ID A0A124I5Y8_9ACTN Unreviewed; 299 AA.
AC A0A124I5Y8;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Streptogrisin {ECO:0000313|EMBL:KUN91440.1};
GN ORFNames=AQJ67_42510 {ECO:0000313|EMBL:KUN91440.1};
OS Streptomyces caeruleatus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=661399 {ECO:0000313|EMBL:KUN91440.1, ECO:0000313|Proteomes:UP000053429};
RN [1] {ECO:0000313|EMBL:KUN91440.1, ECO:0000313|Proteomes:UP000053429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-24802 {ECO:0000313|EMBL:KUN91440.1,
RC ECO:0000313|Proteomes:UP000053429};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces caeruleatus NRRL B-24802, type
RT strain for the species Streptomyces caeruleatus.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUN91440.1}.
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DR EMBL; LMWY01000065; KUN91440.1; -; Genomic_DNA.
DR RefSeq; WP_062725207.1; NZ_KQ948948.1.
DR AlphaFoldDB; A0A124I5Y8; -.
DR STRING; 661399.AQJ67_42510; -.
DR Proteomes; UP000053429; Unassembled WGS sequence.
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:UP000053429};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..37
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 38..299
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007174084"
FT DOMAIN 59..98
FT /note="Peptidase S1A alpha-lytic prodomain"
FT /evidence="ECO:0000259|Pfam:PF02983"
FT DOMAIN 118..291
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|Pfam:PF00089"
FT ACT_SITE 148
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-1"
FT ACT_SITE 178
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-1"
FT ACT_SITE 255
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-1"
FT DISULFID 129..149
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-2"
FT DISULFID 213..223
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-2"
FT DISULFID 249..276
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-2"
SQ SEQUENCE 299 AA; 30159 MW; 70FE461CB5ABA05A CRC64;
MSTVRRTPVR RRPRLVASVV SLVVAAALAM SDTSAAAAPT ADAGPSAASV AGAASAVESL
GVAGTAWTVD ERTGKLRVLA DSTVTDADLA RIRRATGAFP GVATLERLDG RLRTLLSGGD
GIYAAGRRCS AGVNVRSGST YYFVTAGHCT DTLPTWYTSS AMTTTVGATT GTSFPGNDFG
VVQYSNPSVP HPGTIGTVDV TGTATAYVSQ SVCRRGATTG VHCGVVTALN ATVTYPEGTV
SGLIRTNICA EPGDSGGPLY AGDKVVGILS GGSGNCASGG STYYQPIQEV LSAYGLSVY
//
