ID A0A1D3DYS9_9ACTN Unreviewed; 397 AA.
AC A0A1D3DYS9;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Peptidase S8 {ECO:0000313|EMBL:OEJ97458.1};
GN ORFNames=J116_026390 {ECO:0000313|EMBL:OEJ97458.1};
OS Streptomyces thermolilacinus SPC6.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1306406 {ECO:0000313|EMBL:OEJ97458.1, ECO:0000313|Proteomes:UP000095329};
RN [1] {ECO:0000313|EMBL:OEJ97458.1, ECO:0000313|Proteomes:UP000095329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPC6 {ECO:0000313|EMBL:OEJ97458.1,
RC ECO:0000313|Proteomes:UP000095329};
RX PubMed=23868127;
RA Chen X., Zhang B., Zhang W., Wu X., Zhang M., Chen T., Liu G., Dyson P.;
RT "Genome Sequence of Streptomyces violaceusniger Strain SPC6, a Halotolerant
RT Streptomycete That Exhibits Rapid Growth and Development.";
RL Genome Announc. 1:0-0(2013).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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:OEJ97458.1}.
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DR EMBL; ASHX02000001; OEJ97458.1; -; Genomic_DNA.
DR RefSeq; WP_023590088.1; NZ_ASHX02000001.1.
DR AlphaFoldDB; A0A1D3DYS9; -.
DR STRING; 1306406.J116_026390; -.
DR eggNOG; COG1404; Bacteria.
DR OrthoDB; 9798386at2; -.
DR Proteomes; UP000095329; 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; 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; 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};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..397
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008914999"
FT DOMAIN 66..110
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 152..378
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 343
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 397 AA; 40183 MW; AC30220286ED0E2E CRC64;
MRLSARCASV ALLLLLPFAA PPAAQADSEP ARTAPAPLRT HAVGGIDGQY IVTLKPNVAS
AHAARMAGVT PLHSYSQVLN GFAAKMSPAQ LTAVRNMPEV AAVEQDAEVT AVPVREGTPS
TRVAASSWGL DRIDQPYLPL NGQFNVNGTG AGVYALILDS GIDYAHPEFA GRAYFGYDAM
GDGRRGQDCN GHGTHVAGTV GGSTFGVARQ VRLVSLRVLG CDGKGSWSGI IGGFEWAAAN
AGNAPAVLNA SLGGPRSEAV NAAATALYEK GVLPVVAAGN SAVDACGISP ASAPGSFTVG
ASNHLDQEAS FSNFGPCLSI YAPGTQIRSA RLGGGSVALD GTSMASPHVA GVAALYKAQN
PTAAPGTVAG WLVDQSVKNT LTVSKTSPNR LLQTGGL
//
