ID A0A1G6VKN6_9BURK Unreviewed; 492 AA.
AC A0A1G6VKN6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=SAMN05192589_10769 {ECO:0000313|EMBL:SDD54172.1};
OS Paracidovorax valerianellae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Paracidovorax.
OX NCBI_TaxID=187868 {ECO:0000313|EMBL:SDD54172.1, ECO:0000313|Proteomes:UP000198781};
RN [1] {ECO:0000313|EMBL:SDD54172.1, ECO:0000313|Proteomes:UP000198781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16619 {ECO:0000313|EMBL:SDD54172.1,
RC ECO:0000313|Proteomes:UP000198781};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FMZC01000007; SDD54172.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6VKN6; -.
DR STRING; 187868.SAMN05192589_10769; -.
DR Proteomes; UP000198781; 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, ECO:0000313|EMBL:SDD54172.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198781};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..492
FT /note="Probable periplasmic serine endoprotease DegP-like"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038413187"
FT DOMAIN 279..339
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 88..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 129
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 159
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 230
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 492 AA; 52078 MW; 8A516A13F6AC57E5 CRC64;
MTTNWKNLQS CAVAVAMALT AATAVVPADV LAQTPPPTVR GLPDFTDLVD QVGPSVVNIR
TLEKATERAG PNAMDEEMLE FFRRFGVPVP PNVPRQQRPQ RPQPDEEQPR GVGSGFILTQ
DGYVMTNAHV VEGADEVIVT LTDKREFKAK IVGADKRTDV AVVKIEATGL PAVKVGDLNR
LRVGEWVMAI GSPFGLENSV TAGIVSAKQR DTGDYLPFIQ TDVAINPGNS GGPLINMRGE
VVGINSQIYS RSGGFMGISF AIPMDEAIRV SDQLRATGRV TRGRIGVQIG QVTKDVAESI
GLGKPQGALV SGVEAGSPAD KAGVEAGDII TKFDGKTIEK TADLPRLVGN TKPGNKSTVT
VFRRGATKDL SITVAEIEPD DKPVASKGAE KEGAKPKPSP AAQQLGLSVA DLTDAQKKEL
KLKGGVRVNA ATDAAARAGL REGDVILSIA NIEVANLKDF ETALGKADKG KAINVLFRRG
EWAQYALIRP AR
//