ID   DEGPL_PSE14             Reviewed;         479 AA.
AC   Q48EU9;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=PSPPH_3952;
OS   Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
OS   (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=264730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1448A / Race 6;
RX   PubMed=16159782; DOI=10.1128/jb.187.18.6488-6498.2005;
RA   Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA   Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn Giglio M.,
RA   Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Crabtree J.,
RA   Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L., Halpin R.,
RA   Holley T., Khouri H.M., Feldblyum T.V., White O., Fraser C.M.,
RA   Chatterjee A.K., Cartinhour S., Schneider D., Mansfield J.W., Collmer A.,
RA   Buell R.;
RT   "Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola
RT   1448A reveals divergence among pathovars in genes involved in virulence and
RT   transposition.";
RL   J. Bacteriol. 187:6488-6498(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; CP000058; AAZ33488.1; -; Genomic_DNA.
DR   RefSeq; WP_011169354.1; NC_005773.3.
DR   AlphaFoldDB; Q48EU9; -.
DR   SMR; Q48EU9; -.
DR   STRING; 264730.PSPPH_3952; -.
DR   MEROPS; S01.453; -.
DR   EnsemblBacteria; AAZ33488; AAZ33488; PSPPH_3952.
DR   KEGG; psp:PSPPH_3952; -.
DR   eggNOG; COG0265; Bacteria.
DR   HOGENOM; CLU_020120_1_0_6; -.
DR   OMA; NRSVSMR; -.
DR   OrthoDB; 741829at2; -.
DR   Proteomes; UP000000551; 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..479
FT                   /note="Probable periplasmic serine endoprotease DegP-like"
FT                   /id="PRO_0000414224"
FT   DOMAIN          266..357
FT                   /note="PDZ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          363..468
FT                   /note="PDZ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   REGION          77..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        119
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        149
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        222
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   BINDING         220..222
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         277..281
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   479 AA;  50546 MW;  1AA3163E0AD41D73 CRC64;
     MSIPRMKSYF SLIAAVLMLG QVATAQAENL PDFTGLVEQA SPAVVNISTR QKLPDRAIAN
     QQMPDLEGLP PMLREFLERS MPPGSRPPGA GKGDRQRETQ SLGSGFIISP DGYILTNNHV
     IDGADEILVR LSDRSELKAK LIGTDSRTDV AVLKIDGKDL PTAKLGNSNT LKVGEWVLAI
     GSPFGFDHSV TKGIVSAKGR SLPNDTYVPF IQTDVAINPG NSGGPLFNMA GEVVGINSQI
     FTRSGGFMGL SFAIPIDVAM DVANQLKASG KVSRGWLGVV IQEVNKDLAE SFGLDKPAGA
     LVAQVLEDGP AAKGGLQVGD VILSANGQPI IMSADLPHLI GNLKDGSKAE LEVIRDGKRQ
     KLTVTVGALP DEGQEMGDVA GTGAERSSNR LGVSVIELTA EQKKSLDLKG GVAIKEVTGG
     PASLIGLQPG DVITHLNNQA ITSSKQFTEV AKSLPKDRSV SMRVLRQGRA TFITFKLSE