ID A0A2U2ZJI2_9ACTN Unreviewed; 514 AA.
AC A0A2U2ZJI2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Protease {ECO:0000313|EMBL:PWI12399.1};
GN ORFNames=DIZ27_02225 {ECO:0000313|EMBL:PWI12399.1};
OS Streptomyces sp. NWU339.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2185284 {ECO:0000313|EMBL:PWI12399.1, ECO:0000313|Proteomes:UP000245372};
RN [1] {ECO:0000313|EMBL:PWI12399.1, ECO:0000313|Proteomes:UP000245372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NWU339 {ECO:0000313|EMBL:PWI12399.1,
RC ECO:0000313|Proteomes:UP000245372};
RA Adegboye M.F., Lobb B., Babalola O., Doxey A.C., Ma K.;
RT "Draft genomes of two novel cellulolytic Streptomyces strains isolated from
RT South African rhizosphere soils.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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:PWI12399.1}.
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DR EMBL; QFRK01000001; PWI12399.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U2ZJI2; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000245372; 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; 2.40.10.120; -; 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.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:PWI12399.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:PWI12399.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000245372};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 149..172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 418..498
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
FT REGION 1..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..59
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..118
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 514 AA; 50176 MW; ED4C6DFD0C5E15B0 CRC64;
MSTENEGTNE GASVPPAPSV PPTPVDAPAA PAHQERPAPE GGSPTTSMPP VPPTAPGAAP
GHGTPEHPAY GDHAGYGGHG AREQAPAGPP SGAPSGAPAG TSSAPDPSWP PPPAPGIPSY
DGGAGHGAGG WGSYQQPAPK NGGGKRGRLA AAVLAAALVA GGLGGGLGYT LAKNNDDGNG
STTVSSSTSG GNVKRDPGTV AAVAAKALPS TVTIEAQGSS GEGGTGTGFV FDTQGHIVTN
NHVVAEAVEG GKVAATFPDG KKYDAEVVGH AQGYDVAVIK LKNAPSNLKP LTLGNSDEVA
VGDSTIAIGA PFGLSNTVTT GIISAKNRPV ASSDGTGNQA SYMSALQTDA SINPGNSGGP
LLDAQGNVIG INSAIQSTSN GGFGTGQAGS IGLGFAIPIN QAKYVAQELI KTGKPVYAKI
GASVSLEEGA GGAKITDQGA GGSAAVDPGG PADQAGLRPG DVITKLDDRV IDSGPTLIGE
IWTHKPGDKV TLTYERGGKQ QTTELTLGSR IGDS
//
