ID F8JWY6_STREN Unreviewed; 353 AA.
AC F8JWY6; G8X1X6;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Streptogrisin-B {ECO:0000313|EMBL:AEW93300.1};
GN OrderedLocusNames=SCATT_09290 {ECO:0000313|EMBL:AEW93300.1};
OS Streptantibioticus cattleyicolor (strain ATCC 35852 / DSM 46488 / JCM 4925
OS / NBRC 14057 / NRRL 8057) (Streptomyces cattleya).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptantibioticus.
OX NCBI_TaxID=1003195 {ECO:0000313|EMBL:AEW93300.1, ECO:0000313|Proteomes:UP000007842};
RN [1] {ECO:0000313|Proteomes:UP000007842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35852 / DSM 46488 / JCM 4925 / NBRC 14057 / NRRL 8057
RC {ECO:0000313|Proteomes:UP000007842};
RA Ou H.-Y., Li P., Zhao C., O'Hagan D., Deng Z.;
RT "Complete genome sequence of Streptomyces cattleya strain DSM 46488.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
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DR EMBL; CP003219; AEW93300.1; -; Genomic_DNA.
DR RefSeq; WP_014141698.1; NC_017586.1.
DR AlphaFoldDB; F8JWY6; -.
DR STRING; 1003195.SCATT_09290; -.
DR KEGG; scy:SCATT_09290; -.
DR PATRIC; fig|1003195.11.peg.2518; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_030648_1_0_11; -.
DR OrthoDB; 8781117at2; -.
DR Proteomes; UP000007842; Chromosome.
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:InterPro.
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 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR001134-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000007842};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..353
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039505111"
FT DOMAIN 98..151
FT /note="Peptidase S1A alpha-lytic prodomain"
FT /evidence="ECO:0000259|Pfam:PF02983"
FT DOMAIN 192..344
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|Pfam:PF00089"
FT ACT_SITE 201
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-1"
FT ACT_SITE 231
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-1"
FT ACT_SITE 309
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-1"
FT DISULFID 182..202
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-2"
FT DISULFID 303..330
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-2"
SQ SEQUENCE 353 AA; 35404 MW; 4FDA6A20A924F293 CRC64;
MRIKRVTPPA ATGRRLRLLA VACGLVAATA VSLPAADAAP AARATPDAAA GVARTLGAAA
TAGTYYDAAA KATVVNVTSD AAARQVRAAG AVPRLVKYSS AQLDTAGAAV QRLGIAGTAW
AQDPRTDQLV VSADHGVPAG RYAALRTTAA RYGDAVRVQR VAGRFRELLS GGDAIYGGGY
RCSLGFNVHS GGTYYFLTAG HCGKAVSTWY TSSGQSTVIG PTTGYTFPGN DYALVRYSNT
SLPHPSAVGG QTITGAGNAY VGESVTRRGS TTGVHSGTVT GLNATVNYGS DGIVRGLIQT
NVCAEPGDSG GSLYSGSTAV GLTSGGSGDC TSGGTTFFQP VTAALSHFGV SLP
//
