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Database: UniProt
Entry: A0A1G6VKN6_9BURK
LinkDB: A0A1G6VKN6_9BURK
Original site: A0A1G6VKN6_9BURK 
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
//
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