ID A0A0M8SGG7_9ACTN Unreviewed; 513 AA.
AC A0A0M8SGG7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:KOU36314.1};
GN ORFNames=ADK51_04165 {ECO:0000313|EMBL:KOU36314.1};
OS Streptomyces sp. WM6368.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415554 {ECO:0000313|EMBL:KOU36314.1, ECO:0000313|Proteomes:UP000037718};
RN [1] {ECO:0000313|EMBL:KOU36314.1, ECO:0000313|Proteomes:UP000037718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM6368 {ECO:0000313|EMBL:KOU36314.1,
RC ECO:0000313|Proteomes:UP000037718};
RA Noorani M.;
RL Submitted (JUL-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:KOU36314.1}.
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DR EMBL; LGDA01000010; KOU36314.1; -; Genomic_DNA.
DR RefSeq; WP_053701532.1; NZ_LGDA01000010.1.
DR AlphaFoldDB; A0A0M8SGG7; -.
DR PATRIC; fig|1415554.3.peg.859; -.
DR Proteomes; UP000037718; 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; 2.60.120.260; Galactose-binding domain-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; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR002884; P_dom.
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 InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51829; P_HOMO_B; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
DR PROSITE; PS51318; TAT; 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..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..513
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005822938"
FT DOMAIN 398..513
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT ACT_SITE 165
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 198
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 340
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 513 AA; 51688 MW; 4132DBE7CF8BA62F CRC64;
MPVMRHTRRR FAGISATAVV ALALGSASAL PASAVGGGTA GVVQNAGAPG SIPGSYIVTL
KDSAARSTAA SGKAVAKRYG AKIDKTYSAA LNGYAVKLSE AQAKKLAADP AVTSVVQNRT
FTVSTTQPTP PSWGLDRVDQ GALPLNQSYS YPDKAGEGVT AYIIDTGVRI THQDFGGRAS
YGYDAIDNDS TAQDGHGHGT HVAGTVAGGS YGVAKKAKIV GVRVLDNSGN GTTAQVVAGI
DWVTRNAVKP AVANMSLGGG ADSASGITYA VAAGNESSNA STKSPARVTE AITVGATTST
DVRASYSNFG TVLDIFAPGS AITSAWGTGD TATNTINGTS MATPHVAGAA AVYLSQNPAS
TPTQVATALV GSSTPNVVGG GGTGSPNRLL RVVAQGPVPP GKRFENTADQ AVGDNATAES
SITVSGVVGN APSALQVPID IKHPYIGDLK VDLVAPDGSV YTLHNRANGG DDNIIRTFTV
NASAETANGV WKLRVNDNST GDTGKIDSWA LQF
//
