TRI2_STRCO
ID TRI2_STRCO Reviewed; 1171 AA.
AC Q9RKB9;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Putative tricorn protease homolog 2;
DE EC=3.4.21.-;
GN Name=tri2; OrderedLocusNames=SCO3168; ORFNames=SCE87.19;
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).
CC -!- FUNCTION: Degrades oligopeptides in a sequential manner. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S41B family. {ECO:0000305}.
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DR EMBL; AL939115; CAB59664.1; -; Genomic_DNA.
DR RefSeq; NP_627384.1; NC_003888.3.
DR RefSeq; WP_011028806.1; NC_003888.3.
DR AlphaFoldDB; Q9RKB9; -.
DR SMR; Q9RKB9; -.
DR STRING; 100226.SCO3168; -.
DR MEROPS; S41.006; -.
DR GeneID; 1098602; -.
DR KEGG; sco:SCO3168; -.
DR PATRIC; fig|100226.15.peg.3228; -.
DR eggNOG; COG0793; Bacteria.
DR eggNOG; COG4946; Bacteria.
DR HOGENOM; CLU_005503_1_0_11; -.
DR InParanoid; Q9RKB9; -.
DR OMA; WLRWPIS; -.
DR PhylomeDB; Q9RKB9; -.
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; -; 2.
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 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Protease; Reference proteome; Serine protease.
FT CHAIN 1..1171
FT /note="Putative tricorn protease homolog 2"
FT /id="PRO_0000207200"
FT REGION 432..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..941
FT /note="PDZ-like"
FT REGION 1149..1171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 827
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 1051
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P96086"
FT ACT_SITE 1109
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P96086"
FT BINDING 1002..1004
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P96086"
FT BINDING 1079..1081
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P96086"
FT SITE 1052
FT /note="Transition state stabilizer; via amide nitrogen"
FT /evidence="ECO:0000250|UniProtKB:P96086"
SQ SEQUENCE 1171 AA; 125661 MW; 9C53019CEC0B0A25 CRC64;
MRGARKSMGR VSYLRLPHLS GDQLCFVAED DLWLASLDGP GRAWRLTVDR TKAGPPRFSP
DGRHIAYTSW RTLVPEVHLV PVDGGPGRQL THWGGLDTRV CGWSPPDPDG TTAVLAVASH
GEPFSHLTWA YKVTPDGDPG RKLPWGPVTD IQAADLDGER RTLLLTGTPP HEPAAWKRYR
GGATGRLWLH GERLLPDLGG HLSAPMFVGG RIAFLSDHEG VGNLYSCAQD GTGLRRHTDH
DAFYARNAAS DGTRVVYQCA GDLWIVDDLA PGSAPRRLDV RLSGPRAGRR THQVPAAQHV
GGISVDETGR ASAVVVRGSL YWLTHRDGPA RTIADTPGVR VRLPEMLGES GRIAYVTDAE
GEDAVEISYL PRATGGRAAR RLASGRLGRV LELVSDPAGD RLAVASHDGR LLILDVAEPD
TEVTLALEAV DAGYPPDAGD EDAAGTAARA DSAPDAPAED TDARDIAAGT GTGDIADADA
AAGGTVTPGS PGTPATAGGQ VTELIRSVNG PVRDLAFSPD GTWLTWSHPG IGRTLRQIKM
ARIDGPEGTL VVDVTNGRFE DENPVFTRDG RYLAFLSWRG FDPVYDVHTG DLSFPLGCRP
YLVPLSSATP SPFALNPEGR PAAGGLDPLE DEPGEGGAVM VEVEGLESRV TPFPVTASKY
SALEPVAGGG LVWLRWPISG ALGETFANPA DPSERPTLEH FNLAKAKKSE LVDHLDWFRV
SGDGSRLVVL DEGELRAVPA SEVGDGDSTT WIDLRRILHE VDPAAEWRQA YDEAGRLIRA
YFWDPGMCGI DWDAVLDQYR PLLERVASPD EFADLLREVL GELGTSHAYV VAARRNEGPA
HYQRWQGLLG ANLACRDGRW LVRRILPGDS SDSKARSPLA GTGIRDGAVL THVDGRPVDP
VLGPSPLLAG AGGTTVELTF APAEGCQGPS RRVAVVPLVD ERPLRYQDWV AKRREVVREL
SGGRCGYLHI PDMGGSGWAQ FNRDLRMEVS RPALIVDVRG NAGGHISELV IEKLTRTILG
WDLTRDAQPV SYTSNAPRGP VVAVADEATS SDGDMITAAF KLLRLGPVVG QRTWGGVVGM
TGRHRLGDGS VITVPMNAAW FDAYGWSVEN YGVAPDVEAL RTPLDWAEGR YPVLDEAVRL
ALELLETNPP ATPPGYEAVP DRSRPPLPPR E
