ID   A0A0A1HSL0_9PSED        Unreviewed;       386 AA.
AC   A0A0A1HSL0;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Probable periplasmic serine endoprotease DegP-like {ECO:0000256|ARBA:ARBA00013958};
DE   AltName: Full=Protease Do {ECO:0000256|ARBA:ARBA00032850};
GN   ORFNames=BN844_3692 {ECO:0000313|EMBL:CDF93037.1};
OS   Pseudomonas sp. SHC52.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=984195 {ECO:0000313|EMBL:CDF93037.1, ECO:0000313|Proteomes:UP000031550};
RN   [1] {ECO:0000313|EMBL:CDF93037.1, ECO:0000313|Proteomes:UP000031550}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SHC52 {ECO:0000313|EMBL:CDF93037.1,
RC   ECO:0000313|Proteomes:UP000031550};
RA   Van der Voort M., Mendes R., Raaijmakers J.M.;
RT   "Genome mining of the rhizosphere bacterium Pseudomonas sp. SH-C52.";
RL   Submitted (MAY-2013) 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:0000256|ARBA:ARBA00002610}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDF93037.1}.
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DR   EMBL; CBLV010000072; CDF93037.1; -; Genomic_DNA.
DR   RefSeq; WP_041020854.1; NZ_CBLV010000072.1.
DR   AlphaFoldDB; A0A0A1HSL0; -.
DR   OrthoDB; 9758917at2; -.
DR   Proteomes; UP000031550; Unassembled WGS sequence.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00987; PDZ_serine_protease; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 2.40.10.120; -; 1.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   PANTHER; PTHR43343; PEPTIDASE S12; 1.
DR   PANTHER; PTHR43343:SF3; PROTEASE DO-LIKE 8, CHLOROPLASTIC; 1.
DR   Pfam; PF13180; PDZ_2; 1.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:CDF93037.1};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Protease {ECO:0000313|EMBL:CDF93037.1};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016}.
FT   DOMAIN          271..334
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
SQ   SEQUENCE   386 AA;  40918 MW;  C7B02C96FBD908E2 CRC64;
     MLKALRFSGW PLLAGVLVAL LIIQRYPEWV GLPSLDVNLQ QAPQSKALLQ GPVSYADAVT
     IAAPAVVNLY TTKVINKPSH PLFEDPQFRR FFGDNSPKQK RMESSLGSGV IMSPEGYLLT
     NNHVTSGADQ IVVALKDGRE TLARVIGSDP ETDLAVLKID LKNLPAITIG RSDSIRIGDV
     ALAIGNPFGV GQTVTMGIIS ATGRNQLGLN NYEDFIQTDA AINPGNSGGA LVDANGNLTG
     INTAIFSKSG GSQGIGFAIP VKLAMEVMKS IIEHGQVIRG WLGIEVQPLT QELAESFGLS
     GRPGIVVAGI FRDGPAQKAG LQLGDVILSI DGEPAGDGRR SMNQVARIKP TDKVTIQVMR
     NGKELKLTAE IGLRPPPAPI AVKEEQ
//