ID A0A0Q9EX17_9GAMM Unreviewed; 502 AA.
AC A0A0Q9EX17;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=ASE45_11700 {ECO:0000313|EMBL:KRD67442.1};
OS Lysobacter sp. Root96.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1736612 {ECO:0000313|EMBL:KRD67442.1, ECO:0000313|Proteomes:UP000050805};
RN [1] {ECO:0000313|EMBL:KRD67442.1, ECO:0000313|Proteomes:UP000050805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root96 {ECO:0000313|EMBL:KRD67442.1,
RC ECO:0000313|Proteomes:UP000050805};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRD67442.1, ECO:0000313|Proteomes:UP000050805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root96 {ECO:0000313|EMBL:KRD67442.1,
RC ECO:0000313|Proteomes:UP000050805};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRD67442.1}.
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DR EMBL; LMJN01000003; KRD67442.1; -; Genomic_DNA.
DR RefSeq; WP_055909735.1; NZ_LMJN01000003.1.
DR AlphaFoldDB; A0A0Q9EX17; -.
DR STRING; 1736612.ASE45_11700; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000050805; Unassembled WGS sequence.
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; 2.
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:SF130; PERIPLASMIC SERINE ENDOPROTEASE DEGP-LIKE; 1.
DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR Pfam; PF13180; PDZ_2; 2.
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; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000050805};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..502
FT /note="Probable periplasmic serine endoprotease DegP-like"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039120823"
FT DOMAIN 284..370
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 93..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 130
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 160
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 235
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 502 AA; 51178 MW; 774EF75379FF44D0 CRC64;
MTRPLRSIAL ASALAAVLPV ACTAQTPSTP IAPPPVATPA APLVSGLPDF TALVQRVGPA
VVNVRAEIAP RRASRTQMPN EDEIPEIFRR FFGPDMPGGP QAPRGPRGGG NSLGTGFLIS
QDGYVLTNHH VVDGADTVKI TLSDRREFTA KVIGSDEQSD VALLKIDAKS LPFLRLANAS
LTKPGQWVIA IGSPFGLDHS VTAGIVSAVG RSNPYADQQY VPFIQTDVAI NQGNSGGPLL
NTSGEVVGIN SQIFSNSGGY MGVSFAIPID VAMNSAEQLR ATGKVQRGLL GVGVQTITAE
SAKGLGLTDT RGALVNSVQA GGAAEKAGLQ LGDVILAVND RPVNMSSDLP PLIGALAPGA
KVKLEINRGG KTLTETVVLG ALDAQVAGAP GPAANDDEDA PAGAPGSNPL GLVGQDLTPA
VRQRLGLKAG EGVLVQAPGD VAGEAGLRPR DVVLSVGRNS VGSASALNRE LAKVRPGDTV
MLLVRRGAAT QFIAVTAEAK AG
//
