DEGP_SALTY
ID DEGP_SALTY Reviewed; 475 AA.
AC P26982;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 148.
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=STM0209;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C5;
RX PubMed=1645840; DOI=10.1111/j.1365-2958.1991.tb02122.x;
RA Johnson K., Charles I., Dougan G., Pickard D., O'Gaora P., Costa G.,
RA Ali T., Miller I., Hormaeche C.;
RT "The role of a stress-response protein in Salmonella typhimurium
RT virulence.";
RL Mol. Microbiol. 5:401-407(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(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; X54548; CAA38420.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL19173.1; -; Genomic_DNA.
DR PIR; S15337; S15337.
DR RefSeq; NP_459214.1; NC_003197.2.
DR RefSeq; WP_000753958.1; NC_003197.2.
DR AlphaFoldDB; P26982; -.
DR SMR; P26982; -.
DR STRING; 99287.STM0209; -.
DR MEROPS; S01.273; -.
DR PaxDb; P26982; -.
DR EnsemblBacteria; AAL19173; AAL19173; STM0209.
DR GeneID; 1251727; -.
DR KEGG; stm:STM0209; -.
DR PATRIC; fig|99287.12.peg.222; -.
DR HOGENOM; CLU_020120_1_1_6; -.
DR OMA; NRSVSMR; -.
DR PhylomeDB; P26982; -.
DR BioCyc; SENT99287:STM0209-MON; -.
DR BRENDA; 3.4.21.107; 5542.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; ISS:UniProtKB.
DR GO; GO:0042597; C:periplasmic space; IBA:GO_Central.
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; 2.
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..475
FT /note="Periplasmic serine endoprotease DegP"
FT /id="PRO_0000026922"
FT DOMAIN 281..372
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 378..467
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT ACT_SITE 132
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P0C0V0"
FT ACT_SITE 162
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P0C0V0"
FT ACT_SITE 237
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P0C0V0"
FT BINDING 59
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 235..237
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 253..257
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 292..296
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT DISULFID 84..96
FT /evidence="ECO:0000250"
SQ SEQUENCE 475 AA; 49315 MW; 86E685BF3C1A289F CRC64;
MKKTTLAMSA LALSLGLALS PLSATAAETS SSAMTAQQMP SLAPMLEKVM PSVVSINVEG
STTVNTPRMP RNFQQFFGDD SPFCQDGSPF QNSPFCQGGG NGGNGGQQQK FMALGSGVII
DAAKGYVVTN NHVVDNASVI KVQLSDGRKF DAKVVGKDPR SDIALIQIQN PKNLTAIKLA
DSDALRVGDY TVAIGNPFGL GETVTSGIVS ALGRSGLNVE NYENFIQTDA AINRGNSGGA
LVNLNGELIG INTAILAPDG GNIGIGFAIP SNMVKNLTSQ MVEYGQVKRG ELGIMGTELN
SELAKAMKVD AQRGAFVSQV MPNSSAAKAG IKAGDVITSL NGKPISSFAA LRAQVGTMPV
GSKISLGLLR EGKAITVNLE LQQSSQSQVD SSTIFSGIEG AEMSNKGQDK GVVVSSVKAN
SPAAQIGLKK GDVIIGANQQ PVKNIAELRK ILDSKPSVLA LNIQRGDSSI YLLMQ
