ID A0A1R1SAL0_9ACTN Unreviewed; 393 AA.
AC A0A1R1SAL0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Putative secreted serine protease {ECO:0000313|EMBL:OMI35059.1};
GN ORFNames=SPAR_33241 {ECO:0000313|EMBL:OMI35059.1};
OS Streptomyces sparsogenes DSM 40356.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1331668 {ECO:0000313|EMBL:OMI35059.1, ECO:0000313|Proteomes:UP000186168};
RN [1] {ECO:0000313|EMBL:OMI35059.1, ECO:0000313|Proteomes:UP000186168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40356 {ECO:0000313|EMBL:OMI35059.1,
RC ECO:0000313|Proteomes:UP000186168};
RA Coyne S., Seebeck F.P.;
RT "Genome sequence of Streptomyces sparsogenes DSM 40356.";
RL Submitted (MAY-2013) 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:OMI35059.1}.
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DR EMBL; ASQP01000421; OMI35059.1; -; Genomic_DNA.
DR RefSeq; WP_076971867.1; NZ_ASQP01000421.1.
DR AlphaFoldDB; A0A1R1SAL0; -.
DR Proteomes; UP000186168; 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; -; 2.
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; IPR001254; Trypsin_dom.
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.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR001134-2};
KW Hydrolase {ECO:0000313|EMBL:OMI35059.1};
KW Protease {ECO:0000313|EMBL:OMI35059.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000186168};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..393
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038749784"
FT DOMAIN 122..181
FT /note="Peptidase S1A alpha-lytic prodomain"
FT /evidence="ECO:0000259|Pfam:PF02983"
FT DOMAIN 211..383
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|Pfam:PF00089"
FT ACT_SITE 237
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-1"
FT ACT_SITE 265
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-1"
FT ACT_SITE 347
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-1"
FT DISULFID 222..238
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-2"
FT DISULFID 305..315
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-2"
FT DISULFID 341..368
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-2"
SQ SEQUENCE 393 AA; 39929 MW; 55029DD8A10D31BD CRC64;
MRRTTGVRVG LSALLVLGAL TGAGAALSPA AAAPGPEPAA PSAKLVSALG RDLGLTDGQA
RERLGQEAAA MKLAPKAERA AGKAFGGSWF DADTGRLVVG VTNDERAAAV WATGATARIV
RHTAKELDAV KARLDEKAGK KAAPAGVSGW HVDPKAGDVV ISVRRGSERD AAVRAFVGEA
KGQAKRAGSV PVRVERAAAQ APATFAAGTV GGDPYYTGNV RCSIGFSVQG GFVTAGHCGR
AGASVNGWDG SYVGNFRGSS FPGNDYAYVS VGSGWWTVPV VLGWGTVPDA LVRGSAEAPV
GASICRSGST THWHCGTVLA KNETVNYSQG AVYQMTKTNV CAEPGDSGGS FISGDQAQGV
TSGGWGNCGS GGETWFQPVN EILSVYGLRL HTA
//
