY9}.
TURN 216 219 {ECO:0000244|PDB:3MH7}.
STRAND 225 228 {ECO:0000244|PDB:1KY9}.
STRAND 238 241 {ECO:0000244|PDB:1KY9}.
STRAND 247 252 {ECO:0000244|PDB:1KY9}.
HELIX 257 259 {ECO:0000244|PDB:3MH7}.
STRAND 262 269 {ECO:0000244|PDB:1KY9}.
HELIX 270 283 {ECO:0000244|PDB:1KY9}.
STRAND 293 297 {ECO:0000244|PDB:3MH7}.
HELIX 301 304 {ECO:0000244|PDB:1KY9}.
STRAND 313 315 {ECO:0000244|PDB:1KY9}.
STRAND 323 325 {ECO:0000244|PDB:1KY9}.
TURN 326 329 {ECO:0000244|PDB:1KY9}.
STRAND 338 343 {ECO:0000244|PDB:1KY9}.
HELIX 348 353 {ECO:0000244|PDB:1KY9}.
STRAND 356 358 {ECO:0000244|PDB:1KY9}.
STRAND 364 371 {ECO:0000244|PDB:1KY9}.
STRAND 373 375 {ECO:0000244|PDB:1KY9}.
STRAND 382 384 {ECO:0000244|PDB:1KY9}.
STRAND 388 393 {ECO:0000244|PDB:1KY9}.
STRAND 401 403 {ECO:0000244|PDB:3MH7}.
TURN 406 408 {ECO:0000244|PDB:1KY9}.
STRAND 411 415 {ECO:0000244|PDB:3MH7}.
STRAND 418 420 {ECO:0000244|PDB:3OU0}.
HELIX 423 425 {ECO:0000244|PDB:1KY9}.
STRAND 432 436 {ECO:0000244|PDB:1KY9}.
HELIX 444 450 {ECO:0000244|PDB:1KY9}.
TURN 451 453 {ECO:0000244|PDB:1KY9}.
STRAND 460 466 {ECO:0000244|PDB:1KY9}.
STRAND 468 471 {ECO:0000244|PDB:1KY9}.
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


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