ID A0A089X8V9_STRGA Unreviewed; 300 AA.
AC A0A089X8V9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Streptogrisin-B {ECO:0000313|EMBL:AIR97554.1};
DE EC=3.4.21.81 {ECO:0000313|EMBL:AIR97554.1};
GN Name=sprB {ECO:0000313|EMBL:AIR97554.1};
GN ORFNames=SGLAU_07695 {ECO:0000313|EMBL:AIR97554.1};
OS Streptomyces glaucescens.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1907 {ECO:0000313|EMBL:AIR97554.1, ECO:0000313|Proteomes:UP000029482};
RN [1] {ECO:0000313|Proteomes:UP000029482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40922 / GLA O {ECO:0000313|Proteomes:UP000029482};
RX PubMed=25499805; DOI=10.1016/j.jbiotec.2014.11.036;
RA Ortseifen V., Winkler A., Albersmeier A., Wendler S., Puhler A.,
RA Kalinowski J., Ruckert C.;
RT "Complete genome sequence of the actinobacterium Streptomyces glaucescens
RT GLA.O (DSM 40922) consisting of a linear chromosome and one linear
RT plasmid.";
RL J. Biotechnol. 194:81-83(2015).
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
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DR EMBL; CP009438; AIR97554.1; -; Genomic_DNA.
DR RefSeq; WP_043499489.1; NZ_CP009438.1.
DR AlphaFoldDB; A0A089X8V9; -.
DR STRING; 1907.SGLAU_07695; -.
DR KEGG; sgu:SGLAU_07695; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_030648_1_0_11; -.
DR OrthoDB; 8781117at2; -.
DR Proteomes; UP000029482; Chromosome.
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; 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:AIR97554.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029482};
KW 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_5001851516"
FT DOMAIN 44..98
FT /note="Peptidase S1A alpha-lytic prodomain"
FT /evidence="ECO:0000259|Pfam:PF02983"
FT DOMAIN 115..292
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|Pfam:PF00089"
FT ACT_SITE 148
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 128..149
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-2"
FT DISULFID 249..277
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-2"
SQ SEQUENCE 300 AA; 30147 MW; 130389883A38901B CRC64;
MRIKRTTPRS GISRRTRLTA VSAGLVAAAA IAIPSANASD TATFSAAELK SAGASVLEAD
VPGTAWAVDS KTNRLVVTVD STVSQAEIAK IKEQAGANAD ALTIKRTPGK FSKLIQGGDA
IYASSWRCSL GFNVQNSSGA QFFVTAGHCT DGAGTWYSNS GRTTVIGSTA GSSFPGNDYG
LVRYSGSVSR PGTANGVDIT RAATPAVGTT VIRDGSTTGT HSGRVTALNA TVNYGGGDVV
SGLIQTNVCA EPGDSGGPLY GSNGTAYGLT SGGSGNCSTG GTTFFQPVTE ALSAYGVSVY
//
