ID   DEGPL_HAHCH             Reviewed;         469 AA.
AC   Q2SL36;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=HCH_01795;
OS   Hahella chejuensis (strain KCTC 2396).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Hahellaceae; Hahella.
OX   NCBI_TaxID=349521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 2396;
RX   PubMed=16352867; DOI=10.1093/nar/gki1016;
RA   Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA   Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA   Oh T.K., Kim J.F.;
RT   "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT   algicidal agent.";
RL   Nucleic Acids Res. 33:7066-7073(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; CP000155; ABC28638.1; -; Genomic_DNA.
DR   RefSeq; WP_011395710.1; NC_007645.1.
DR   AlphaFoldDB; Q2SL36; -.
DR   SMR; Q2SL36; -.
DR   STRING; 349521.HCH_01795; -.
DR   PRIDE; Q2SL36; -.
DR   EnsemblBacteria; ABC28638; ABC28638; HCH_01795.
DR   KEGG; hch:HCH_01795; -.
DR   eggNOG; COG0265; Bacteria.
DR   HOGENOM; CLU_020120_1_0_6; -.
DR   OMA; NRSVSMR; -.
DR   OrthoDB; 741829at2; -.
DR   Proteomes; UP000000238; 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; 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; Reference proteome; Repeat;
KW   Serine protease; Signal; 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_0000414221"
FT   DOMAIN          255..346
FT                   /note="PDZ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          352..457
FT                   /note="PDZ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   ACT_SITE        108
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        138
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        211
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   BINDING         209..211
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         266..270
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   469 AA;  50156 MW;  F3422F4C37073255 CRC64;
     MKVCQKYTAV LLVWLSAVVS MRAGAVDLPD FTGLVERTSP AVVNISTVRK VGDDSAQYYF
     GGPEQDQIPE FFRHFFGDPY RRRGPQEAQS TGSGFIVSKD GYILTNNHVV AGADEIFVRL
     MDRRELTAKL IGSDEKSDLA VLKVEADDLP VLNLGKSSEL KVGEWVVAIG SPFGFEYTVT
     AGIVSAKGRS LPNENYVPFI QTDVAINPGN SGGPLFNLEG EVVGINSQIY TRSGGFMGVS
     FAIPIDVALD VMNQLKDTGA VKRGWLGVLI QEVNKDLAES FNLNKPRGAL VAQVMKGSPA
     DKAGLQPGDV IVSYNGNEIG LSSELPHLVG RTSPGQKASM KVVRRGDEMD VAVEIGQLPA
     DDNGVASVPA GQTAPQNNAL NLQVRDLTDE EKESMQVAGG VMVAQVFPGP AATAGIQPND
     VISSINNKDV ETVAQFHEVV EKLPVGKSLP VLIIRQGNPA FIVLKLNNK