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Database: UniProt
Entry: B9DZL0_CLOK1
LinkDB: B9DZL0_CLOK1
Original site: B9DZL0_CLOK1 
ID   B9DZL0_CLOK1            Unreviewed;       440 AA.
AC   B9DZL0;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 77.
DE   RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   OrderedLocusNames=CKR_0634 {ECO:0000313|EMBL:BAH05685.1};
OS   Clostridium kluyveri (strain NBRC 12016).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=583346 {ECO:0000313|EMBL:BAH05685.1, ECO:0000313|Proteomes:UP000007969};
RN   [1] {ECO:0000313|Proteomes:UP000007969}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 12016 {ECO:0000313|Proteomes:UP000007969};
RA   Inui M., Nonaka H., Shinoda Y., Ikenaga Y., Abe M., Naito K., Vertes A.A.,
RA   Yukawa H.;
RT   "Complete genome sequence of Clostridium kluyveri and comparative genomics
RT   of Clostridia species.";
RL   Submitted (SEP-2005) 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}.
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DR   EMBL; AP009049; BAH05685.1; -; Genomic_DNA.
DR   RefSeq; WP_011989280.1; NC_011837.1.
DR   AlphaFoldDB; B9DZL0; -.
DR   KEGG; ckr:CKR_0634; -.
DR   HOGENOM; CLU_011263_15_7_9; -.
DR   Proteomes; UP000007969; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd07477; Peptidases_S8_Subtilisin_subset; 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; 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   InterPro; IPR034202; Subtilisin_Carlsberg-like.
DR   PANTHER; PTHR43806:SF59; EXTRACELLULAR PROTEASE; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF13290; CHB_HEX_C_1; 1.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
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}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}.
FT   DOMAIN          20..65
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          97..344
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   ACT_SITE        106
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        138
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        296
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   440 AA;  46571 MW;  BE8443078711EDFE CRC64;
     MKRYIIKFKT SSTDKNKLIS KYDEDFKHQF NNFNAATAEM TPQDISKLKQ DSAVDYVEED
     YIVKMSTVSS VKSSTSVTNW GIDDINASQA WASGLTGEDI KIAIIDSGIA SHSNLTIAGG
     KNVISDSSST SYTDENGHGT HVAGIIAAQG LNGGVKGVAP DASIYAVKAL DSDGEGYTSD
     IISGIDWAIQ NDMDIISMSL GSDESSTALK NAIDTAYNDG ILIVAAAGND GNTRGTGTNI
     EYPANYSSVI AVGAVNSNNT RASFSSTGSK LEVSAPGVDI VSTYLNNGYE KMSGTSMSTP
     FVTGDLALLK QKYPSYTNVQ LRQLLDSNII DPGISGKDSL YGYGLITAPT STTTTTISTP
     TASIAAGTYT SSQTVSLSDT TSGVSIYYTL DGTTPTKIPK PTASVPSGSY RTPLIVMLQI
     KFPNERIFHY FITTIYALMT
//
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