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Database: UniProt
Entry: A0A1Y3W0T2_9BACT
LinkDB: A0A1Y3W0T2_9BACT
Original site: A0A1Y3W0T2_9BACT 
ID   A0A1Y3W0T2_9BACT        Unreviewed;       532 AA.
AC   A0A1Y3W0T2;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Peptidase S41 {ECO:0000313|EMBL:OUN66851.1};
GN   ORFNames=B5G13_01010 {ECO:0000313|EMBL:OUN66851.1};
OS   Butyricimonas sp. An62.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Odoribacteraceae;
OC   Butyricimonas.
OX   NCBI_TaxID=1965649 {ECO:0000313|EMBL:OUN66851.1, ECO:0000313|Proteomes:UP000196559};
RN   [1] {ECO:0000313|Proteomes:UP000196559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An62 {ECO:0000313|Proteomes:UP000196559};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) 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:OUN66851.1}.
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DR   EMBL; NFHW01000001; OUN66851.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y3W0T2; -.
DR   OrthoDB; 9812068at2; -.
DR   Proteomes; UP000196559; 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   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   Protease {ECO:0000256|RuleBase:RU004404};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196559};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU004404}.
FT   DOMAIN          91..152
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
SQ   SEQUENCE   532 AA;  59986 MW;  F5967A71CDE30117 CRC64;
     MNKSNLRALL TPIVLALAIV FGMMLNRFLP DRTQVSASSE MFLPVTGSKL DLIISMIQNS
     YVDTVDTRQI VENTIPVLLK DLDPHTVYIP AKDMQRANEG IVGNFGGVGI QFYKYLDTVT
     VVKVVPGGPS EKAGIKDGDR IVRVNDSLVA GVKMGQDKIQ ELMRGELGTK VELTIARRGE
     PKLIKKEVVR GSIPVKSVDV AYMLNDTTGY LKTNTFGMHT YAEFMQALVK LKAEGMRKII
     IDLRENEGGV LPIAIQMINE FLDADRLILY TQGQAQPRTD YKSNGKGQFK DLRVDVLISE
     FSASASEIFA GAIQDNDRGL IIGRRSFGKG LVQEQRMLPD GSALRLTVAR YYTPSGRSIQ
     KPYNEGKEKY YNDLYNRLVH GEFSQKDSIV FDENLKYQTV DGRTVYGGGG IMPDVFVPAD
     TTGVSRYLSD VTRTQFLYEY TFDFMDRHRP EMVNLKDYKQ IQNYLKSFDL VNEMANYAAR
     RGLKRDEKGI KESYQVLRTR IEAYIARHTI DDEGFYPILG QIDNTLQEAI KQ
//
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