ID A0A0X3VGF4_9ACTN Unreviewed; 527 AA.
AC A0A0X3VGF4;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Protease {ECO:0000313|EMBL:KUL43879.1};
GN ORFNames=ADL12_06695 {ECO:0000313|EMBL:KUL43879.1};
OS Streptomyces regalis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68262 {ECO:0000313|EMBL:KUL43879.1, ECO:0000313|Proteomes:UP000053923};
RN [1] {ECO:0000313|Proteomes:UP000053923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3151 {ECO:0000313|Proteomes:UP000053923};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (OCT-2015) 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:KUL43879.1}.
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DR EMBL; LLZG01000029; KUL43879.1; -; Genomic_DNA.
DR RefSeq; WP_062699546.1; NZ_LLZG01000029.1.
DR AlphaFoldDB; A0A0X3VGF4; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000053923; 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 SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:KUL43879.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:KUL43879.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053923};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 163..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 437..520
FT /note="PDZ"
FT /evidence="ECO:0000259|Pfam:PF13180"
FT REGION 1..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..120
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 527 AA; 51343 MW; 315EEB6AA214DDEC CRC64;
MSTENEGAAV PPAPSAPPVP VDAPAVPASQ ERPAPEGDAA PTTQLPPVPN GTLANANGTQ
PHAADAAANG SQPYGAEAAS NRAQQPAAPA ASNADQPPAS QGSAPDASWP PPPPPTPPYA
DSGAAAGGAG AGAGAGAGDG VGSGWGATYQ QPAPKSGRGR GGLLAAVLIA ALVAGGLGGG
LGYTLAKNDD TSSSTTVSAA DSGGDLKRDP GTVASVTARA LPSTVTIEAE SSSGEGGTGT
GFVFDTEGHI VTNNHVVADA VDGGKLTATF PNGKKYDAEV VGHAQGYDVA VIKLKSAPSD
LKPLTLGNSD DVAVGDSTIA IGAPFGLSNT VTTGIISAKN RPVASSDGTG SNASYMSALQ
TDASINPGNS GGPLLDAQGN VIGINSAIQS AANGLGGTSQ SGSIGLGFAI PINQAKYVAK
QLIKTGKPVY AKIGASVSLE DTTDGAKITE QGASGSDPVE AGGPAAKAGL KPGDVITKLD
DRVIDSGPTL IGEIWTHQPG DKVTITYERG GQSHTVELTL GSRTGDS
//