ID C0C459_9FIRM Unreviewed; 394 AA.
AC C0C459;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE SubName: Full=Peptidase, S41 family {ECO:0000313|EMBL:EEG72852.1};
DE EC=3.4.21.- {ECO:0000313|EMBL:EEG72852.1};
GN ORFNames=CLOHYLEM_06874 {ECO:0000313|EMBL:EEG72852.1};
OS [Clostridium] hylemonae DSM 15053.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=553973 {ECO:0000313|EMBL:EEG72852.1, ECO:0000313|Proteomes:UP000004893};
RN [1] {ECO:0000313|EMBL:EEG72852.1, ECO:0000313|Proteomes:UP000004893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15053 {ECO:0000313|EMBL:EEG72852.1,
RC ECO:0000313|Proteomes:UP000004893};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Clostridium hylemonae (DSM 15053).";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEG72852.1, ECO:0000313|Proteomes:UP000004893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15053 {ECO:0000313|EMBL:EEG72852.1,
RC ECO:0000313|Proteomes:UP000004893};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
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:EEG72852.1}.
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DR EMBL; ABYI02000034; EEG72852.1; -; Genomic_DNA.
DR RefSeq; WP_006444231.1; NZ_GG657760.1.
DR AlphaFoldDB; C0C459; -.
DR STRING; 553973.CLOHYLEM_06874; -.
DR MEROPS; S41.004; -.
DR eggNOG; COG0793; Bacteria.
DR HOGENOM; CLU_017295_3_2_9; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000004893; Unassembled WGS sequence.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00988; PDZ_CTP_protease; 1.
DR CDD; cd07560; Peptidase_S41_CPP; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004447; Peptidase_S41A.
DR InterPro; IPR005151; Tail-specific_protease.
DR NCBIfam; TIGR00225; prc; 1.
DR PANTHER; PTHR32060:SF30; CARBOXY-TERMINAL PROCESSING PROTEASE CTPA; 1.
DR PANTHER; PTHR32060; TAIL-SPECIFIC PROTEASE; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF03572; Peptidase_S41; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00245; TSPc; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004404};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004404};
KW Serine protease {ECO:0000256|RuleBase:RU004404}.
FT DOMAIN 95..165
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 394 AA; 42717 MW; 79F9BF1AA9B573D2 CRC64;
MKKNKGFIKG ALCGALAVLL IAGIVSCAGK KNVLSAGGDK IVDSKTEEKL SQLQGLIDGK
YLGDVDEDAL QSGIYKGYIN GLSDPYSVYY DKEETEQLLE TTSGEYSGIG AVLSQNRDTG
IITILQVYDD SPAQKAGIQD NDILYKVDGE EVTGIDLTEV VSGIKGEEGT EVKLTVLRGD
AKDEVEVTAV RGKVEAQTVK YEMKEDQIGY IRVTEFDSVT YDQYKEAIDD LEGQGMKGLI
VDLRNNPGGN LSTVCDMLDL MLPEGLIVYT DDKDGNRSEE TSDEEHQFKL PMTVLVNGNS
ASASEIYAGA IQDYSLGEII GTQTYGKGVV QQIFDLKDGT CVKLTIAEYF TPKGRNINGK
GITPDVEVEF EADEADPEAD NQLEKALEVI KGKM
//