ID J2RT49_9PSED Unreviewed; 386 AA.
AC J2RT49;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Probable periplasmic serine endoprotease DegP-like {ECO:0000256|ARBA:ARBA00013958};
DE AltName: Full=Protease Do {ECO:0000256|ARBA:ARBA00032850};
GN ORFNames=PMI29_05902 {ECO:0000313|EMBL:EJM52664.1};
OS Pseudomonas sp. GM49.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1144331 {ECO:0000313|EMBL:EJM52664.1, ECO:0000313|Proteomes:UP000007288};
RN [1] {ECO:0000313|EMBL:EJM52664.1, ECO:0000313|Proteomes:UP000007288}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM49 {ECO:0000313|EMBL:EJM52664.1,
RC ECO:0000313|Proteomes:UP000007288};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJM52664.1}.
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DR EMBL; AKJL01000314; EJM52664.1; -; Genomic_DNA.
DR RefSeq; WP_008003891.1; NZ_AKJL01000314.1.
DR AlphaFoldDB; J2RT49; -.
DR PATRIC; fig|1144331.3.peg.5621; -.
DR Proteomes; UP000007288; 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:0000313|EMBL:EJM52664.1};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Protease {ECO:0000313|EMBL:EJM52664.1};
KW Stress response {ECO:0000256|ARBA:ARBA00023016}.
FT DOMAIN 271..334
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 386 AA; 40999 MW; 28ABB936443CE365 CRC64;
MLKALRFSGW PLLAGVLVAL LIIQRYPQWV GLPSLDVNLQ QAPQTTSMQQ GPVSYAEAVS
TAAPSVVNLY TTKVINKPNH PLFEDPQFRR FFGDNSPKQK RMESSLGSGV IMSPEGYILT
NNHVTSGADQ IVVALKDGRE TLARVIGSDP ETDLAVLKID LKNLPSITVG RSDNIRIGDV
ALAIGNPFGV GQTVTMGIIS ATGRNQLGLN NYEDFIQTDA AINPGNSGGA LVDAIGNLTG
INTAIFSKSG GSQGIGFAIP VKLAMEVMKS IIEHGQVIRG WLGIEVQPLT QELAESFGLS
GRPGIVVAGI FRDGPAQKAG LQLGDVILAI DGEPAGDGRR SMNQVARIKP TDKVAIEVMR
NGKELKLTAE VGLRPPPAPA QEKEEE
//
