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Database: UniProt
Entry: A0A0E3WAR2_9FIRM
LinkDB: A0A0E3WAR2_9FIRM
Original site: A0A0E3WAR2_9FIRM 
ID   A0A0E3WAR2_9FIRM        Unreviewed;       382 AA.
AC   A0A0E3WAR2;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Tail specific protease {ECO:0000313|EMBL:CQB51990.1};
GN   ORFNames=2453 {ECO:0000313|EMBL:CQB51990.1};
OS   Syntrophomonas zehnderi OL-4.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC   Syntrophomonas.
OX   NCBI_TaxID=690567 {ECO:0000313|EMBL:CQB51990.1, ECO:0000313|Proteomes:UP000045545};
RN   [1] {ECO:0000313|EMBL:CQB51990.1, ECO:0000313|Proteomes:UP000045545}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OL-4 {ECO:0000313|EMBL:CQB51990.1,
RC   ECO:0000313|Proteomes:UP000045545};
RA   Murphy D.;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S41A family.
CC       {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
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DR   EMBL; CGIH01000042; CQB51990.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0E3WAR2; -.
DR   STRING; 690567.2453; -.
DR   Proteomes; UP000045545; 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; PF00595; PDZ; 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, ECO:0000313|EMBL:CQB51990.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000045545};
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..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          88..154
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
SQ   SEQUENCE   382 AA;  41837 MW;  670731D8E085145F CRC64;
     MILKDNKIVR GFYKFFAFLG LLVFLSLAFV FITNSSSISS LFAVVGLLKT QSLYEPQTGK
     MIQGATSGIV SSLKDPYSKY LNKSQWEELK LQLNAEFGGI GVYVLELDGQ LGIVSPIKGT
     PAYRQGLKNG DIIVRINGES AVNMSQDDAV NRMRGEPGTQ LNLSIFRPSD GQEHDFKIVR
     EIINVPSVDD KVIGDGVPIG YIKLNQFHAH SVQEIANSLN RLNKKDIKGL ILDLRDNGGG
     DFDASIAIAD IFLEDKEIVS AKDARGKEKH HRSEPGSFKL PMVVLVNGNS ASAAEILSGA
     LQDNKRAVLV GEKTYGKGLV QTVFPLRDGG ALKLTTQKYF TPKGTDINEI GINPDFVVKN
     PEGQDVDLQL QRAIEVLKEK IM
//
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