PRTB_STRGR
ID PRTB_STRGR Reviewed; 299 AA.
AC P00777;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Streptogrisin-B;
DE EC=3.4.21.81;
DE AltName: Full=Pronase enzyme B;
DE AltName: Full=SGPB;
DE AltName: Full=Serine protease B;
DE Flags: Precursor;
GN Name=sprB;
OS Streptomyces griseus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3112129; DOI=10.1128/jb.169.8.3778-3784.1987;
RA Henderson G., Krygsman P., Liu C.J., Davey C.C., Malek L.T.;
RT "Characterization and structure of genes for proteases A and B from
RT Streptomyces griseus.";
RL J. Bacteriol. 169:3778-3784(1987).
RN [2]
RP PROTEIN SEQUENCE OF 115-299.
RC STRAIN=K-1;
RX PubMed=4218101; DOI=10.1016/s0006-291x(74)80396-7;
RA Jurasek L., Carpenter M.R., Smillie L.B., Gertler A., Levy S.,
RA Ericsson L.H.;
RT "Amino acid sequence of Streptomyces griseus protease B, A MAJOR COMPONENT
RT OF Pronase.";
RL Biochem. Biophys. Res. Commun. 61:1095-1100(1974).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND SEQUENCE REVISION.
RX PubMed=1186854; DOI=10.1038/257758a0;
RA Delbaere L.T.J., Hutcheon W.L.B., James M.N.G., Thiessen W.E.;
RT "Tertiary structural differences between microbial serine proteases and
RT pancreatic serine enzymes.";
RL Nature 257:758-763(1975).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND SEQUENCE REVISION.
RX PubMed=110426; DOI=10.1139/o79-017;
RA Delbaere L.T.J., Brayer G.D., James M.N.G.;
RT "The 2.8-A resolution structure of Streptomyces griseus protease B and its
RT homology with alpha-chymotrypsin and Streptomyces griseus protease A.";
RL Can. J. Biochem. 57:135-144(1979).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=2494344; DOI=10.1016/0022-2836(89)90376-8;
RA Greenblatt H.M., Ryan C.A., James M.N.G.;
RT "Structure of the complex of Streptomyces griseus proteinase B and
RT polypeptide chymotrypsin inhibitor-1 from Russet Burbank potato tubers at
RT 2.1-A resolution.";
RL J. Mol. Biol. 205:201-228(1989).
RN [6]
RP ACTIVE SITE.
RX PubMed=4212092; DOI=10.1016/0014-5793(74)81110-5;
RA Gertler A.;
RT "Inhibition of Streptomyces griseus protease B by peptide chloromethyl
RT ketones: partial mapping of the binding site and identification of the
RT reactive residue.";
RL FEBS Lett. 43:81-85(1974).
RN [7]
RP ACTIVE SITE.
RX PubMed=5636372; DOI=10.1016/0005-2744(68)90107-1;
RA Wahlby S., Engstrom L.;
RT "Studies on Streptomyces griseus protease. II. The amino acid sequence
RT around the reactive serine residue of DFP-sensitive components with
RT esterase activity.";
RL Biochim. Biophys. Acta 151:402-408(1968).
CC -!- FUNCTION: Has a primary specificity for large aliphatic or aromatic
CC amino acids.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins with trypsin-like specificity.;
CC EC=3.4.21.81;
CC -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000305}.
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DR EMBL; M17104; AAA26819.1; -; Genomic_DNA.
DR PIR; B26974; PRSMBG.
DR RefSeq; WP_003970068.1; NZ_UAVD01000020.1.
DR PDB; 1CSO; X-ray; 1.90 A; E=115-299.
DR PDB; 1CT0; X-ray; 1.80 A; E=115-299.
DR PDB; 1CT2; X-ray; 1.65 A; E=115-299.
DR PDB; 1CT4; X-ray; 1.60 A; E=115-299.
DR PDB; 1DS2; X-ray; 1.70 A; E=115-299.
DR PDB; 1SGD; X-ray; 1.80 A; E=115-299.
DR PDB; 1SGE; X-ray; 1.80 A; E=115-299.
DR PDB; 1SGN; X-ray; 1.80 A; E=115-299.
DR PDB; 1SGP; X-ray; 1.40 A; E=115-299.
DR PDB; 1SGQ; X-ray; 1.90 A; E=115-299.
DR PDB; 1SGR; X-ray; 1.80 A; E=115-299.
DR PDB; 1SGY; X-ray; 1.80 A; E=115-299.
DR PDB; 2GKV; X-ray; 1.70 A; E=115-299.
DR PDB; 2NU0; X-ray; 1.95 A; E=115-299.
DR PDB; 2NU1; X-ray; 1.80 A; E=115-299.
DR PDB; 2NU2; X-ray; 1.65 A; E=115-299.
DR PDB; 2NU3; X-ray; 1.80 A; E=115-299.
DR PDB; 2NU4; X-ray; 1.75 A; E=115-299.
