ID Q54392_STRLI Unreviewed; 300 AA.
AC Q54392;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 24-JAN-2024, entry version 89.
DE SubName: Full=Protease {ECO:0000313|EMBL:AAB49732.1};
GN Name=sal {ECO:0000313|EMBL:AAB49732.1};
OS Streptomyces lividans.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1916 {ECO:0000313|EMBL:AAB49732.1};
RN [1] {ECO:0000313|EMBL:AAB49732.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=66 {ECO:0000313|EMBL:AAB49732.1};
RX PubMed=8868236;
RA Binnie C., Liao L., Walczyk E., Malek L.T.;
RT "Isolation and characterization of a gene encoding a chymotrypsin-like
RT serine protease from Streptomyces lividans 66.";
RL Can. J. Microbiol. 42:284-288(1996).
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
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DR EMBL; L44109; AAB49732.1; -; Genomic_DNA.
DR PIR; T36768; T36768.
DR AlphaFoldDB; Q54392; -.
DR SMR; Q54392; -.
DR MEROPS; S01.263; -.
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; 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; IPR006311; TAT_signal.
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; 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:AAB49732.1};
KW Protease {ECO:0000313|EMBL:AAB49732.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..38
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 39..300
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004248748"
FT DOMAIN 45..99
FT /note="Peptidase S1A alpha-lytic prodomain"
FT /evidence="ECO:0000259|Pfam:PF02983"
FT DOMAIN 116..292
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|Pfam:PF00089"
FT ACT_SITE 149
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..150
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-2"
FT DISULFID 249..277
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-2"
SQ SEQUENCE 300 AA; 29977 MW; 92FC8D04FA2CA09A CRC64;
MRIKRTTPRS GITRRTRLIA VSTGLVAAAA VAIPSANAAP APATFSAAEL SSAGNAVLQA
DVPGTAWAVD SKSGRVLLTV DSTVSQAEIA KIKEQAGDKA DALTIKRTPG KFNKLIQGGD
AIYASSWRCS LGFNVRTSSG AEYFLTAGHC TDGAGAWRAS SGGTVIGQTA GSSFPGNDYG
IVQYTGSVSR PGTANGVDIT RAATPSVGTT VIRDGSTTGT HSGRVTALNA TVNYGGGDVV
GGLIQTTVCA EPGDSGGSLY GSNGTAYGLT SGGSGNCSSG GTTFFQPVTE ALSAYGVSVY
//
