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Database: UniProt
Entry: A0A1G9FFT3_9PSED
LinkDB: A0A1G9FFT3_9PSED
Original site: A0A1G9FFT3_9PSED 
ID   A0A1G9FFT3_9PSED        Unreviewed;       383 AA.
AC   A0A1G9FFT3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Probable periplasmic serine endoprotease DegP-like {ECO:0000256|ARBA:ARBA00013958};
DE   AltName: Full=Protease Do {ECO:0000256|ARBA:ARBA00032850};
GN   ORFNames=SAMN05216186_11196 {ECO:0000313|EMBL:SDK87197.1};
OS   Pseudomonas indica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=137658 {ECO:0000313|EMBL:SDK87197.1, ECO:0000313|Proteomes:UP000198706};
RN   [1] {ECO:0000313|EMBL:SDK87197.1, ECO:0000313|Proteomes:UP000198706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 21544 {ECO:0000313|EMBL:SDK87197.1,
RC   ECO:0000313|Proteomes:UP000198706};
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; FNFD01000011; SDK87197.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9FFT3; -.
DR   STRING; 137658.SAMN05216186_11196; -.
DR   OrthoDB; 9758917at2; -.
DR   Proteomes; UP000198706; Unassembled WGS sequence.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-KW.
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; 2.40.10.120; -; 1.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   PANTHER; PTHR43343; PEPTIDASE S12; 1.
DR   PANTHER; PTHR43343:SF3; PROTEASE DO-LIKE 8, CHLOROPLASTIC; 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   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022825};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Protease {ECO:0000313|EMBL:SDK87197.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198706};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016}.
FT   DOMAIN          272..335
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
SQ   SEQUENCE   383 AA;  40842 MW;  E5DC2202FBD86BDF CRC64;
     MLKALRFLGW PLLVGVLLAL LIIQRYPQWV GLPHQEAQVR QAPISLLPQQ GPVSYAQAVS
     RAAPAVANLY TAKVVTRPSH PLFEDPVFRR FYGERSLPRQ RRMESSLGSA VIMSPEGYLL
     TNNHVTADAD QIVVALKDGR ETLARVIGSD PETDLAVLKI DLENLPAITL GSSDNISIGD
     VALAIGNPFG VGQTVTMGII SATGRNQLGL NTYEDFIQTD AAINPGNSGG ALVDARGNLI
     GINTAIFSKS GGSQGIGFAI PAKLAMEVMQ AIIEHGQVIR GWLGIEVQPL TPELAESFDM
     EGRPGIVVAG IYRDGPAERA GLQPGDLILS IDGEPANDGR SSMNQVARTR PGEVIDIDVM
     RNGKELKLQA EVGVRPPVSS TPE
//
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