ID A0A101U7X3_9ACTN Unreviewed; 400 AA.
AC A0A101U7X3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:KUO05724.1};
GN ORFNames=AQJ58_39645 {ECO:0000313|EMBL:KUO05724.1};
OS Streptomyces sp. DSM 15324.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1739111 {ECO:0000313|EMBL:KUO05724.1, ECO:0000313|Proteomes:UP000053431};
RN [1] {ECO:0000313|EMBL:KUO05724.1, ECO:0000313|Proteomes:UP000053431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15324 {ECO:0000313|EMBL:KUO05724.1,
RC ECO:0000313|Proteomes:UP000053431};
RA Ruckert C., Winkler A., Kalinowski J., Wink J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces sp. DSM 15324, isolated from soil.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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:KUO05724.1}.
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DR EMBL; LMXA01000061; KUO05724.1; -; Genomic_DNA.
DR RefSeq; WP_067259456.1; NZ_KQ949047.1.
DR AlphaFoldDB; A0A101U7X3; -.
DR OrthoDB; 9798386at2; -.
DR Proteomes; UP000053431; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000053431};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..400
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007107732"
FT DOMAIN 69..118
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 150..379
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 159
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 192
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 344
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 400 AA; 40189 MW; 8A9C72836C0D0436 CRC64;
MARTHIRRLR RAGSLTAVVT TMVLSAASPP AQAVPEGRVV GAGRPGSVGG SYLVTLKGDT
RASPDTGRRL TTAYGVRISH TYGTVLNGFA VHADAGQARR LAADPSIASV VQDTAVTVDA
VRSPPSWGLD RVDQPGLPLD GDYRAPGSGG AGVTVYVIDT GIRISHRDFG GRASYGWDFV
GGDRDAPDGN GHGTEVAGIV AGRTFGVAAK AKVVAVRVLD DTGAGTTARV IAGIDWVTRH
AHRPAVANLS LGGSYNAQLD AAVRASIRSG VTCVVAAGNA GRPAALGSPA DVREAVTVGA
TDRGDARAAF SDYGSALDLF APGVAVTSAS SASDTGRVAR SGTSMAAPHA AGAAALYLAG
HPKATPAQVA RALVTGAVNG RISGRGAGSP DRLLQVARLG
//
