ID A0A235GE64_9NOCA Unreviewed; 538 AA.
AC A0A235GE64;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=S1-C subfamily serine protease {ECO:0000313|EMBL:OYD71517.1};
GN ORFNames=BDB13_5192 {ECO:0000313|EMBL:OYD71517.1};
OS Rhodococcus sp. OK302.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1882769 {ECO:0000313|EMBL:OYD71517.1, ECO:0000313|Proteomes:UP000215121};
RN [1] {ECO:0000313|EMBL:OYD71517.1, ECO:0000313|Proteomes:UP000215121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK302 {ECO:0000313|EMBL:OYD71517.1,
RC ECO:0000313|Proteomes:UP000215121};
RA Pelletier D.;
RT "Populus root and rhizosphere microbial communities from Tennessee, USA.";
RL Submitted (AUG-2017) 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:OYD71517.1}.
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; NPJZ01000001; OYD71517.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A235GE64; -.
DR Proteomes; UP000215121; 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.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:OYD71517.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:OYD71517.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 194..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 438..526
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 39..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 538 AA; 54412 MW; 1D1911B61D773B71 CRC64;
MPGSVLWANG CPVVGANELF GAAASAFIRR SAILDRVTDG QRGHSGVDTD SSANGLVDRP
ADAPVLEPRP VYRPQIDPAS RQVFGRPSGV DGSFSPTSVR GVPAPDVVVG SPDPVLAEAF
GRPDGETESI GRDPDAEAAS EPEDEQPSDP WRDPASSVAL GSPAAQTQPE ILPPAPKLDV
RDVLFGRKVA PSALAALAGI ALVIALVGGL LATVITADRG ALTSQRVTLV QSGSGEQPQS
QVAKVADAVL PSVVSIQVAV GDQGSTGSGV VIDGAGYIVT NNHVISSAVP PAQNARIQVI
FSDGTKTDAQ IVGRDVKTDL AVLKVAADNL TVAQLGKSGD VQVGDEVIAV GSPLGLSKTV
TSGIVSALNR PLRLSGDGTD TNAVIDAVQT DAAINHGNSG GALVDDEARV IGINTAMLSE
SGGSVGLGFA IPIDTVTTVA QAIIRDGSVH HPDIGVNART AVNDATSGAA VANVRDGSPA
QRAGIVEGDV IVKVGDRPVT SADELVVAVN STTIGQPVNV QLIRDGRQVD ISVTPVSD
//
