TRI_SACS2
ID TRI_SACS2 Reviewed; 1068 AA.
AC P95871;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Tricorn protease homolog;
DE EC=3.4.21.-;
GN Name=tri; OrderedLocusNames=SSO2098; ORFNames=C06024, C06_007;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=8899719; DOI=10.1111/j.1365-2958.1996.tb02666.x;
RA Sensen C.W., Klenk H.-P., Singh R.K., Allard G., Chan C.C.-Y., Liu Q.Y.,
RA Penny S.L., Young F., Schenk M.E., Gaasterland T., Doolittle W.F.,
RA Ragan M.A., Charlebois R.L.;
RT "Organizational characteristics and information content of an archaeal
RT genome: 156 kb of sequence from Sulfolobus solfataricus P2.";
RL Mol. Microbiol. 22:175-191(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
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; Y08256; CAA69507.1; -; Genomic_DNA.
DR EMBL; AE006641; AAK42276.1; -; Genomic_DNA.
DR PIR; S73091; S73091.
DR AlphaFoldDB; P95871; -.
DR SMR; P95871; -.
DR STRING; 273057.SSO2098; -.
DR MEROPS; S41.005; -.
DR EnsemblBacteria; AAK42276; AAK42276; SSO2098.
DR KEGG; sso:SSO2098; -.
DR PATRIC; fig|273057.12.peg.2178; -.
DR eggNOG; arCOG03384; Archaea.
DR HOGENOM; CLU_005503_1_0_2; -.
DR InParanoid; P95871; -.
DR OMA; YLHVPDM; -.
DR PhylomeDB; P95871; -.
DR Proteomes; UP000001974; 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; 1.
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..1068
FT /note="Tricorn protease homolog"
FT /id="PRO_0000207194"
FT REGION 61..326
FT /note="Six-bladed beta propeller"
FT /evidence="ECO:0000250"
FT REGION 338..686
FT /note="Seven-bladed beta propeller"
FT /evidence="ECO:0000250"
FT REGION 692..762
FT /note="C-1"
FT /evidence="ECO:0000250"
FT REGION 771..864
FT /note="PDZ-like"
FT REGION 865..1068
FT /note="C-2"
FT /evidence="ECO:0000250"
FT ACT_SITE 756
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 974
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P96086"
FT ACT_SITE 1032
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P96086"
FT BINDING 927
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P96086"
FT SITE 975
FT /note="Transition state stabilizer; via amide nitrogen"
FT /evidence="ECO:0000250|UniProtKB:P96086"
SQ SEQUENCE 1068 AA; 123115 MW; 9F34FC13C9F3D4EC CRC64;
MLSLLIIRAT QFAITSFRCE STIYRYCAKY YYIGFHNHKD LIGVKEFCGK HYILKIIHYH
MKAYYMYPDI RGDLISFTSD DDVWLLSLKD MKPLRITSGL GVSTRPKISP SGRKVAFSVI
WLKSGKQGGD IYVVEDGQAR RVTYFGSRNS RVAGWISEDE IIVITDFHTP FIQWTEAYKV
NVNNGKTEKL PFGMLSNIVI KDDIIVIARG YQDLPNWKGY KGGTKGELWI SSDGGKTFEK
FVSLDGNVSW PMIVRERVYF LSDHEGVGNL YSVDLKGKDL RRHTNFTDYY CRNASSDGKR
IVFQNAGDIY LYDPEKDSLT KLDINLPTDR KKKQPKFVNV MEYMNEAVVN GNYIALVSRG
KVFLMRPWDG PSVQLGKKQG VKYRQIQVLP NGDVIGVNDE DKLVILGKDG SEKVINKDFS
RIERVKVSPD GKKVLLSNNK LELWVYEIDN DNARLIDKSE YDLILEFDWH PNAEWFAYAF
PEGYYTQSIK LAHIDGKVVR ITTPYGYDFS PSFDPDGRYL YFLAARHLDP TNDKVIFNLS
FQRVVKPYLV VLGNYYSPFN QPLDEANSND KNVIIEGIED RVVPFPIEEE NYVQIAGAKN
NKIFLFSYPI RGLRSQTGDV FGRLEVYDLE NKAKELYADN VSSFSLSSDK SKILLILKDS
LRLFDVNVKP DFNSTGRKGG VIDLSRVKVY VEPEKEWRQM LRETWKLMKQ NYWNEERLKN
WDSILPKYER LLDRISTRFE LSDVIQEMQG ETRTSHSYET AYDYDTPEPL SVGGLGAEFE
YDESNKCYKI TKIYVGDSTN ENERSPLRDP GVQLNVGDCI KNIDGEDANG NIYSHLINKD
QVILDVITAD GKNKRVTVKV LKDERFLIYR YWVEKNREYV HEKSKGRLGY IHIPDMMYQG
FAEFYRLFMS EFHREGLVVD VRFNRGGFVS GLLLEKLLLK RVGYDYPRNG KPIPMPYFSS
PKVLVGITNE HAGSDGDIFS FLFKKYKLGV LIGRRTWGGV VGIRPRYRLV DKTYISQPEF
AVNFEDVGFG IENYGVDPDI VVEIKPDDYV NNRDTQLDTA IELALKQL
