ID T0ND45_9CLOT Unreviewed; 409 AA.
AC T0ND45;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0000259|Pfam:PF00082};
GN ORFNames=M918_06130 {ECO:0000313|EMBL:EQB88055.1};
OS Clostridium sp. BL8.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1354301 {ECO:0000313|EMBL:EQB88055.1, ECO:0000313|Proteomes:UP000015873};
RN [1] {ECO:0000313|EMBL:EQB88055.1, ECO:0000313|Proteomes:UP000015873}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BL8 {ECO:0000313|EMBL:EQB88055.1,
RC ECO:0000313|Proteomes:UP000015873};
RX PubMed=25076986; DOI=10.1186/1757-4749-6-30;
RA Marathe N.P., Shetty S.A., Lanjekar V.B., Rasane M.H., Ranade D.R.,
RA Shouche Y.S.;
RT "Genome sequencing of multidrug resistant novel Clostridium sp. BL8 reveals
RT its potential for pathogenicity.";
RL Gut Pathog. 6:30-30(2014).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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:EQB88055.1}.
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DR EMBL; AUPA01000176; EQB88055.1; -; Genomic_DNA.
DR AlphaFoldDB; T0ND45; -.
DR STRING; 1354301.M918_06130; -.
DR PATRIC; fig|1354301.3.peg.2394; -.
DR OrthoDB; 9798386at2; -.
DR Proteomes; UP000015873; 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 PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01240};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01240};
KW Reference proteome {ECO:0000313|Proteomes:UP000015873};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01240}.
FT DOMAIN 125..263
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 134
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 164
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 345
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 409 AA; 46704 MW; D6CEF84414F60631 CRC64;
MKKYILLSIT IIILLWSGYF FSNKISKEKE VSTFLSKSYE LPAFDENLPD PLHVRLNQVD
LKGKDLSELD INDRSKDLFH AYFDTTTKWP TKDKMPKDYN PKEILNMGKD PGLDIKKLHK
QGITGKNIGI AILDSPLKNK HEDYQDRIKH YEELYNPRTD NLMHGPAVTS IAAGKTVGVA
PKADIYYFAI NNTYLDKAGN SRMDFEKVAN AIDKVINLNN ELPDNKKIKV ISMSMGCSQE
DKGYKEFLEA VDKASKEGIF VISTSLSRTH GFKFSGLGRF PVDNPNETSS YVAGKFWEGS
VFSKNTPEQF LEWDTGYVHF PMDSRTVAGP NYNDEYTFHR YGAFSWVVPY ISGLYVLAYD
ANDKITPEVF WKTVIETSKP IEVEYKSQKY ELKHVISPVD LIEKIKTLS
//
