ID   A0A1I1S276_9CLOT        Unreviewed;      1274 AA.
AC   A0A1I1S276;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Subtilase family protein {ECO:0000313|EMBL:SFD40599.1};
GN   ORFNames=SAMN05421842_14212 {ECO:0000313|EMBL:SFD40599.1};
OS   Clostridium uliginosum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=119641 {ECO:0000313|EMBL:SFD40599.1, ECO:0000313|Proteomes:UP000199263};
RN   [1] {ECO:0000313|EMBL:SFD40599.1, ECO:0000313|Proteomes:UP000199263}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12992 {ECO:0000313|EMBL:SFD40599.1,
RC   ECO:0000313|Proteomes:UP000199263};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01240}.
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DR   EMBL; FOMG01000042; SFD40599.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1S276; -.
DR   STRING; 119641.SAMN05421842_14212; -.
DR   OrthoDB; 2744137at2; -.
DR   Proteomes; UP000199263; 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; cd07478; Peptidases_S8_CspA-like; 2.
DR   Gene3D; 2.60.120.1290; -; 2.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 2.
DR   InterPro; IPR034045; Pep_S8_CspA-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; IPR015500; Peptidase_S8_subtilisin-rel.
DR   PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR   PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR   Pfam; PF00082; Peptidase_S8; 4.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Subtilisin-like; 2.
DR   PROSITE; PS51892; SUBTILASE; 2.
DR   PROSITE; PS00136; SUBTILASE_ASP; 2.
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:UP000199263};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}.
FT   DOMAIN          124..245
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          461..582
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          769..966
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          1107..1226
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   ACT_SITE        133
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        205
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        527
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        778
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        850
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        1172
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   1274 AA;  140005 MW;  FBA13652BDF5F1E7 CRC64;
     MNLLNKISGQ LRDNFRCGSR VEENIENMPD EIFFSLLDTV FTLVEYKGDI ASMVKKIPNA
     RIFIVDKNRA ILAIRGDVQE VVDELFDVII YVNPSSLYTL CDISPVEASG ATSFYNSVYL
     PLNGSGVIVG IVDTGIDYLN EEFINEDNTS RILTIWDQLI PTGKKPEGQF VGSEYTREEI
     NKAIKAKKDG QDPYSIVPSK DENGHGTSMA SVVGARGANP AVIGVAPRCD FAIVKLGTSP
     PKLNDQLGVY GNALTFSTSV LFLSMKYLYD LSYKLKKPIV ILLPLSGVRG AHNGLAVNER
     YIDEISKVRG ITVVVPTGNQ GDADNHVSGK IVKRGDIQSI QVKVDKNQKN LNIEIWISKP
     DKFALSIVSP SGEIISRIPP SLNKITEIKF LYESTIIYVQ YSIPEVLTGD EKITINARNI
     REGIWIFQLI GELVVTGDYD AYLLQRELLA PGTKFLNPNP YETLTIPSTS SYAISVGYYN
     QNNNSNVTES GRGYTRDGRV KPEVVAGGVN ALVTAVGGAT QVISGSSVAA AVVAGCSALI
     FQWGIINGND KNLYATKVKT YLIAGTSKRE GDIYPNPQWG YGMVNIKGVF DNIRLKINEF
     RGNDDEFFRI EESTFATIEY QGDIANAIEK NLNARVFFID EKRAIIVVKG DVNEVINKLS
     DVSIHVIPDL TDEEFFGIAQ FTFATIEYQG DVASAVKKIP NARVLILDKK RALLVIAGSI
     QDVQDVLDEL SDVIIYAVPT VLHTLCDISP VESSGVTAFH NSIYLPLDGR GVTIGIVDTG
     IDYLNEEFIN EDGTSRVLAI WDQTVTGGKK PEGQYGGSEY TREEINKAIK AKKEGQDPYK
     IVPSKDEIGH GTSMASIIGA RGVNPEVRGV APKCNFVIVK LYRAPLTVLD DFGVYGNVVT
     YTTSILFSGI KYLYDLSRKL KIPMVILVPL GTNSGPHNGL AFIERYIDEI SKVKGITVVV
     PNGNQGDSDT HTSGTITETA DTKSIELKID KSQKNIKFEI WISKPDKFSL SIISPSGEII
     ERIPPSLNKV TEIKFLYEST MIYVEYSIPE TLTGEERITI KARNIREGTW TFKLTGELVV
     TGKYDAYLIQ RELLAPGTKF LNPDPYETLT IPSTSSYAIS VGYYNQNNNS NVTESGRGYT
     RDGRVKPDVV AGGVNALVTA VGGATQVISG SSVAAAVVAG CSALIFQWGI INGNDKNLYA
     TKVKTYLIGG ALKREGDIYP NPQWGYGMVN LKGIFDNIRL KINEFRGNND IVIKKPIDEN
     EYYVRNLFIR LPRE
//