ID A0A0M8Z0G7_9ACTN Unreviewed; 378 AA.
AC A0A0M8Z0G7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Protease {ECO:0000313|EMBL:KOX47390.1};
DE Flags: Fragment;
GN ORFNames=ADL09_14740 {ECO:0000313|EMBL:KOX47390.1};
OS Streptomyces sp. NRRL F-7442.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519498 {ECO:0000313|EMBL:KOX47390.1, ECO:0000313|Proteomes:UP000037772};
RN [1] {ECO:0000313|EMBL:KOX47390.1, ECO:0000313|Proteomes:UP000037772}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL F-7442 {ECO:0000313|EMBL:KOX47390.1,
RC ECO:0000313|Proteomes:UP000037772};
RA Noorani M.;
RL Submitted (JUL-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:KOX47390.1}.
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DR EMBL; LGEH01000141; KOX47390.1; -; Genomic_DNA.
DR RefSeq; WP_053663776.1; NZ_LGEH01000141.1.
DR AlphaFoldDB; A0A0M8Z0G7; -.
DR PATRIC; fig|1519498.3.peg.3055; -.
DR OrthoDB; 8781117at2; -.
DR Proteomes; UP000037772; 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:UniProtKB-KW.
DR CDD; cd21112; alphaLP-like; 1.
DR Gene3D; 3.30.300.50; -; 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; IPR035070; Streptogrisin_prodomain.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR43019:SF23; PROTEASE DO-LIKE 5, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43019; SERINE ENDOPROTEASE DEGS; 1.
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; PS51318; TAT; 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 Hydrolase {ECO:0000313|EMBL:KOX47390.1};
KW Protease {ECO:0000313|EMBL:KOX47390.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..378
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005829956"
FT DOMAIN 109..163
FT /note="Peptidase S1A alpha-lytic prodomain"
FT /evidence="ECO:0000259|Pfam:PF02983"
FT DOMAIN 210..365
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|Pfam:PF00089"
FT ACT_SITE 215
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-1"
FT ACT_SITE 245
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-1"
FT ACT_SITE 326
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-1"
FT DISULFID 195..216
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-2"
FT DISULFID 320..348
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-2"
FT NON_TER 378
FT /evidence="ECO:0000313|EMBL:KOX47390.1"
SQ SEQUENCE 378 AA; 37975 MW; 46891FE673526DF2 CRC64;
MSHKRIPKRR AAMAAGGVIA LGAAALLLPH ANAAQDGGSP DEAAAPRTLK AADAPDLAAR
LAGLLGDTFA GSYYDSGARR LVVNVVPGDD DEAVVRAKRA GAEVREVDNS MGELRSGART
LKSEASIPGT SWAVDPRTNR ILVTADSTVT GDRWDRLEST VEGLGSGMAT IRRSAGTFTT
FVSGGDAVFG GGARCSLGFN VTAGDGSPAF LTAGHCGVAA AQWSDAQGGR PIATVDRAVF
PGQGDFALVR YDDPATDAPS EVNLGDQTLP ISGAAEATVG QEVFRMGSTT GLADGRVLGL
DATVNYPEGT VTGLIQTDVC AEPGDSGGSL FTRDGLAIGL TSGGSGDCTT GGETFFQPVT
TALNAVGATL GDEGAGAG
//
