ID   DEGPL_PSEPG             Reviewed;         477 AA.
AC   B0KV30;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=PputGB1_4377;
OS   Pseudomonas putida (strain GB-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=76869;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-1;
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., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT   "Complete sequence of Pseudomonas putida GB-1.";
RL   Submitted (JAN-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}.
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DR   EMBL; CP000926; ABZ00266.1; -; Genomic_DNA.
DR   RefSeq; WP_012273930.1; NC_010322.1.
DR   AlphaFoldDB; B0KV30; -.
DR   SMR; B0KV30; -.
DR   STRING; 76869.PputGB1_4377; -.
DR   MEROPS; S01.453; -.
DR   PRIDE; B0KV30; -.
DR   EnsemblBacteria; ABZ00266; ABZ00266; PputGB1_4377.
DR   KEGG; ppg:PputGB1_4377; -.
DR   eggNOG; COG0265; Bacteria.
DR   HOGENOM; CLU_020120_1_0_6; -.
DR   OMA; NRSVSMR; -.
DR   Proteomes; UP000002157; Chromosome.
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..477
FT                   /note="Probable periplasmic serine endoprotease DegP-like"
FT                   /id="PRO_5000305886"
FT   DOMAIN          264..355
FT                   /note="PDZ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          361..466
FT                   /note="PDZ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
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   477 AA;  50931 MW;  900BFB915E3CD870 CRC64;
     MSIPRLKSYL TMFAAVLMLG QVLTAQAEEA LPDFTSLVEQ ASPAVVNIST KQKLPDRRIA
     AGQMPDLEGL PPMFREFFER NMPQQPRSPR GDRQREAQSL GSGFIISSDG YVLTNNHVVA
     DADEIIVRLS DRSELQAKLV GTDPRTDVAL LKVEGKNLPI VKLGDSEKLK VGEWVLAIGS
     PFGFDHSVTK GIVSAKGRTL PNDTYVPFIQ TDVAINPGNS GGPLFNMKGE VVGINSQIFT
     RSGGFMGLSF AIPIDVAIDV SNQLKKDGKV SRGWLGVVIQ EVNKDLAESF GLDKPAGALV
     AQVLENGPAA KGGLQVGDVI LSMNGQPIVM SADLPHLVGG LKDGEKAKLE IIRNGKRQNL
     DISVGALPDD DADIGTGAEG SAERSSNRLG VSVADLTAEQ KKSLELKGGV VIKEVQDGPA
     AMIGLRPGDV ISHLNNQAIG SAKEFTEIAK ELPKNRSVSM RVLRQGRASF ITFKLAE