ID A0A0N1K814_9ACTN Unreviewed; 504 AA.
AC A0A0N1K814;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Protease {ECO:0000313|EMBL:KPC82338.1};
GN ORFNames=ADK82_13640 {ECO:0000313|EMBL:KPC82338.1};
OS Streptomyces sp. NRRL S-4.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519471 {ECO:0000313|EMBL:KPC82338.1, ECO:0000313|Proteomes:UP000037987};
RN [1] {ECO:0000313|Proteomes:UP000037987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL S-4 {ECO:0000313|Proteomes:UP000037987};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-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:KPC82338.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LGKJ01000112; KPC82338.1; -; Genomic_DNA.
DR RefSeq; WP_053929572.1; NZ_LGKJ01000112.1.
DR AlphaFoldDB; A0A0N1K814; -.
DR STRING; 1519471.ADK82_13640; -.
DR PATRIC; fig|1519471.3.peg.2829; -.
DR Proteomes; UP000037987; 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:KPC82338.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:KPC82338.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 138..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 408..488
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
FT REGION 1..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..51
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..108
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 504 AA; 49378 MW; 6C7223DC46D21B81 CRC64;
MSTENEGNEG NAVPAAPSVP SVPPVPAAAP EGTPQGGRPA PEAPPAAPAD APTAQVPTAT
HHDGTGPAHH DGTGPAAATH EQHPYAPPSP RPPGGSAGWP PPPPAVPSYA DGGDGHPAWG
APVPSGPEPS RKRRAGGLVA AVAVAALVAG GVGGALGYWA ADSNDSGSSG STTVAASNSP
KDFKREPGTV AGVAASALPS VVTIDAQSGD GEGGTGTGFV YDKEGHILTN NHVVASAADS
GQLTVTFSNG KKYDAEVVGR AQGYDVAVLK LKNAPDGLAP LALGDSDKVA VGDSTIAIGA
PFGLSNTVTT GIISAKDRPV ASGDGSSNKN SYMSALQTDA SINPGNSGGP LLDAGGAVIG
INSAIQSTSG GGVGQSQAGS IGLGFAIPVN QAKNVAEQLI RTGQPVYPVI GATVTMEEKT
GGAVISDEGA GGTPAVTPDG PAADAGLKAG DVITKFNDTV VESGPTLIGE IWTHKPGDKV
TLTYKRDGRT ATAELTLGER KGDS
//
