ID A0A0D6SBL9_9PSED Unreviewed; 385 AA.
AC A0A0D6SBL9;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Probable periplasmic serine endoprotease DegP-like {ECO:0000256|ARBA:ARBA00013958};
DE AltName: Full=Protease Do {ECO:0000256|ARBA:ARBA00032850};
GN ORFNames=SZ55_3747 {ECO:0000313|EMBL:KIV65985.1};
OS Pseudomonas sp. FeS53a.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1604022 {ECO:0000313|EMBL:KIV65985.1, ECO:0000313|Proteomes:UP000032531};
RN [1] {ECO:0000313|EMBL:KIV65985.1, ECO:0000313|Proteomes:UP000032531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FeS53a {ECO:0000313|EMBL:KIV65985.1,
RC ECO:0000313|Proteomes:UP000032531};
RA de Souza R., Sant'Anna F.H., Ambrosini A., Tadra-Sfeir M., Faoro H.,
RA Alvarenga S.M., Pedrosa F.O., Souza E.M., Passaglia L.M.;
RT "Genome of Pseudomonas sp. FeS53a associated with rice cropped in iron-
RT stressed soils.";
RL Submitted (JAN-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:KIV65985.1}.
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DR EMBL; JYFT01000060; KIV65985.1; -; Genomic_DNA.
DR RefSeq; WP_044409654.1; NZ_JYFT01000060.1.
DR AlphaFoldDB; A0A0D6SBL9; -.
DR PATRIC; fig|1604022.3.peg.5108; -.
DR Proteomes; UP000032531; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0000313|EMBL:KIV65985.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Protease {ECO:0000313|EMBL:KIV65985.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000032531};
KW Stress response {ECO:0000256|ARBA:ARBA00023016};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 271..362
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 385 AA; 40955 MW; 03BA572883911AD6 CRC64;
MSKALRFFGW PLLVGVLVAL LIIQQYPELV GLPRQEVHLQ EAPRYSVSRP GPESYAEAVN
SASPAVVNLY TTKVVSKPAH PLFDDPQFRR FFGDNLPRQR RMESSLGSAV IMSPEGYLLT
NNHVTAGAEQ IVVALKDGRE TLARLVGSDP ETDLAVLKID LDNLPAITLG RSDAIRIGDV
ALAIGNPFGV GQTVTMGIIS ATGRNQLGLN TYEDFIQTDA AINPGNSGGA LVDAAGNLVG
INTAIFSRTG GSQGIGFAIP TKLALEVMKA IIEHGQVIRG WLGIEVQPLT PELAESFGLT
GRPGIVVAGI YRDSPAQRAN LLPGDIILAI DGEPAGDGRR SMNQVARTKP GEKVSIQVMR
NGKLLELVAE VGLRPPQQVA PAEND
//
