ID   DEGPL_PSEPW             Reviewed;         479 AA.
AC   B1J4D7;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=PputW619_1070;
OS   Pseudomonas putida (strain W619).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=390235;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W619;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA   Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Taghavi S., Vangronsveld D., van der Lelie D.,
RA   Richardson P.;
RT   "Complete sequence of Pseudomonas putida W619.";
RL   Submitted (FEB-2008) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000949; ACA71575.1; -; Genomic_DNA.
DR   RefSeq; WP_012312989.1; NC_010501.1.
DR   AlphaFoldDB; B1J4D7; -.
DR   SMR; B1J4D7; -.
DR   STRING; 390235.PputW619_1070; -.
DR   MEROPS; S01.453; -.
DR   EnsemblBacteria; ACA71575; ACA71575; PputW619_1070.
DR   KEGG; ppw:PputW619_1070; -.
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..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..479
FT                   /note="Probable periplasmic serine endoprotease DegP-like"
FT                   /id="PRO_5000314745"
FT   DOMAIN          264..355
FT                   /note="PDZ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          361..468
FT                   /note="PDZ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   REGION          368..395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        381..395
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        117
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        147
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        220
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   BINDING         218..220
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         275..279
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   479 AA;  51041 MW;  54FB7C80F244C79A CRC64;
     MSIPRLKSYL SMFAAVLMLG QVLSAQAEEA LPDFTTLVEQ ASPAVVNIST KQKLPDRRIA
     AGQMPDLEGL PPMFREFFER NMPQQPRSPR GDRQREAQSL GSGFIISSDG YVLTNNHVVA
     DADEIIVRLS DRSELQAKLV GTDPRTDVAL LKVDGKNLPT VKLGDSEKLK VGEWVLAIGS
     PFGFDHSVTK GIVSAKGRTL PNDTYVPFIQ TDVAINPGNS GGPLFNMNGE VVGINSQIFT
     RSGGFMGLSF AIPIDVAIDV SNQLKKDGKV SRGWLGVVIQ EVNKDLAESF GLDKPAGALV
     AQVLEDGPAA KSGLQVGDVI LSMNGQPIVM SADLPHLVGT LKAGAKAKLE IIRNGKRQNL
     DVTIGAMPDD DADIGTGTGA DGSAERSSNR LGVSVSDLTA EQKKSLELKG GVVIKEVQDG
     PAAMIGLRPG DVISHLNNQA IASAKQFTEI AKDLPKNRSV SMRVLRQGRA SFITFKLAE