DEGP_ECO57
ID DEGP_ECO57 Reviewed; 474 AA.
AC P0C0V1; P09376; P15724;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Periplasmic serine endoprotease DegP;
DE EC=3.4.21.107;
DE AltName: Full=Heat shock protein DegP;
DE AltName: Full=Protease Do;
DE Flags: Precursor;
GN Name=degP; Synonyms=htrA, ptd; OrderedLocusNames=Z0173, ECs0165;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: DegP acts as a chaperone at low temperatures but switches to
CC a peptidase (heat shock protein) at higher temperatures. It degrades
CC transiently denatured and unfolded proteins which accumulate in the
CC periplasm following heat shock or other stress conditions. DegP is
CC efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a
CC preference for beta-branched side chain amino acids. Only unfolded
CC proteins devoid of disulfide bonds appear capable of being cleaved,
CC thereby preventing non-specific proteolysis of folded proteins. Its
CC proteolytic activity is essential for the survival of cells at elevated
CC temperatures. It can degrade IciA, ada, casein, globin and PapA. DegP
CC shares specificity with DegQ. DegP is also involved in the biogenesis
CC of partially folded outer-membrane proteins (OMP) (By similarity).
CC {ECO:0000250}.
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 -!- 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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
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DR EMBL; AE005174; AAG54465.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB33588.1; -; Genomic_DNA.
DR PIR; S45229; S45229.
DR RefSeq; NP_308192.1; NC_002695.1.
DR RefSeq; WP_000753946.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0C0V1; -.
DR SMR; P0C0V1; -.
DR IntAct; P0C0V1; 2.
DR STRING; 155864.EDL933_0166; -.
DR MEROPS; S01.273; -.
DR EnsemblBacteria; AAG54465; AAG54465; Z0173.
DR EnsemblBacteria; BAB33588; BAB33588; ECs_0165.
DR GeneID; 67416238; -.
DR GeneID; 913821; -.
DR KEGG; ece:Z0173; -.
DR KEGG; ecs:ECs_0165; -.
DR PATRIC; fig|386585.9.peg.265; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_1_1_6; -.
DR OMA; NRSVSMR; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0006457; P:protein folding; ISS:UniProtKB.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB.
DR GO; GO:0009266; P:response to temperature stimulus; ISS:UniProtKB.
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 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Disulfide bond; Hydrolase; Membrane;
KW Protease; Reference proteome; Repeat; Serine protease; Signal;
KW Stress response.
FT SIGNAL 1..26
FT /evidence="ECO:0000250"
FT CHAIN 27..474
FT /note="Periplasmic serine endoprotease DegP"
FT /id="PRO_0000045160"
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:0000250|UniProtKB:P0C0V0"
FT ACT_SITE 161
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P0C0V0"
FT ACT_SITE 236
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P0C0V0"
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 234..236
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 252..256
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 291..295
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT DISULFID 83..95
FT /evidence="ECO:0000250"
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
