ID A0A086N599_9ACTN Unreviewed; 360 AA.
AC A0A086N599;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Streptogrisin {ECO:0000313|EMBL:KFG76317.1};
GN ORFNames=FM21_09480 {ECO:0000313|EMBL:KFG76317.1};
OS Streptomyces mutabilis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=67332 {ECO:0000313|EMBL:KFG76317.1, ECO:0000313|Proteomes:UP000029095};
RN [1] {ECO:0000313|EMBL:KFG76317.1, ECO:0000313|Proteomes:UP000029095}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TRM45540 {ECO:0000313|EMBL:KFG76317.1,
RC ECO:0000313|Proteomes:UP000029095};
RA Luo X., Zhang L.;
RT "Complete genome sequence of the Streptomyces mutabilis TRM45540.";
RL Submitted (MAY-2014) 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:KFG76317.1}.
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DR EMBL; JNFQ01000001; KFG76317.1; -; Genomic_DNA.
DR RefSeq; WP_043374674.1; NZ_KN039946.1.
DR AlphaFoldDB; A0A086N599; -.
DR STRING; 1915400.FM21_09480; -.
DR HOGENOM; CLU_030648_0_1_11; -.
DR Proteomes; UP000029095; 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; IPR010916; TonB_box_CS.
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; PS00430; TONB_DEPENDENT_REC_1; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..360
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001811697"
FT DOMAIN 102..157
FT /note="Peptidase S1A alpha-lytic prodomain"
FT /evidence="ECO:0000259|Pfam:PF02983"
FT DOMAIN 198..352
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|Pfam:PF00089"
FT ACT_SITE 206
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-1"
FT ACT_SITE 234
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-1"
FT ACT_SITE 316
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-1"
FT DISULFID 187..207
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-2"
FT DISULFID 310..337
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-2"
SQ SEQUENCE 360 AA; 36644 MW; FEFA241F9D3BFAC2 CRC64;
MKHRRIPRRR AAVVGAGITA LVAAGVTFQS ANASEAPEAS APETLSVTAA GKLASTLLGD
LGADAAGTYY DARAKSLVVN VLDENAAQTV EEAGAKARIV ENSLADLKSA RTTLTEDATI
PGTSWATDPT TNKVVVTADR TVSKAEWARL AEVVDGLGAK AELKRTEGEY KPFVAGGDAI
TGDGGRCSLG FNVTKGGEPY FLTAGHCTEG VTTWSDSSGN VIGENEASSF PGDDYGLVKY
TAEVDHPSEV NLYDGSFQAI SGVAEATVGM EVTRSGSTTQ VHSGTVTGLD ATVNYGNGDI
VNGLIRTDVC AEPGDSGGSL FSGDQAVGLT SGGSGDCTSG GETFFQPVTE ALSVTGTQIG
//
