TRI1_STRCO
ID TRI1_STRCO Reviewed; 1067 AA.
AC Q9RDE2;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Tricorn protease homolog 1;
DE EC=3.4.21.-;
GN Name=tri1; OrderedLocusNames=SCO2549; ORFNames=SCC77.16c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [2]
RP CHARACTERIZATION.
RC STRAIN=A3(2) / NRRL B-16638;
RX PubMed=11347893; DOI=10.1515/bc.2001.055;
RA Tamura N., Pfeifer G., Baumeister W., Tamura T.;
RT "Tricorn protease in bacteria: characterization of the enzyme from
RT Streptomyces coelicolor.";
RL Biol. Chem. 382:449-458(2001).
CC -!- FUNCTION: Degrades oligopeptides in a sequential manner. {ECO:0000250}.
CC -!- ACTIVITY REGULATION: Stimulated by MgCl2.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5-7.8.;
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.;
CC -!- SUBUNIT: Forms a homohexameric complex; it is not known if it assembles
CC into higher-order structures.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S41B family. {ECO:0000305}.
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DR EMBL; AL939113; CAB66227.1; -; Genomic_DNA.
DR RefSeq; NP_626787.1; NC_003888.3.
DR RefSeq; WP_011028423.1; NZ_VNID01000001.1.
DR AlphaFoldDB; Q9RDE2; -.
DR SMR; Q9RDE2; -.
DR STRING; 100226.SCO2549; -.
DR MEROPS; S41.006; -.
DR GeneID; 1097983; -.
DR KEGG; sco:SCO2549; -.
DR PATRIC; fig|100226.15.peg.2594; -.
DR eggNOG; COG0793; Bacteria.
DR eggNOG; COG4946; Bacteria.
DR HOGENOM; CLU_005503_1_0_11; -.
DR InParanoid; Q9RDE2; -.
DR OMA; YLHVPDM; -.
DR PhylomeDB; Q9RDE2; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008236; F:serine-type peptidase activity; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011659; PD40.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR005151; Tail-specific_protease.
DR InterPro; IPR028204; Tricorn_C1.
DR InterPro; IPR029414; Tricorn_PDZ.
DR InterPro; IPR012393; Tricorn_protease.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR43253; PTHR43253; 1.
DR Pfam; PF07676; PD40; 2.
DR Pfam; PF03572; Peptidase_S41; 1.
DR Pfam; PF14684; Tricorn_C1; 1.
DR Pfam; PF14685; Tricorn_PDZ; 1.
DR PIRSF; PIRSF036421; Tricorn_protease; 1.
DR SMART; SM00245; TSPc; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF52096; SSF52096; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Protease; Reference proteome; Serine protease.
FT CHAIN 1..1067
FT /note="Tricorn protease homolog 1"
FT /id="PRO_0000207199"
FT REGION 518..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..851
FT /note="PDZ-like"
FT COMPBIAS 530..545
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 740
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 961
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P96086"
FT ACT_SITE 1019
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P96086"
FT BINDING 914
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P96086"
FT SITE 962
FT /note="Transition state stabilizer; via amide nitrogen"
FT /evidence="ECO:0000250|UniProtKB:P96086"
SQ SEQUENCE 1067 AA; 115647 MW; 10861E9D5FDC286D CRC64;
MGVTQPAAPA YLRFPHPHGE LVAFTAEDDV WLAPLDGGRA WRVSADNVPV NHPRISPDGT
KVAWTSTRDG APEVHVAPVE GGPAKRLTHW GSIRTQVRGW TADGRVLALS TYGQASLRRS
WARALPLDGG PATTLPYGPV GDVAQGPHTV LLSAPMGREA AWWKRYRGGT AGKLWIDRED
DGEFVRLHDG LDGNIEYPFW VGDRIAFLSD HEGTGALYSS LADGSDLRRH TPVDGFYARH
AATDGSRVVY ASAGELWTLD DLDGAEPRRL DIRLGGARVD LQSYPVNAAR WFGSASPDHT
ARGSAVAVRG GVHWVTHRSG PARALAATPG VRNRLPRTFR VDGEEWVVWV TDAEGDDALE
FAPATGLAPG ATARRLAAGQ LGRVLHLAVA PDGSRVAVAS HDGRVLLVER ESGEVREVDR
SEDGDASGLV FSPDSSWLAW SHPGPEPLRQ LKLANTTDLS VSEATPLRFK DYSPAFTLDG
KHLAFLSTRS FDPVYDEHVF DLAFVEGARP YLITLAATTP SPFGPQRHGR PFETPDREET
PDSEGTPTTR IDIEGLADRI VPFPVEAARY SRLRAAKDGV LWLRHPLTGV LGASRANPED
PDPNTELERY DLAQQRVEHL GGDADHFEVS GDGKRVLLWT DGRLKVVPSD RRASGDEDSD
TNITVDLGRV RQTVEPAAEW RQMFDETGRI MRDHYWRADM NGVDWDGVLD RYRPVLDRVA
THDDLVDLLW EVHGELGTSH AYVTPRGGHG SGARQGLLGA DLSRHEDGAW RIDRVLPSET
SDPDARSPLA APGVAVRAGD AIVAVAGQAV DPVTGPGPLL VGTAGKPVEL TVSPSGGGEV
RHAVVVPLAD EEPLRYHAWV ADRRAYVHEK SGGRLGYLHV PDMQAPGWAQ IHRDLRVEVA
REGLVVDVRE NRGGHTSQLV VEKLARRIVG WDLPRGMRPT SYPQDAPRGP VVAVANEFSG
SDGDIVNAAI KALGIGPVVG VRTWGGVIGI DSRYRLVDGT LITQPKYAFW LEGYGWGVEN
HGVDPDVEVP QRPQDHAAGR DPQLDEAIAL ALAALEETPA KTPPSLP
