PRTA_STRGR
ID PRTA_STRGR Reviewed; 297 AA.
AC P00776;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Streptogrisin-A;
DE EC=3.4.21.80;
DE AltName: Full=Pronase enzyme A;
DE AltName: Full=SGPA;
DE AltName: Full=Serine protease A;
DE Flags: Precursor;
GN Name=sprA;
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 116-297.
RX PubMed=4214713; DOI=10.1016/0014-5793(74)80412-6;
RA Johnson P., Smillie L.B.;
RT "The amino acid sequence and predicted structure of Streptomyces griseus
RT protease A.";
RL FEBS Lett. 47:1-6(1974).
RN [3]
RP SEQUENCE REVISION TO 249.
RA Apostol I., Smillie L.B., Laskowski M. Jr.;
RL Submitted (JUL-1996) to UniProtKB.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=119870; DOI=10.1016/0022-2836(79)90486-8;
RA Sielecki A.R., Hendrickson W.A., Broughton C.G., Delbaere L.T.J.,
RA Brayer G.D., James M.N.G.;
RT "Protein structure refinement: Streptomyces griseus serine protease A at
RT 1.8-A resolution.";
RL J. Mol. Biol. 134:781-804(1979).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=101674; DOI=10.1016/0022-2836(78)90159-6;
RA Brayer G.D., Delbaere L.T.J., James M.N.G.;
RT "Molecular structure of crystalline Streptomyces griseus protease A at 2.8-
RT A resolution. II. Molecular conformation, comparison with alpha-
RT chymotrypsin and active-site geometry.";
RL J. Mol. Biol. 124:261-283(1978).
CC -!- FUNCTION: Has a primary specificity for large aliphatic or aromatic
CC amino acids.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins with specificity similar to
CC chymotrypsin.; EC=3.4.21.80;
CC -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000305}.
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DR EMBL; M17103; AAA26818.1; -; Genomic_DNA.
DR PIR; A26974; PRSMAG.
DR RefSeq; WP_003964236.1; NZ_UAVD01000006.1.
DR PDB; 1SGC; X-ray; 1.80 A; A=117-297.
DR PDB; 2SGA; X-ray; 1.50 A; A=117-297.
DR PDB; 3SGA; X-ray; 1.80 A; E=117-297.
DR PDB; 4SGA; X-ray; 1.80 A; E=117-297.
DR PDB; 5SGA; X-ray; 1.80 A; E=117-297.
DR PDBsum; 1SGC; -.
DR PDBsum; 2SGA; -.
DR PDBsum; 3SGA; -.
DR PDBsum; 4SGA; -.
DR PDBsum; 5SGA; -.
DR AlphaFoldDB; P00776; -.
DR SMR; P00776; -.
DR Allergome; 3640; Str g Pronase.
DR MEROPS; S01.261; -.
DR GeneID; 6210956; -.
DR OMA; WYTEAST; -.
DR EvolutionaryTrace; P00776; -.
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 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..115
FT /evidence="ECO:0000269|PubMed:4214713"
FT /id="PRO_0000026909"
FT CHAIN 116..297
FT /note="Streptogrisin-A"
FT /id="PRO_0000026910"
FT ACT_SITE 149
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 171
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 253
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT DISULFID 130..150
FT /evidence="ECO:0000269|PubMed:101674"
FT DISULFID 247..274
FT /evidence="ECO:0000269|PubMed:101674"
FT CONFLICT 151
FT /note="T -> TS (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:2SGA"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:2SGA"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:2SGA"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:2SGA"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:2SGA"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:2SGA"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:2SGA"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:2SGA"
FT STRAND 172..178
FT /evidence="ECO:0007829|PDB:2SGA"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:2SGA"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:2SGA"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:2SGA"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:2SGA"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:2SGA"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:2SGA"
FT STRAND 217..231
FT /evidence="ECO:0007829|PDB:2SGA"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:2SGA"
FT STRAND 237..245
FT /evidence="ECO:0007829|PDB:2SGA"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:2SGA"
FT STRAND 262..273
FT /evidence="ECO:0007829|PDB:2SGA"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:2SGA"
FT STRAND 277..284
FT /evidence="ECO:0007829|PDB:2SGA"
FT HELIX 285..292
FT /evidence="ECO:0007829|PDB:2SGA"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:2SGA"
SQ SEQUENCE 297 AA; 29663 MW; 7F6CF04A81B4B3C9 CRC64;
MTFKRFSPLS STSRYARLLA VASGLVAAAA LATPSAVAAP EAESKATVSQ LADASSAILA
ADVAGTAWYT EASTGKIVLT ADSTVSKAEL AKVSNALAGS KAKLTVKRAE GKFTPLIAGG
EAITTGGSRC SLGFNVSVNG VAHALTAGHC TNISASWSIG TRTGTSFPNN DYGIIRHSNP
AAADGRVYLY NGSYQDITTA GNAFVGQAVQ RSGSTTGLRS GSVTGLNATV NYGSSGIVYG
MIQTNVCAEP GDSGGSLFAG STALGLTSGG SGNCRTGGTT FYQPVTEALS AYGATVL
