TRYP_STRGR
ID TRYP_STRGR Reviewed; 259 AA.
AC P00775;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Trypsin;
DE EC=3.4.21.4;
DE AltName: Full=SGT;
DE Flags: Precursor;
GN Name=sprT;
OS Streptomyces griseus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10137 / DSM 40855 / NBRC 3430 / NCIMB 8232 / NCTC 6961 / IMRU
RC 3496;
RX PubMed=1755852; DOI=10.1016/0006-291x(91)91248-b;
RA Kim J.C., Cha S.H., Jeong S.T., Oh S.K., Byun S.M.;
RT "Molecular cloning and nucleotide sequence of Streptomyces griseus trypsin
RT gene.";
RL Biochem. Biophys. Res. Commun. 181:707-713(1991).
RN [2]
RP PROTEIN SEQUENCE OF 37-259.
RX PubMed=804314; DOI=10.1021/bi00677a011;
RA Olafson R.W., Jurasek L., Carpenter M.R., Smillie L.B.;
RT "Amino acid sequence of Streptomyces griseus trypsin. Cyanogen bromide
RT fragments and complete sequence.";
RL Biochemistry 14:1168-1177(1975).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=3135412; DOI=10.1016/0022-2836(88)90541-4;
RA Read R.J., James M.N.G.;
RT "Refined crystal structure of Streptomyces griseus trypsin at 1.7-A
RT resolution.";
RL J. Mol. Biol. 200:523-551(1988).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4;
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; M64471; AAA26820.1; ALT_SEQ; Genomic_DNA.
DR PIR; JQ1302; TRSMG.
DR RefSeq; WP_003965150.1; NZ_UAVD01000024.1.
DR PDB; 1OS8; X-ray; 1.55 A; A=37-259.
DR PDB; 1OSS; X-ray; 1.93 A; A=37-259.
DR PDB; 1SGT; X-ray; 1.70 A; A=37-259.
DR PDB; 2FMJ; X-ray; 1.65 A; A=37-259.
DR PDB; 3BEU; X-ray; 1.05 A; A/B=37-259.
DR PDB; 3I77; X-ray; 2.10 A; A=37-259.
DR PDB; 3I78; X-ray; 3.00 A; A=37-259.
DR PDBsum; 1OS8; -.
DR PDBsum; 1OSS; -.
DR PDBsum; 1SGT; -.
DR PDBsum; 2FMJ; -.
DR PDBsum; 3BEU; -.
DR PDBsum; 3I77; -.
DR PDBsum; 3I78; -.
DR AlphaFoldDB; P00775; -.
DR SMR; P00775; -.
DR DrugBank; DB03127; Benzamidine.
DR MEROPS; S01.101; -.
DR GeneID; 6211046; -.
DR OMA; YNGVHVC; -.
DR BRENDA; 3.4.21.4; 6035.
DR EvolutionaryTrace; P00775; -.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Protease; Serine protease; Signal; Zymogen.
FT SIGNAL 1..32
FT PROPEP 33..36
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:804314"
FT /id="PRO_0000028307"
FT CHAIN 37..259
FT /note="Trypsin"
FT /id="PRO_0000028308"
FT DOMAIN 37..257
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 73
FT /note="Charge relay system"
FT ACT_SITE 118
FT /note="Charge relay system"
FT ACT_SITE 208
FT /note="Charge relay system"
FT SITE 202
FT /note="Required for specificity"
FT DISULFID 58..74
FT DISULFID 177..192
FT DISULFID 204..233
FT CONFLICT 95..96
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:3BEU"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:3BEU"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:3BEU"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:3BEU"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:3BEU"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:3BEU"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:3BEU"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:3BEU"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:3I78"
FT STRAND 99..108
FT /evidence="ECO:0007829|PDB:3BEU"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:1OS8"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:3BEU"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:1SGT"
FT STRAND 142..152
FT /evidence="ECO:0007829|PDB:3BEU"
FT STRAND 165..172
FT /evidence="ECO:0007829|PDB:3BEU"
FT HELIX 174..180
FT /evidence="ECO:0007829|PDB:3BEU"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:1OS8"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:3BEU"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:3BEU"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:3BEU"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:3BEU"
FT STRAND 221..234
FT /evidence="ECO:0007829|PDB:3BEU"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:3BEU"
FT HELIX 245..256
FT /evidence="ECO:0007829|PDB:3BEU"
SQ SEQUENCE 259 AA; 26776 MW; 050233AFF1F64823 CRC64;
MKHFLRALKR CSVAVATVAI AVVGLQPVTA SAAPNPVVGG TRAAQGEFPF MVRLSMGCGG
ALYAQDIVLT AAHCVSGSGN NTSITATGGV VDLQSSSAVK VRSTKVLQAP GYNGTGKDWA
LIKLAQPINQ PTLKIATTTA YNQGTFTVAG WGANREGGSQ QRYLLKANVP FVSDAACRSA
YGNELVANEE ICAGYPDTGG VDTCQGDSGG PMFRKDNADE WIQVGIVSWG YGCARPGYPG
VYTEVSTFAS AIASAARTL
