ID A0A395YKQ6_9CLOT Unreviewed; 439 AA.
AC A0A395YKQ6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=S41 family peptidase {ECO:0000313|EMBL:RGY98253.1};
GN ORFNames=DXA13_11945 {ECO:0000313|EMBL:RGY98253.1};
OS Clostridium sp. AM58-1XD.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=2292307 {ECO:0000313|EMBL:RGY98253.1, ECO:0000313|Proteomes:UP000266320};
RN [1] {ECO:0000313|EMBL:RGY98253.1, ECO:0000313|Proteomes:UP000266320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM58-1XD {ECO:0000313|EMBL:RGY98253.1,
RC ECO:0000313|Proteomes:UP000266320};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) 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:RGY98253.1}.
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DR EMBL; QSDR01000017; RGY98253.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395YKQ6; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000266320; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Gene3D; 3.30.750.44; -; 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:SF22; CARBOXYL-TERMINAL-PROCESSING PEPTIDASE 2, CHLOROPLASTIC-RELATED; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU004404};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU004404};
KW Reference proteome {ECO:0000313|Proteomes:UP000266320};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 116..184
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 439 AA; 48361 MW; 7248EFE2BBD52367 CRC64;
MESKSKFWHG VLVGALVTVF GGLLVIGASS GILMLGRRTL NVEQQQQIQT VESETDMEKG
ELDYQKINVK LELLNQKVGE AFYFEPDEKN MEEGIYAGLM AGLGDPYSGY YTPEEYADLM
EDTQGVYCGI GAMISQNLET KVMTVIRVFE GSPAAEAGLL AGDMIFKIDG KDVSQENVDL
VVKNYVKGKE GTDVVVTVLR PSASDYIDIT MTRRNIEVPT VEHKMLEDGI GYVLITQFEM
VTADQFKAAV KDLQDQGMKK LMIDLRSNPG GVVDGAVSIA AFLLPEGDIL RTEYKNGQED
VYRTKDKKLR VDTTTGSKFP QYPVLDEDEL DIPIAILVNG NSASASEILA GAMKDYKRAT
LVGTKTFGKG IVQNVYPLRD GSAIKLTVAK YFTPSGYDLH EKGIEPDVEV ELSDELIAKG
YYSLEEDNQV QKAIEILNE
//
