ID A0A0X3XJ36_9ACTN Unreviewed; 680 AA.
AC A0A0X3XJ36;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Protease {ECO:0000313|EMBL:KUL69809.1};
GN ORFNames=ADL34_29520 {ECO:0000313|EMBL:KUL69809.1};
OS Streptomyces sp. NRRL WC-3605.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609103 {ECO:0000313|EMBL:KUL69809.1, ECO:0000313|Proteomes:UP000052945};
RN [1] {ECO:0000313|EMBL:KUL69809.1, ECO:0000313|Proteomes:UP000052945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL WC-3605 {ECO:0000313|EMBL:KUL69809.1,
RC ECO:0000313|Proteomes:UP000052945};
RA Gilbert D.G.;
RL Submitted (OCT-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:KUL69809.1}.
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DR EMBL; LLZN01000091; KUL69809.1; -; Genomic_DNA.
DR RefSeq; WP_062668700.1; NZ_LLZN01000091.1.
DR AlphaFoldDB; A0A0X3XJ36; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000052945; 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:KUL69809.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:KUL69809.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000052945};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 317..340
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 585..665
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
FT REGION 1..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..199
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..270
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 680 AA; 67942 MW; 38F8A80514A635BC CRC64;
MNEGKPTRAK WWNRSRPQEG SPGASGASAD GDFELARPAR PQETPGTADD YPLPPAPDSR
ATPDGDFELA VPQRQPVPQP REGEEPSETA TTADASASGA VSPAEGGETD TPANAPAAPV
SDLSTPAVDA GTGTEASQAP GSPSADAGTG TEATSAPVAP APPQDASPRP LHDPDPYSTP
PYGEPGPWAP APPVQHPAAT PAHGTPAAAA PAPAPHQQAV PAQSAPAPHQ QAVPAQSAPA
PHHQAPGAPV HAAPDPAFAD APPPAVPTVP GAPGTLGTPH DPWRNYDPWA RAAQRAAAAP
LQESGAGVRR RRGVKGALLV GALVIALVSG GVGGALGAYL ERNGGLDTVE LPQAGAEAPD
RAPDSVAGIA ARALPSVVTL HVSGRSEQGT GTGFVLDDRG HILTNNHVVE PAGDDGEISV
TFHSGDTAKA TVVGRDSGYD LAVVKVTGVS GLRPLPLGNS ENVQVGDPVV AIGAPFDLEG
TVTSGIISAK QRPITAGGED GDGSDVSYVD ALQTDAPINP GNSGGPLLDR AGRVVGINSA
IRSAGSGAEP DGGQAGSIGL GFAIPVNQAK RVAEELINTG KATHPVIGVT LDMAYGGDGA
RVGTKDSEGG PAVTKGGPGA KAGIEPGDVI TEIDGARVHS GEELIIKTRA HRPGDRLELT
LKRDGKEITL KLTLGSSSGR
//
