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
//