ID   DEGPL_PSEF1             Reviewed;         479 AA.
AC   F6AA62;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   03-AUG-2022, entry version 48.
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=Psefu_3239;
OS   Pseudomonas fulva (strain 12-X).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=743720;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12-X;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Pagani I., Davenport K., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Lcollab F.I.,
RA   Woyke T.;
RT   "Complete sequence of Pseudomonas fulva 12-X.";
RL   Submitted (APR-2011) 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; CP002727; AEF23201.1; -; Genomic_DNA.
DR   AlphaFoldDB; F6AA62; -.
DR   SMR; F6AA62; -.
DR   STRING; 743720.Psefu_3239; -.
DR   EnsemblBacteria; AEF23201; AEF23201; Psefu_3239.
DR   KEGG; pfv:Psefu_3239; -.
DR   eggNOG; COG0265; Bacteria.
DR   HOGENOM; CLU_020120_1_0_6; -.
DR   OMA; NRSVSMR; -.
DR   Proteomes; UP000000686; 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; Reference proteome; Repeat;
KW   Serine protease; Signal; 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_5000747883"
FT   DOMAIN          265..356
FT                   /note="PDZ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          362..468
FT                   /note="PDZ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   REGION          368..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        118
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        148
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        221
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   BINDING         219..221
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         276..280
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   479 AA;  50338 MW;  A0B245631D88A4E8 CRC64;
     MSMPSLKKYA AALFAVFLMG QSVAAHAQLP DFTPLVEAAS PAVVNISTRQ KVPNAVASNG
     GLSVPDLEGL PPMFREFFER SIPQQPRAPG GGGRQREAQS LGSGFIISKD GYILTNNHVV
     ADADEIIVRL SDRSELEAKL IGTDPRSDVA LLKVEANDLP TVKLGNSDNL KVGEWVLAIG
     SPFGFDHSVT AGIVSAKGRS LPNESYVPFI QTDVAINPGN SGGPLFNLDG EVVGINSQIF
     TRSGGFMGLS FAIPMSVAMD VADQLKASGK VSRGWLGVVI QEVNKDLAES FGLEKPAGAL
     VAQVLEDGPA AKGGLQVGDV ILSLDGKPII MSADLPHLVG ALKPGTKANL EIVREGSRKT
     LKVAVGTMPA DDGDEATNDA APSAERSSNR LGVSVAELTD EQKKALDLRG GVVIREVQDG
     PAALIGLRPG DVITHLNNQA ITSAKNFTEV AQSLPKNRSV SMRVLRQGRA SFITFKLAE