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Database: UniProt
Entry: A0A0X3XJW6_9ACTN
LinkDB: A0A0X3XJW6_9ACTN
Original site: A0A0X3XJW6_9ACTN 
ID   A0A0X3XJW6_9ACTN        Unreviewed;      1101 AA.
AC   A0A0X3XJW6;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Peptidase S8 {ECO:0000313|EMBL:KUL69663.1};
GN   ORFNames=ADL34_28755 {ECO:0000313|EMBL:KUL69663.1};
OS   Streptomyces sp. NRRL WC-3605.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1609103 {ECO:0000313|EMBL:KUL69663.1, ECO:0000313|Proteomes:UP000052945};
RN   [1] {ECO:0000313|EMBL:KUL69663.1, ECO:0000313|Proteomes:UP000052945}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL WC-3605 {ECO:0000313|EMBL:KUL69663.1,
RC   ECO:0000313|Proteomes:UP000052945};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01240, 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:KUL69663.1}.
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DR   EMBL; LLZN01000091; KUL69663.1; -; Genomic_DNA.
DR   RefSeq; WP_062671599.1; NZ_LLZN01000091.1.
DR   AlphaFoldDB; A0A0X3XJW6; -.
DR   OrthoDB; 9798386at2; -.
DR   Proteomes; UP000052945; 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   InterPro; IPR017297; Peptidase_S8A_DPH-A.
DR   PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR   PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PIRSF; PIRSF037854; Dihydropyridine_esterase; 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:UP000052945};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..1101
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007058037"
FT   DOMAIN          218..482
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   REGION          25..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        227
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        259
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        436
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   1101 AA;  114533 MW;  467A14DEDA3436C6 CRC64;
     MRRHVRRACA AAVASAAALA LTAGTTGPAS AQPERRPSGA ASDPSPHRVT LITGDRVSVD
     SKGRVVGLER AKGRTRIPVQ IRRIDGHTLV IPADAAGLVA DGTLDRRLFD VTELTRSRTG
     ASGAKGPKVI VGYRGAATGA KADVRDAGTL RRTLKSLNAD AVQTTDRGAP GLWDALTDGD
     RTASGVAHVW LDGVRRASLD KSVAQIGAPK AWAAGYDGKG VKIAVLDTGV DATHPDLEGQ
     VVAAKNFSPA PGTTDKVGHG THVASIAAGT GAKSGGKYKG VAPGAAILNG KVLDDEGYGD
     DSSILAGMEW AAEQGAQIVN MSLGGTDTPE VDPLEAAVDK LSAEKGVLFT IAAGNAGPES
     VGSPGSADAA LTVGAVDDKD ALAPWSSTGP RAGDGAVKPD VTAPGVDITA ASAKGSVIAQ
     EVGENPPGYV TIEGTSMATP HVAGAAAILK QQHPDWTYTE LKGALTASAK GGAYTPFQQG
     AGRVQVDKAI KQNVIAEPVS VSFGTQQWPH TDDKPDARKL TYRNLGTKDV TLRLAVKATD
     PEGHAAPAGF FKLGATEVTV PAGGTASVDF TVDTRLGGTL DGAYSAYVTA TGGGQSVRTA
     AAVQREVESY DVTVKHIGRD GKPAPEYNTA LIGFSGLADE RFYQVPTTPS GTVRLRVPKG
     TYLMDAWIAK DWVTMEGGLD WVVQPKLNVT RNTTLTIDAR TTRSADITVP DPRAEPVFAA
     SGYFYDAAGI GIAAGLGSFA DLRMAHLGPE IASGLTQTWN AQYTRGAAAE YDVATSAKVK
     KIQGHKVRHF TAGELAKVSS GLGAAAPGKT GALLPVGFLP DDVVFATPVE QKLPGTRTLY
     VSTSDKIQWT FDMEQYSGRD ADGLLVVDAF YTLGDPQTFA AGKSYTKTFN TAVFGPHINK
     DYGLFRDGND IYGFLPLFAD ANKHAGSSDV TSVTTNLYRN GSKIGTNADP LLGEAFKVPS
     ADAEYRLTTS VKRSVKVAAA STRIDASWTF RSKKPSGDQV SLPASTVRFG AKTGLDSRAE
     AGKKVTFPVT VVGAAAGRNL KSLHVYVSYD YGQTWKKLDV KNGKITVKNP AKGKGISFHG
     KVADKKGNKA TISIYNAYYG K
//
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