ID A0A068QWQ0_9GAMM Unreviewed; 352 AA.
AC A0A068QWQ0;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Protease degS {ECO:0000313|EMBL:CDG19204.1};
DE EC=3.4.21.- {ECO:0000313|EMBL:CDG19204.1};
GN Name=degS {ECO:0000313|EMBL:CDG19204.1};
GN ORFNames=XDD1_3514 {ECO:0000313|EMBL:CDG19204.1};
OS Xenorhabdus doucetiae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=351671 {ECO:0000313|EMBL:CDG19204.1, ECO:0000313|Proteomes:UP000032721};
RN [1] {ECO:0000313|EMBL:CDG19204.1, ECO:0000313|Proteomes:UP000032721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FRM16 / DSM 17909 {ECO:0000313|Proteomes:UP000032721};
RA Genoscope - CEA;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR EMBL; FO704550; CDG19204.1; -; Genomic_DNA.
DR RefSeq; WP_045972792.1; NZ_VNHN01000018.1.
DR AlphaFoldDB; A0A068QWQ0; -.
DR STRING; 351671.XDD1_3514; -.
DR KEGG; xdo:XDD1_3514; -.
DR HOGENOM; CLU_020120_2_2_6; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000032721; Chromosome.
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; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011783; Pept_S1C_DegS.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001940; Peptidase_S1C.
DR NCBIfam; TIGR02038; protease_degS; 1.
DR PANTHER; PTHR22939:SF101; PERIPLASMIC PH-DEPENDENT SERINE ENDOPROTEASE DEGQ; 1.
DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 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 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CDG19204.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:CDG19204.1}.
FT DOMAIN 246..324
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 95
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611783-1"
FT ACT_SITE 125
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611783-1"
FT ACT_SITE 199
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611783-1"
FT BINDING 182
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR611783-2"
FT BINDING 257..262
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR611783-2"
SQ SEQUENCE 352 AA; 37391 MW; 1B88B984306B0A77 CRC64;
MLIKLLRAIL IGLLIAAILL VAIPSLRPNG LKDFLSGNNS DKISSFSKAV RRAAPAVVNI
YSSSMGSFSH ESRELLPLGS GVIMSEQGYI LTNRHVINKA GSIIVALQDG RFYEALLVGS
DGPTDLAVLK INATNLPLIP INPKRMAHVG DIVLAIGNPY NLGQTITQGI ISATGRVGLS
PTRRQNFLQT DASINQGNSG GALVNTLGEL VGINTLTFDK SEFGSTPEGL GFAIPTKLAT
TIMQKLIRDG RVIRGYIGIT ARELPYIRSS GSHINQIQGL RVFQVAPNGP AEKAGIKVGD
IITSVNHQPA ISPVETMDRV AEIRPGSVVP VTVLRDGASL TLNVTIDEFD GY
//
