ID A0A1Z1WLP5_9ACTN Unreviewed; 228 AA.
AC A0A1Z1WLP5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Streptogrisin-B {ECO:0000313|EMBL:ARX87377.1};
GN ORFNames=SMD44_06858 {ECO:0000313|EMBL:ARX87377.1};
OS Streptomyces alboflavus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=67267 {ECO:0000313|EMBL:ARX87377.1, ECO:0000313|Proteomes:UP000195880};
RN [1] {ECO:0000313|EMBL:ARX87377.1, ECO:0000313|Proteomes:UP000195880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MDJK44 {ECO:0000313|EMBL:ARX87377.1,
RC ECO:0000313|Proteomes:UP000195880};
RA Wang Y., Du B., Ding Y., Liu H., Hou Q., Liu K., Wang C., Yao L.;
RT "Streptomyces alboflavus Genome sequencing and assembly.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
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DR EMBL; CP021748; ARX87377.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z1WLP5; -.
DR STRING; 67267.GCA_000716675_03134; -.
DR KEGG; salf:SMD44_06858; -.
DR eggNOG; COG0265; Bacteria.
DR OrthoDB; 8781117at2; -.
DR Proteomes; UP000195880; Chromosome.
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; IPR001316; Pept_S1A_streptogrisin.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001254; Trypsin_dom.
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 Reference proteome {ECO:0000313|Proteomes:UP000195880};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..228
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012057280"
FT DOMAIN 115..215
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|Pfam:PF00089"
FT DISULFID 50..70
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-2"
FT DISULFID 138..148
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-2"
FT DISULFID 174..201
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-2"
SQ SEQUENCE 228 AA; 23459 MW; 5E42D9ED4F4CBA19 CRC64;
MRLRLIIAQL LCAALAALGL LAAPTATAAP ASAQTAIRGG DVLYSASGRC TVAFNVSNGT
RFYGIMGGHC GTVGTQWFAD PRLTVPVGVT ETVVFPRSSY ALVRYTNTNL TYPSEIRAGS
QIIRINRAPQ PVVGQQICRT GPTTGMHCGT IQSLNATVTF PEGTVYGLIR TNVCAEPGDA
GGPGFAGDAA LGIVVGGSGN CSSGGTTFFQ PLPPILNAHG LRVGYART
//
