ID A0AAN0QZV8_9PSED Unreviewed; 477 AA. AC A0AAN0QZV8; DT 02-OCT-2024, integrated into UniProtKB/TrEMBL. DT 02-OCT-2024, sequence version 1. DT 27-NOV-2024, entry version 2. DE RecName: Full=Probable periplasmic serine endoprotease DegP-like {ECO:0000256|ARBA:ARBA00013958}; DE EC=3.4.21.107 {ECO:0000256|ARBA:ARBA00013035}; DE AltName: Full=Protease Do {ECO:0000256|ARBA:ARBA00032850}; GN ORFNames=PVLB_05170 {ECO:0000313|EMBL:AGZ33841.1}; OS Pseudomonas sp. VLB120. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=69328 {ECO:0000313|EMBL:AGZ33841.1, ECO:0000313|Proteomes:UP000017756}; RN [1] {ECO:0000313|EMBL:AGZ33841.1, ECO:0000313|Proteomes:UP000017756} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VLB120 {ECO:0000313|EMBL:AGZ33841.1, RC ECO:0000313|Proteomes:UP000017756}; RX PubMed=25128338; DOI=10.1128/AEM.01940-14; RA Volmer J., Neumann C., Buhler B., Schmid A.; RT "Engineering of Pseudomonas taiwanensis VLB120 for Constitutive Solvent RT Tolerance and Increased Specific Styrene Epoxidation Activity."; RL Appl. Environ. Microbiol. 80:6539-6548(2014). 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 -!- 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 Evidence={ECO:0000256|ARBA:ARBA00001772}; CC -!- SIMILARITY: Belongs to the peptidase S1C family. CC {ECO:0000256|ARBA:ARBA00010541}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP003961; AGZ33841.1; -; Genomic_DNA. DR RefSeq; WP_023378969.1; NC_022738.1. DR Proteomes; UP000017756; Chromosome. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR CDD; cd00987; PDZ_serine_protease; 2. DR FunFam; 2.30.42.10:FF:000037; Periplasmic serine endoprotease DegP-like; 1. DR FunFam; 2.40.10.120:FF:000007; Periplasmic serine endoprotease DegP-like; 1. DR Gene3D; 2.30.42.10; -; 2. DR Gene3D; 2.40.10.120; -; 1. 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 NCBIfam; TIGR02037; degP_htrA_DO; 1. DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1. DR PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 1. DR Pfam; PF00595; PDZ; 1. DR Pfam; PF13180; PDZ_2; 1. DR Pfam; PF13365; Trypsin_2; 1. DR PRINTS; PR00834; PROTEASES2C. DR SMART; SM00228; PDZ; 2. DR SUPFAM; SSF50156; PDZ domain-like; 2. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1. DR PROSITE; PS50106; PDZ; 2. PE 3: Inferred from homology; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:AGZ33841.1}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Serine protease {ECO:0000256|ARBA:ARBA00022825}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}; KW Stress response {ECO:0000256|ARBA:ARBA00023016}. FT SIGNAL 1..27 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 28..477 FT /note="Probable periplasmic serine endoprotease DegP-like" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5042883002" FT DOMAIN 261..343 FT /note="PDZ" FT /evidence="ECO:0000259|PROSITE:PS50106" FT DOMAIN 371..441 FT /note="PDZ" FT /evidence="ECO:0000259|PROSITE:PS50106" SQ SEQUENCE 477 AA; 51020 MW; A8CA1676C927FF69 CRC64; MSIPRLKSYL TMFAAVLMLG QVLTAQAEEA LPDFTTLVEQ ASPAVVNIST KQKLPDRRVA AGQMPDLEGL PPMFREFFER NMPQQPRAPR GDRQREAMSL GSGFIISSDG YVLTNNHVVA DADEIIVRLS DRSELQAKLI GTDPRTDVAL LKVEGKNLPT VKLGDSEKLK VGEWVLAIGS PFGFDHSVTK GIVSAKGRTL PNDTYVPFIQ TDVAINPGNS GGPLFNMKGE VVGINSQIFT RSGGFMGLSF AIPIDVALDV SNQLKKDGKV SRGWLGVVIQ EVNKDLAESF GLDKPAGALV AQVLEGGPAA KGGLQVGDVI LSMNGQPIVM SADLPHLVGG LKDGEKAKLE IIRNGKRQNL DITIGAMPDD DADIEASAQG GAERSSNRLG VSVADLTDEQ KKTLELKGGV VIKEIQDGPA ALIGLRPGDV ISHLNNQAIS SAKQFTEIAK DLPKNRSVSM RVLRQGRASF ITFKLAE //