(data stored in ACNUC7421 zone)

SWISSPROT: 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   05-JUL-2017, entry version 82.
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.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., 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.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and 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
CC       switches to a peptidase (heat shock protein) at higher
CC       temperatures. It degrades transiently denatured and unfolded
CC       proteins which accumulate in the periplasm following heat shock or
CC       other stress conditions. DegP is efficient with Val-Xaa and Ile-
CC       Xaa peptide bonds, suggesting a preference for beta-branched side
CC       chain amino acids. Only unfolded proteins devoid of disulfide
CC       bonds appear capable of being cleaved, thereby preventing non-
CC       specific proteolysis of folded proteins. Its proteolytic activity
CC       is essential for the survival of cells at elevated temperatures.
CC       It can degrade IciA, ada, casein, globin and PapA. DegP shares
CC       specificity with DegQ. DegP is also involved in the biogenesis of
CC       partially folded outer-membrane proteins (OMP) (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: Acts on substrates that are at least partially
CC       unfolded. The cleavage site P1 residue is normally between a pair
CC       of hydrophobic residues, such as Val-|-Val.
CC   -!- SUBUNIT: DegP can reversibly switch between different oligomeric
CC       forms that represent inactive (6-mer) and active (12-and 24-mer)
CC       protease states. Substrate binding triggers the conversion of the
CC       resting DegP trimer and hexamer into catalytically active 12- and
CC       24-mers. The conversion of 6-mer (DegP6) into 12-mer (DegP12) or
CC       24-mer (DegP24) is crucial in regulating protease activity (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: DegP is indispensable for bacterial survival at
CC       temperatures above 42 degrees Celsius, however is also able to
CC       digest its natural substrates in a reducing environment at
CC       temperatures as low as 20 degrees Celsius. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
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_MWVM01000012.1.
DR   ProteinModelPortal; P0C0V1; -.
DR   SMR; P0C0V1; -.
DR   IntAct; P0C0V1; 2.
DR   STRING; 155864.Z0173; -.
DR   PRIDE; P0C0V1; -.
DR   EnsemblBacteria; AAG54465; AAG54465; Z0173.
DR   EnsemblBacteria; BAB33588; BAB33588; BAB33588.
DR   GeneID; 913821; -.
DR   KEGG; ece:Z0173; -.
DR   KEGG; ecs:ECs0165; -.
DR   PATRIC; fig|386585.9.peg.265; -.
DR   eggNOG; ENOG4105C0H; Bacteria.
DR   eggNOG; COG0265; LUCA.
DR   HOGENOM; HOG000223642; -.
DR   KO; K04771; -.
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:0006515; P:misfolded or incompletely synthesized protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0006457; P:protein folding; 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   InterPro; IPR001478; PDZ.
DR   InterPro; IPR011782; Pept_S1C_Do.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   Pfam; PF00595; PDZ; 2.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SMART; SM00228; PDZ; 2.
DR   SUPFAM; SSF50156; SSF50156; 2.
DR   SUPFAM; SSF50494; SSF50494; 2.
DR   TIGRFAMs; TIGR02037; degP_htrA_DO; 1.
DR   PROSITE; PS50106; PDZ; 2.
PE   3: Inferred from homology;
DR   PRODOM; P0C0V1.
DR   SWISS-2DPAGE; P0C0V1.
KW   Cell inner membrane; Cell membrane; Complete proteome; Disulfide bond;
KW   Hydrolase; Membrane; Protease; Repeat; Serine protease; Signal;
KW   Stress response.
FT   SIGNAL        1     26       {ECO:0000250}.
FT   CHAIN        27    474       Periplasmic serine endoprotease DegP.
FT                                /FTId=PRO_0000045160.
FT   DOMAIN      280    371       PDZ 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00143}.
FT   DOMAIN      377    466       PDZ 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00143}.
FT   REGION      234    236       Substrate binding. {ECO:0000250}.
FT   REGION      252    256       Substrate binding. {ECO:0000250}.
FT   REGION      291    295       Substrate binding. {ECO:0000250}.
FT   ACT_SITE    131    131       Charge relay system.
FT                                {ECO:0000250|UniProtKB:P0C0V0}.
FT   ACT_SITE    161    161       Charge relay system.
FT                                {ECO:0000250|UniProtKB:P0C0V0}.
FT   ACT_SITE    236    236       Charge relay system.
FT                                {ECO:0000250|UniProtKB:P0C0V0}.
FT   BINDING      58     58       Substrate. {ECO:0000250}.
FT   BINDING     131    131       Substrate. {ECO:0000250}.
FT   BINDING     161    161       Substrate. {ECO:0000250}.
FT   DISULFID     83     95       {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
//

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