ID A0A1H0MMJ6_9PSEU Unreviewed; 506 AA.
AC A0A1H0MMJ6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Putative serine protease PepD {ECO:0000313|EMBL:SDO81632.1};
GN ORFNames=SAMN05421507_10450 {ECO:0000313|EMBL:SDO81632.1};
OS Lentzea jiangxiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Lentzea.
OX NCBI_TaxID=641025 {ECO:0000313|EMBL:SDO81632.1, ECO:0000313|Proteomes:UP000199691};
RN [1] {ECO:0000313|EMBL:SDO81632.1, ECO:0000313|Proteomes:UP000199691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.6609 {ECO:0000313|EMBL:SDO81632.1,
RC ECO:0000313|Proteomes:UP000199691};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR EMBL; FNIX01000004; SDO81632.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0MMJ6; -.
DR STRING; 641025.SAMN05421507_10450; -.
DR Proteomes; UP000199691; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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; 2.40.10.10; 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:SDO81632.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:SDO81632.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 157..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 415..494
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 506 AA; 50094 MW; EFE767DFE65D91E8 CRC64;
MGMTESNQPA QQPDEPDAVQ PSAGQTDSGA REQGPSLPGP GRPDPLQGGS GQAGAQSAPA
GLGDVPASFT PAQPQVPSPD AGQTQLGGSG PGRQLPPPGS GQPHPLGPGA PAVQFGAEHP
AGPPSAPFAG PQTGQYYLPP GFQPPPAAPR PKGRGKVVAG VAALVLLVGG LSGGLGGYLG
YNFANDSSAI SSLDAPRPAS QTSNAPAGSV EDVANRLLPS VVQIQVVTRS GAGEGSGFVI
SSNGQVVTNN HVIEGAAAGG TIKVVFQDGR TATAKILGRD PSSDIAVIQA EGISGAPVVQ
LGNSADLKIG QGVVAIGSPF ELSGTVTSGI VSSLNRPVSA GGDARNSQAT VLNAIQTDAA
INPGNSGGPL VNMQGQVVGI NSAIYSPNSA GGQAGSVGIG FAIPMDQARR TIDEIVKTGK
PRQTVLGVKV ESTEQGARIS EITSGGAAEK AGLKAGDVIT KFGDRRIDES DTLVAAVRSK
APGDKVTITL SDNRTVEATL DGVEVG
//
