ID H0E561_9ACTN Unreviewed; 395 AA.
AC H0E561;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=Protease Do {ECO:0000313|EMBL:EHN11184.1};
GN ORFNames=PAI11_19480 {ECO:0000313|EMBL:EHN11184.1};
OS Patulibacter medicamentivorans.
OC Bacteria; Actinomycetota; Thermoleophilia; Solirubrobacterales;
OC Patulibacteraceae; Patulibacter.
OX NCBI_TaxID=1097667 {ECO:0000313|EMBL:EHN11184.1, ECO:0000313|Proteomes:UP000005143};
RN [1] {ECO:0000313|EMBL:EHN11184.1, ECO:0000313|Proteomes:UP000005143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=I11 {ECO:0000313|EMBL:EHN11184.1,
RC ECO:0000313|Proteomes:UP000005143};
RX PubMed=23212173; DOI=10.1007/s10532-012-9610-5;
RA Almeida B., Kjeldal H., Lolas I., Knudsen A.D., Carvalho G., Nielsen K.L.,
RA Barreto Crespo M.T., Stensballe A., Nielsen J.L.;
RT "Quantitative proteomic analysis of ibuprofen-degrading Patulibacter sp.
RT strain I11.";
RL Biodegradation 24:615-630(2013).
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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:EHN11184.1}.
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DR EMBL; AGUD01000138; EHN11184.1; -; Genomic_DNA.
DR RefSeq; WP_007573994.1; NZ_AGUD01000138.1.
DR AlphaFoldDB; H0E561; -.
DR MEROPS; S01.500; -.
DR PATRIC; fig|1097667.3.peg.1931; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000005143; 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; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
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 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:EHN11184.1};
KW Protease {ECO:0000313|EMBL:EHN11184.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005143}.
FT DOMAIN 261..322
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 348..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 395 AA; 38454 MW; 0D2A35A9AC12C599 CRC64;
MPRPSRSLIV LCSAAVAGGT GGAVLVGAIA PGGHTTTVTQ AAAAAADSRP VADTSGGALS
ARQIYQRSKD AIAYVTAASS RGGGSAGTAT GSGFVISADG YVVTNEHVID GADEVTVKIG
DRKEATAKVV GVDASTDIAL LKVDTGGAQL PTLALGDSTT IQVGDPTYAI GNPYGLDRTL
TTGVISALHR SIQSPNGYAI NDVLQTDAAL NPGNSGGPLL DSQGRVVGVN SQIATSSSGS
GGEGGNTGVG FAVPSSTVAR VVEQLRASGK ATHAYLGVST ADGQGGSSTA GATLAAVPSG
GPAADGGLRR GDVVTAIDDA KVGDAASLGT AVDAHRPGDR VTVHYRRDGD ERTAKVTLAE
RPAGTTQGAT QQGSGGQPGD GSGGSGSGLP YGLVP
//
