ID A0A0N0T195_9ACTN Unreviewed; 495 AA.
AC A0A0N0T195;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Peptidase S8 {ECO:0000313|EMBL:KOV67436.1};
GN ORFNames=ADL01_24560 {ECO:0000313|EMBL:KOV67436.1};
OS Streptomyces sp. NRRL WC-3618.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519490 {ECO:0000313|EMBL:KOV67436.1, ECO:0000313|Proteomes:UP000037738};
RN [1] {ECO:0000313|EMBL:KOV67436.1, ECO:0000313|Proteomes:UP000037738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL WC-3618 {ECO:0000313|EMBL:KOV67436.1,
RC ECO:0000313|Proteomes:UP000037738};
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:KOV67436.1}.
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DR EMBL; LGDW01000325; KOV67436.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0T195; -.
DR PATRIC; fig|1519490.3.peg.5363; -.
DR OrthoDB; 9813435at2; -.
DR Proteomes; UP000037738; 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 Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
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 PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
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:UP000037738};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..495
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038464479"
FT DOMAIN 159..468
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 167
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 210
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 418
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 495 AA; 50608 MW; 5A4909A8D0465CC0 CRC64;
MVMASAFAFL PNIQAVAADA EVTTGAAAVA ADAPSLSYVV NVFPGFGPSA YVKKAITKAG
GTIVMSYDRI GVVVVHSANP DFAKIIRKVP GVQSAGNTRN APLPAQSTTD EGAPKVLSAA
EMASATADAT AAQDPLEPLQ WDLPAIKADK AHEKTLGSRK VTVAVIDTGV DDTHPDIAPN
FDRAASVNCV TGKPDTTDGA WRPTTGESPH GTHVAGEIAA AKNGVGVTGV APGVKVSGIK
VSTTAGFFYT EAVVCGFVWA AEHGVDVTNN SYYTDPWYFN CKSDPDQKAL VDAITRASRY
AEHKGVVNVA AAGNENYDLA ADEITDPVSP NDATPSDRVV DPSKCYDIPT QLPGVVTVSS
TGAKGIKSSF SNHGLGVIDI AAPGGDSTRL QTPAPPATSG LILGPLPGGT WGYMAGTSMA
TPHVAGVAAL IKSTHPHAPA ALVKALLYAE ADATPCGDPY DIDGDGKVDA VCEGPKNYNG
FYGHGIADAL DAVTN
//
