ID   DEGPL_PSEF5             Reviewed;         476 AA.
AC   Q4KGQ4;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Probable periplasmic serine endoprotease DegP-like;
DE            EC=3.4.21.107;
DE   AltName: Full=Protease Do;
DE   Flags: Precursor;
GN   Name=mucD; OrderedLocusNames=PFL_1451;
OS   Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=220664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5;
RX   PubMed=15980861; DOI=10.1038/nbt1110;
RA   Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA   Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA   Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA   Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA   Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S. III,
RA   Thomashow L.S., Loper J.E.;
RT   "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT   Pf-5.";
RL   Nat. Biotechnol. 23:873-878(2005).
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; CP000076; AAY90735.1; -; Genomic_DNA.
DR   RefSeq; WP_011059790.1; NC_004129.6.
DR   AlphaFoldDB; Q4KGQ4; -.
DR   SMR; Q4KGQ4; -.
DR   STRING; 220664.PFL_1451; -.
DR   MEROPS; S01.453; -.
DR   World-2DPAGE; 0008:Q4KGQ4; -.
DR   PRIDE; Q4KGQ4; -.
DR   EnsemblBacteria; AAY90735; AAY90735; PFL_1451.
DR   GeneID; 57474470; -.
DR   KEGG; pfl:PFL_1451; -.
DR   PATRIC; fig|220664.5.peg.1484; -.
DR   eggNOG; COG0265; Bacteria.
DR   HOGENOM; CLU_020120_1_0_6; -.
DR   OMA; NRSVSMR; -.
DR   OrthoDB; 741829at2; -.
DR   Proteomes; UP000008540; 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..476
FT                   /note="Probable periplasmic serine endoprotease DegP-like"
FT                   /id="PRO_0000414223"
FT   DOMAIN          263..354
FT                   /note="PDZ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          360..465
FT                   /note="PDZ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   ACT_SITE        116
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        146
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        219
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   BINDING         217..219
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         274..278
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   476 AA;  50724 MW;  CB8FD2155A16F54B CRC64;
     MSIPRLKSYF TILATVLVLG QAVSAQAAEL PDFTQLVEQA SPAVVNISTT QKLPDRRVSN
     SAQMPDLEGL PPMLREFFER GMPQPRSPRG DRQREAQSLG SGFIISADGY ILTNNHVIAD
     ADEILVRLAD RSELKAKLIG TDPRSDVALL KIDGKDLPVL KLGKSQDLKA GQWVVAIGSP
     FGFDHTVTQG IVSAIGRSLP NENYVPFIQT DVPINPGNSG GPLFNLAGEV VGINSQIYTR
     SGGFMGVSFA IPIDVAMDVS NQLKTGGKVS RGWLGVVIQE VNKDLAESFG LEKPAGALVA
     QIQDDGPAAK GGLQVGDVIL SLNGQPIVMS ADLPHLVGAL KAGAKANLEV IRDGKRKNVE
     LTVGAIPEED KDLSMLPKSG VERSSNRLGV AVVELNDEQK KAFDLKGGVV IKEVQDGPAA
     LIGLQPGDVI THLNNQAITS AKEFTEIAKA LPKNRSVSMR VLRQGRASFI TFKLAE