ID   DEGPL_MARMS             Reviewed;         469 AA.
AC   A6VUA4;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=Mmwyl1_1102;
OS   Marinomonas sp. (strain MWYL1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=400668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MWYL1;
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., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y.,
RA   Richardson P.;
RT   "Complete sequence of Marinomonas sp. MWYL1.";
RL   Submitted (JUN-2007) 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; CP000749; ABR70033.1; -; Genomic_DNA.
DR   RefSeq; WP_012068819.1; NC_009654.1.
DR   AlphaFoldDB; A6VUA4; -.
DR   SMR; A6VUA4; -.
DR   STRING; 400668.Mmwyl1_1102; -.
DR   EnsemblBacteria; ABR70033; ABR70033; Mmwyl1_1102.
DR   KEGG; mmw:Mmwyl1_1102; -.
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; -; 1.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR041489; PDZ_6.
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; 1.
DR   Pfam; PF17820; PDZ_6; 1.
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..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..469
FT                   /note="Probable periplasmic serine endoprotease DegP-like"
FT                   /id="PRO_5000259260"
FT   DOMAIN          261..352
FT                   /note="PDZ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          358..458
FT                   /note="PDZ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   ACT_SITE        114
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        144
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        217
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   BINDING         215..217
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         272..276
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   469 AA;  50582 MW;  A6ED35AC20429A3C CRC64;
     MNRLLKQVCM VVVSSFMMAS MLTHAASLPD FTELVEKASP AVVNISTEQT VTTKTANEGG
     QQLGPNSEEL NEFFKHFFGQ QPFGQQAPPQ QGQRSSLGSG FIISHDGYVL TNNHVIDGAD
     VIHVRLNDRR EYVAKLVGTD PRTDLALLKI EADDLPIVKM GDSDKLKPGQ WVLAIGSPFG
     FDYTVTAGIV SATGRSLPSD NYVPFIQTDV AINPGNSGGP LFNLDGEVVG INSQIYTRSG
     GFMGVSFAIP SKVAMSVVDQ LKSDGKVSRA WLGVLIQDVN NELAESFGLD RSNGALISRV
     LPDSPAEKAG LKSGDIILEF NGQSIAHSGE LPYIVGQMKA DEKVDAKVYR DGKEQTISVT
     LEARPNDPKV VAQSQQDQNR LGMIVGEVPA DMAKKFEIDN GVVIEQVLGG TAARNGLQQG
     DVITMLNGKR ITSVAEFAKI AKDIPSGRSV PMRVIRQGYP MFIPFKIMD