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Database: UniProt
Entry: A0A1Q4YWI0_9PSEU
LinkDB: A0A1Q4YWI0_9PSEU
Original site: A0A1Q4YWI0_9PSEU 
ID   A0A1Q4YWI0_9PSEU        Unreviewed;       522 AA.
AC   A0A1Q4YWI0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Serine protease {ECO:0000313|EMBL:OKI38913.1};
GN   ORFNames=A6A25_01550 {ECO:0000313|EMBL:OKI38913.1};
OS   Saccharothrix sp. CB00851.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharothrix.
OX   NCBI_TaxID=1835005 {ECO:0000313|EMBL:OKI38913.1, ECO:0000313|Proteomes:UP000186828};
RN   [1] {ECO:0000313|EMBL:OKI38913.1, ECO:0000313|Proteomes:UP000186828}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB00851 {ECO:0000313|EMBL:OKI38913.1,
RC   ECO:0000313|Proteomes:UP000186828};
RX   PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL   MBio 7:e02104-e02116(2016).
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:OKI38913.1}.
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DR   EMBL; LWLC01000001; OKI38913.1; -; Genomic_DNA.
DR   RefSeq; WP_073885898.1; NZ_LWLC01000001.1.
DR   AlphaFoldDB; A0A1Q4YWI0; -.
DR   STRING; 1835005.A6A25_01550; -.
DR   Proteomes; UP000186828; 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   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.
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:UP000186828};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..522
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038726327"
FT   DOMAIN          403..522
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   ACT_SITE        160
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        193
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        346
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   522 AA;  52870 MW;  6FB3EC6C0ED6E339 CRC64;
     MGDARASWRK TKRLAGVGLA TGTAFAVTAA LTTFTSAAAE GEILGSGAPN AVKDSYIVVL
     NDLSTSSVGT LSGKYQANVK HTYTRALRGF SATMTESQAR KLAADPAVAY VQQDGEVKIS
     GTQAPTPSWG LDRIDQAALP LNNSYTYPNE GEGVTAYIID TGIRNSHGDF GGRAVSGRDT
     VDNDNDTTDC NGHGTHVAGT VGGTKYGVAK KAKLVGVRVL NCAGSGTYAG VIAGIDWVTA
     NAVKPAVANM SLGGGADATV DQAVRNSIAS GVTYGLAAGN DSGANACNTS PARTLEAITV
     GSTTNTDARS SFSNIGTCLD IFAPGSSITS AWHTNDTATN TISGTSMATP HVVGAAAVYL
     AANPTATPQQ VRDALVNGAT SGVVGNAGTG SPNKLLRLVG TSTPPPGGCA AKTNATNVAV
     PDLGTATSPI TIADCAGKAG SAATVEVHVK HTYRGDLAID LITPSGAVKQ LKVTSGSDGA
     DNVDATYTVN LSAENANGTW RLRVRDAYSQ DTGYIDTWTL DL
//
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