DR PDB; 2QA9; X-ray; 1.18 A; E=115-299.
DR PDB; 2QAA; X-ray; 1.23 A; A/B=115-299.
DR PDB; 2SGD; X-ray; 1.80 A; E=115-299.
DR PDB; 2SGE; X-ray; 1.80 A; E=115-299.
DR PDB; 2SGF; X-ray; 1.75 A; E=115-299.
DR PDB; 2SGP; X-ray; 1.80 A; E=115-299.
DR PDB; 2SGQ; X-ray; 1.80 A; E=115-299.
DR PDB; 3SGB; X-ray; 1.80 A; E=115-299.
DR PDB; 3SGQ; X-ray; 1.80 A; E=115-299.
DR PDB; 4SGB; X-ray; 2.10 A; E=115-299.
DR PDBsum; 1CSO; -.
DR PDBsum; 1CT0; -.
DR PDBsum; 1CT2; -.
DR PDBsum; 1CT4; -.
DR PDBsum; 1DS2; -.
DR PDBsum; 1SGD; -.
DR PDBsum; 1SGE; -.
DR PDBsum; 1SGN; -.
DR PDBsum; 1SGP; -.
DR PDBsum; 1SGQ; -.
DR PDBsum; 1SGR; -.
DR PDBsum; 1SGY; -.
DR PDBsum; 2GKV; -.
DR PDBsum; 2NU0; -.
DR PDBsum; 2NU1; -.
DR PDBsum; 2NU2; -.
DR PDBsum; 2NU3; -.
DR PDBsum; 2NU4; -.
DR PDBsum; 2QA9; -.
DR PDBsum; 2QAA; -.
DR PDBsum; 2SGD; -.
DR PDBsum; 2SGE; -.
DR PDBsum; 2SGF; -.
DR PDBsum; 2SGP; -.
DR PDBsum; 2SGQ; -.
DR PDBsum; 3SGB; -.
DR PDBsum; 3SGQ; -.
DR PDBsum; 4SGB; -.
DR AlphaFoldDB; P00777; -.
DR SMR; P00777; -.
DR MINT; P00777; -.
DR Allergome; 3640; Str g Pronase.
DR MEROPS; S01.262; -.
DR PRIDE; P00777; -.
DR GeneID; 6210254; -.
DR OMA; IYASSWR; -.
DR BRENDA; 3.4.21.81; 6035.
DR EvolutionaryTrace; P00777; -.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR004236; Pept_S1_alpha_lytic.
DR InterPro; IPR001316; Pept_S1A_streptogrisin.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF02983; Pro_Al_protease; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001134; Streptogrisin; 1.
DR PRINTS; PR00861; ALYTICPTASE.
DR SUPFAM; SSF50494; SSF50494; 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..38
FT PROPEP 39..114
FT /evidence="ECO:0000269|PubMed:4218101"
FT /id="PRO_0000026911"
FT CHAIN 115..299
FT /note="Streptogrisin-B"
FT /id="PRO_0000026912"
FT ACT_SITE 147
FT /note="Charge relay system"
FT ACT_SITE 177
FT /note="Charge relay system"
FT ACT_SITE 255
FT /note="Charge relay system"
FT DISULFID 128..148
FT DISULFID 249..276
FT CONFLICT 153
FT /note="T -> TG (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="A -> V (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="V -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:2QA9"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:2QA9"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:2QA9"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:2QA9"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:2QA9"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:2QA9"
FT STRAND 163..172
FT /evidence="ECO:0007829|PDB:2QA9"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:2QA9"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:2QA9"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:2QA9"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:2QAA"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:2QA9"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:2QA9"
FT STRAND 219..233
FT /evidence="ECO:0007829|PDB:2QA9"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:2SGP"
FT STRAND 239..247
FT /evidence="ECO:0007829|PDB:2QA9"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:2QA9"
FT STRAND 264..275
FT /evidence="ECO:0007829|PDB:2QA9"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:2QA9"
FT STRAND 279..286
FT /evidence="ECO:0007829|PDB:2QA9"
FT HELIX 287..294
FT /evidence="ECO:0007829|PDB:2QA9"
SQ SEQUENCE 299 AA; 30554 MW; 7A272C9516C7B9B1 CRC64;
MRIKRTSNRS NAARRVRTTA VLAGLAAVAA LAVPTANAET PRTFSANQLT AASDAVLGAD
IAGTAWNIDP QSKRLVVTVD STVSKAEINQ IKKSAGANAD ALRIERTPGK FTKLISGGDA
IYSSTGRCSL GFNVRSGSTY YFLTAGHCTD GATTWWANSA RTTVLGTTSG SSFPNNDYGI
VRYTNTTIPK DGTVGGQDIT SAANATVGMA VTRRGSTTGT HSGSVTALNA TVNYGGGDVV
YGMIRTNVCA EPGDSGGPLY SGTRAIGLTS GGSGNCSSGG TTFFQPVTEA LSAYGVSVY
