ID A0A370B501_9ACTN Unreviewed; 299 AA.
AC A0A370B501;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=S1 family peptidase {ECO:0000313|EMBL:RDG35732.1};
GN ORFNames=DVH02_23640 {ECO:0000313|EMBL:RDG35732.1};
OS Streptomyces corynorhini.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2282652 {ECO:0000313|EMBL:RDG35732.1, ECO:0000313|Proteomes:UP000253741};
RN [1] {ECO:0000313|EMBL:RDG35732.1, ECO:0000313|Proteomes:UP000253741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AC230 {ECO:0000313|EMBL:RDG35732.1,
RC ECO:0000313|Proteomes:UP000253741};
RA Dunlap C.;
RT "Streptomyces species from bats.";
RL Submitted (JUL-2018) 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:RDG35732.1}.
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DR EMBL; QQNA01000200; RDG35732.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370B501; -.
DR OrthoDB; 8781117at2; -.
DR Proteomes; UP000253741; 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: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 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 Reference proteome {ECO:0000313|Proteomes:UP000253741};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..38
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 39..299
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017018059"
FT DOMAIN 44..98
FT /note="Peptidase S1A alpha-lytic prodomain"
FT /evidence="ECO:0000259|Pfam:PF02983"
FT DOMAIN 115..290
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|Pfam:PF00089"
FT ACT_SITE 147
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-1"
FT ACT_SITE 177
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..148
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-2"
FT DISULFID 249..276
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-2"
SQ SEQUENCE 299 AA; 29706 MW; 5741B1C969ED35F3 CRC64;
MRIKRTNPLG GVARRARLIA VTTGLAAAAA LAIPTANAAQ ATTFSANQLS AASEAVLQAD
VAGTAWAVDP ATNALVVQAD STVTQAEIAS LEQAAGTNAG ALRVERTPGT LSKLISGGDA
VYTSSWRCSA GFNVRSGSTY YFLTAGHCTE GLPAWYTSSS GATSIGPSAG SSFPGNDYGI
VRYSNTALAH PGTVGSVTIT GSTNATNGLS VTRRGSTTGI HSGTVTGLNY TVNYGSGDIV
SGLIRTNVCA EPGDSGGPLY SGSLAVGLTS GGSGDCTSGG TTYFQPVTAA LSAYGVSLV
//
