ID A0A0M9YJM1_9ACTN Unreviewed; 622 AA.
AC A0A0M9YJM1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Protease {ECO:0000313|EMBL:KOU49835.1};
GN ORFNames=ADK56_16720 {ECO:0000313|EMBL:KOU49835.1};
OS Streptomyces sp. MMG1522.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415545 {ECO:0000313|EMBL:KOU49835.1, ECO:0000313|Proteomes:UP000037713};
RN [1] {ECO:0000313|EMBL:KOU49835.1, ECO:0000313|Proteomes:UP000037713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMG1522 {ECO:0000313|EMBL:KOU49835.1,
RC ECO:0000313|Proteomes:UP000037713};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KOU49835.1}.
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DR EMBL; LGDF01000118; KOU49835.1; -; Genomic_DNA.
DR RefSeq; WP_053607103.1; NZ_LGDF01000118.1.
DR AlphaFoldDB; A0A0M9YJM1; -.
DR PATRIC; fig|1415545.3.peg.3586; -.
DR Proteomes; UP000037713; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:KOU49835.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:KOU49835.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 259..281
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 527..607
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
FT REGION 1..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..74
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..142
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..216
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 622 AA; 62386 MW; 1CE08271B1C160A0 CRC64;
MDDGKPTGPQ AKWWSRPAAR RADHPEREAA PGPEAGTPES VPSDETGARD ARSGPAAPAP
AAPSKPPVAP APAAPSEAPV VSAPAVPEDR ESAARPPEPG TDVPRPRAAG QPLHEPDEYR
TPPYGDPGPW APAPPVQRPT PAHGTVVPPG AGGPAPRYAA PGGGVTPPPV PAPTPGDGFP
LPPPQPQAHA PQPPHGAPEH PAPEHVPAPA PPPQQTQTHT QPQTQWLQYD PWGAPGEPLT
RPGPEGGDPG RRKKRRGGAF MGALLLALVA GGIGGGVGAY VERNGGLTTV ELPQADRDNG
DRAPESVAGI AASALPSVVT LHVSGAAESG TGTGFVLDAQ GHILTNNHVV APAGSGGDIT
VTFSTGETAS AELVGKDSGY DLAVVKVRGV SGLKPLPLGN SDNVQVGDPV VAIGAPFDLS
NTVTSGIISA KQRPITAGGE KGDGSDISYV DALQTDAPIN PGNSGGPLVD TRAHVIGINS
AIRAADSGRG PESGGQSGSI GLGFAIPINQ GKRVAEELIS TGRATHPVIG VTLDMKYTGD
GAKVGAKDAE GGPAVAADGP AAKAGIRSGD VITHVEGQRV HSGEELIVKI RAHRPGDALE
LKLTRGGAER TVTLKLGSAS GA
//
