ID G8RT96_MYCRN Unreviewed; 442 AA.
AC G8RT96;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Trypsin-like serine protease with C-terminal PDZ domain {ECO:0000313|EMBL:AEV74083.1};
GN OrderedLocusNames=MycrhN_3564 {ECO:0000313|EMBL:AEV74083.1};
OS Mycolicibacterium rhodesiae (strain NBB3) (Mycobacterium rhodesiae).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=710685 {ECO:0000313|EMBL:AEV74083.1, ECO:0000313|Proteomes:UP000005442};
RN [1] {ECO:0000313|EMBL:AEV74083.1, ECO:0000313|Proteomes:UP000005442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBB3 {ECO:0000313|EMBL:AEV74083.1,
RC ECO:0000313|Proteomes:UP000005442};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Gu W., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A.,
RA Rutledge P., Paulsen I., Coleman N., Woyke T.;
RT "Complete sequence of Mycobacterium rhodesiae NBB3.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR EMBL; CP003169; AEV74083.1; -; Genomic_DNA.
DR RefSeq; WP_014211839.1; NC_016604.1.
DR AlphaFoldDB; G8RT96; -.
DR STRING; 710685.MycrhN_3564; -.
DR MEROPS; S01.494; -.
DR KEGG; mrh:MycrhN_3564; -.
DR PATRIC; fig|710685.3.peg.3572; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_3_4_11; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000005442; Chromosome.
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:AEV74083.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:AEV74083.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005442};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 79..101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 348..429
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 442 AA; 43574 MW; 975EC0CADCD7C9EC CRC64;
MTNTPPRAPR HPYRPPYADH VMGQGHPSDA TTGTYRSPYD WRYAGQAVIT PRYDSYHTAR
QEITGPIAIQ RPKNSRNRLT IIGGVVAVAV VSGGIGAAVV AGQSEPSAVS HTAVAQGPGS
RPAANAPAGS VEEVAAKVMP SVVKLQIDSG NSSGEGSGIV LTSDGLILTN NHVVAEAAAS
SRYDGGRGIK ATVSFSDGQT VPFEVVGTDP SGDIAVVRAQ GVSGLTPIAI GSSADVQVGQ
NVVAIGSPLG LQGTVTTGIV SALNRPVAAG DGSGEATSVI DAIQTDAAIN PGNSGGALVN
MNGELIGVNS AIATLGGGGG ESGGAPNGSI GLGFAIPSDQ AKRIADELIS NGTATHGSLG
VQLSKDPGAG GAAIAKVVAG SPAAAAGLPS GAVITKVDDR VIDGPEALVA AVRSKAPGDT
VTLTYVDESG ADQTAQVTLG QA
//
