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   08-NOV-2023, entry version 147.
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; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; 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   GeneID; 6210254; -.
DR   OMA; IYASSWR; -.
DR   OrthoDB; 8781117at2; -.
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   CDD; cd21112; alphaLP-like; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 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; Trypsin-like serine proteases; 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
//