ID   DEGPL_PSEMY             Reviewed;         474 AA.
AC   A4XSC0;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Probable periplasmic serine endoprotease DegP-like;
DE            EC=3.4.21.107;
DE   AltName: Full=Protease Do;
DE   Flags: Precursor;
GN   OrderedLocusNames=Pmen_1471;
OS   Pseudomonas mendocina (strain ymp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=399739;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ymp;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Hersman L., Dubois J., Maurice P., Richardson P.;
RT   "Complete sequence of Pseudomonas mendocina ymp.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Might be efficient in the degradation of transiently
CC       denatured and unfolded proteins which accumulate in the periplasm
CC       following stress conditions. {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   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
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DR   EMBL; CP000680; ABP84236.1; -; Genomic_DNA.
DR   RefSeq; WP_003245464.1; NC_009439.1.
DR   AlphaFoldDB; A4XSC0; -.
DR   SMR; A4XSC0; -.
DR   STRING; 399739.Pmen_1471; -.
DR   EnsemblBacteria; ABP84236; ABP84236; Pmen_1471.
DR   KEGG; pmy:Pmen_1471; -.
DR   PATRIC; fig|399739.8.peg.1493; -.
DR   eggNOG; COG0265; Bacteria.
DR   HOGENOM; CLU_020120_1_0_6; -.
DR   OMA; NRSVSMR; -.
DR   OrthoDB; 741829at2; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; PF13180; PDZ_2; 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   Hydrolase; Periplasm; Protease; Repeat; Serine protease; Signal;
KW   Stress response.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..474
FT                   /note="Probable periplasmic serine endoprotease DegP-like"
FT                   /id="PRO_5000240365"
FT   DOMAIN          260..351
FT                   /note="PDZ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          357..463
FT                   /note="PDZ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   ACT_SITE        113
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        143
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        216
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   BINDING         214..216
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         271..275
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   474 AA;  50212 MW;  E7200F6FA0264E6C CRC64;
     MRNLKSVTPL LMAALLWGQS LLAQASLPDF TALVEEASPA VVNISTRQKM PERSVAAQPG
     LPDLEGLPPM FREFFERSIP QMPRNPGGRQ REAQSLGSGF IISADGYVLT NNHVVADADE
     IIVRLSDRSE LEAKLIGADP RSDVALLKVE GKGLPTVRLG KSDELKVGEW VLAIGSPFGF
     DHSVTAGIVS AKGRNLPSDS YVPFIQTDVA INPGNSGGPL FNLKGEVVGI NSQIFTRSGG
     FMGLSFAIPM EVALQVSEQL KADGKVTRGW LGVVIQEVNK DLAESFGLDR PAGALVAQVL
     EDGPADKGGL QVGDVILSLN GKPIVMSADL PHLVGGLKPG EKAEMDVVRD GSRKKLKVTI
     GTLPEEGQEL AAAGSTKGGE RSSNRLGVTV VELTAEQKKG LDLRGGVVVK EVLSGPAAMI
     GLRPGDVITH LNNQAIDSTA TFAKVAQELP KNRSVSMRVL RQGRASFITF KLAE