ID   U5MMU5_CLOSA            Unreviewed;       618 AA.
AC   U5MMU5;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Peptidase S8 and S53, subtilisin, kexin, sedolisin {ECO:0000313|EMBL:AGX42129.1};
GN   ORFNames=CLSA_c11230 {ECO:0000313|EMBL:AGX42129.1};
OS   Clostridium saccharobutylicum DSM 13864.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1345695 {ECO:0000313|EMBL:AGX42129.1, ECO:0000313|Proteomes:UP000017118};
RN   [1] {ECO:0000313|EMBL:AGX42129.1, ECO:0000313|Proteomes:UP000017118}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13864 {ECO:0000313|EMBL:AGX42129.1};
RX   PubMed=24285650;
RA   Poehlein A., Hartwich K., Krabben P., Ehrenreich A., Liebl W., Durre P.,
RA   Gottschalk G., Daniel R.;
RT   "Complete Genome Sequence of the Solvent Producer Clostridium
RT   saccharobutylicum NCP262 (DSM 13864).";
RL   Genome Announc. 1:e00997-13(2013).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP006721; AGX42129.1; -; Genomic_DNA.
DR   RefSeq; WP_022744411.1; NZ_AYXL01000300.1.
DR   AlphaFoldDB; U5MMU5; -.
DR   GeneID; 55473641; -.
DR   KEGG; csb:CLSA_c11230; -.
DR   PATRIC; fig|1345695.10.peg.3352; -.
DR   eggNOG; COG1404; Bacteria.
DR   HOGENOM; CLU_025670_0_0_9; -.
DR   OrthoDB; 2744137at2; -.
DR   Proteomes; UP000017118; Chromosome.
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; 1.
DR   Gene3D; 2.60.120.1290; -; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR034045; Pep_S8_CspA-like.
DR   InterPro; IPR017310; Pept_S8A_subtilisin_clostridia.
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; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF00082; Peptidase_S8; 2.
DR   PIRSF; PIRSF037894; Subtilisin_rel_CspABC; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 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:UP000017118};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}.
FT   DOMAIN          100..324
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          438..557
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   ACT_SITE        109
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        180
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        502
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   618 AA;  68872 MW;  2B3CBA1A8D7CA37B CRC64;
     MYNLRTCNLY YDPSVENYLI EYRGNFKEQI DKITYACGAI ITDTIGIVAV SANDLDRLIK
     DVPTIVFVDF RPMFVLQDIS PSYVDNINNI KMNPYLNLTG RNVLIGIVDT GIDYLNQEFI
     REDGTSRIAS IWDQTIQNSN NESVYIGETY SNEQINAAIN ASKNNQDPYK IVPSKDVIGH
     GTNMAGIMGA RGYTNKFQGV ANDVEFVVVK LFESSNFRKM LEENNVTYAP VYNSSEIVAA
     LEYLKNMFLK LNKPMVIYLG VGTTEGSHDS ANLISRYLTS IGNFRGLCIV TGVGNEGAAQ
     GHVSGYIKTK GDKKTSELKI PKELKYFSFN IWIQRPNRAS INVISPTGES SNVIQSKIDA
     REIYNFVFTD TKMFVRYYTP EHFTGHEVIQ IIFNDIKPGI WKIQLTGSYI VNGRYDIWLP
     PHNTLPENLV FLEPDPFNTL TIPGTVANAV TVAYYGTGNS LIASSGKGFN ANNVINPDIA
     TIGVNIITTK VSGGTTAVSG SSAATAIVAG ACALLLEWGI INGNDTTMYS PKIVSYLIYG
     AYRNELYKFP NRETGYGDFD LLGVFNVISR LYRNNSRGIP IHTSHNLEDD KFIEYYVNKL
     FIRIPQNDFG GFFNGNEI
//