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Database: UniProt
Entry: A0A191UVH7_9ACTN
LinkDB: A0A191UVH7_9ACTN
Original site: A0A191UVH7_9ACTN 
ID   A0A191UVH7_9ACTN        Unreviewed;       300 AA.
AC   A0A191UVH7;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=S1 family peptidase {ECO:0000313|EMBL:RDD88659.1};
DE   SubName: Full=Serine protease {ECO:0000313|EMBL:GGR86941.1};
DE   SubName: Full=Streptogrisin {ECO:0000313|EMBL:ANJ06736.1};
GN   ORFNames=DVZ84_11765 {ECO:0000313|EMBL:RDD88659.1}, GCM10010220_44240
GN   {ECO:0000313|EMBL:GGR86941.1}, Spa2297_06855
GN   {ECO:0000313|EMBL:ANJ06736.1};
OS   Streptomyces parvulus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=146923 {ECO:0000313|EMBL:ANJ06736.1, ECO:0000313|Proteomes:UP000078468};
RN   [1] {ECO:0000313|EMBL:ANJ06736.1, ECO:0000313|Proteomes:UP000078468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2297 {ECO:0000313|EMBL:ANJ06736.1,
RC   ECO:0000313|Proteomes:UP000078468};
RA   Nishizawa T., Miura T., Harada C., Guo Y., Narisawa K., Ohta H.,
RA   Takahashi H., Shirai M.;
RT   "Non-Contiguous Finished Genome Sequence of Streptomyces parvulus 2297
RT   Integrated Site-Specifically with Actinophage R4.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:RDD88659.1, ECO:0000313|Proteomes:UP000253742}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2297 {ECO:0000313|EMBL:RDD88659.1,
RC   ECO:0000313|Proteomes:UP000253742};
RA   Hu D.;
RT   "Genome guided investigation of antibiotics producing actinomycetales
RT   strain isolated from a Macau mangrove ecosystem.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:GGR86941.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JCM 4068 {ECO:0000313|EMBL:GGR86941.1};
RX   PubMed=30832757;
RA   Wu L., Ma J.;
RT   "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT   project: providing services to taxonomists for standard genome sequencing
RT   and annotation.";
RL   Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN   [4] {ECO:0000313|EMBL:GGR86941.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JCM 4068 {ECO:0000313|EMBL:GGR86941.1};
RA   Sun Q., Ohkuma M.;
RL   Submitted (DEC-2022) 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; CP015866; ANJ06736.1; -; Genomic_DNA.
DR   EMBL; BMRX01000010; GGR86941.1; -; Genomic_DNA.
DR   EMBL; QQBH01000006; RDD88659.1; -; Genomic_DNA.
DR   RefSeq; WP_064727121.1; NZ_QQBH01000006.1.
DR   STRING; 146923.Spa2297_06855; -.
DR   KEGG; spav:Spa2297_06855; -.
DR   OrthoDB; 8781117at2; -.
DR   Proteomes; UP000078468; Chromosome.
DR   Proteomes; UP000253742; Unassembled WGS sequence.
DR   Proteomes; UP000645274; 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; 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:GGR86941.1};
KW   Protease {ECO:0000313|EMBL:GGR86941.1}; 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_5041083672"
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;  29863 MW;  C108332C95B857F3 CRC64;
     MRIKRTTPRS GITRRTRLIA VSTGLVAAAA VAIPSATAAP APVAFSAAEL SSASGAVLKA
     DVPGTAWAVD AKSGRVLLTV DSTVSQAEIA KIKEQAGDKA GALTVKRTPG TFNKLIQGGD
     AIYASSWRCS LGFNVRASNG TEYFLTAGHC TDGAGAWRSS SGGTVIGQTA GSSFPGNDYG
     IVQYTGSVSR PGTANGVDIT RAATPSVGTT VIRDGSTTGT HSGRVTALNA TVNYGGGDVV
     GGLIQTTVCA EPGDSGGSLY GSNGTAYGLT SGGSGNCSSG GTTFFQPVTE ALSAYGVSVY
//
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