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Database: UniProt
Entry: A0A1R3SYP2_9BACT
LinkDB: A0A1R3SYP2_9BACT
Original site: A0A1R3SYP2_9BACT 
ID   A0A1R3SYP2_9BACT        Unreviewed;       540 AA.
AC   A0A1R3SYP2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=C-terminal peptidase {ECO:0000313|EMBL:SCD18999.1};
GN   ORFNames=PSM36_0163 {ECO:0000313|EMBL:SCD18999.1};
OS   Proteiniphilum saccharofermentans.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae;
OC   Proteiniphilum.
OX   NCBI_TaxID=1642647 {ECO:0000313|EMBL:SCD18999.1, ECO:0000313|Proteomes:UP000187464};
RN   [1] {ECO:0000313|EMBL:SCD18999.1, ECO:0000313|Proteomes:UP000187464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M3/6 {ECO:0000313|EMBL:SCD18999.1};
RA   Seilhamer J.J.;
RL   Submitted (AUG-2016) 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; LT605205; SCD18999.1; -; Genomic_DNA.
DR   RefSeq; WP_076928370.1; NZ_LT605205.1.
DR   AlphaFoldDB; A0A1R3SYP2; -.
DR   STRING; 1642647.PSM36_0163; -.
DR   KEGG; psac:PSM36_0163; -.
DR   Proteomes; UP000187464; Chromosome i.
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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU004404};
KW   Protease {ECO:0000256|RuleBase:RU004404};
KW   Reference proteome {ECO:0000313|Proteomes:UP000187464};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU004404}.
FT   DOMAIN          76..161
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
SQ   SEQUENCE   540 AA;  60157 MW;  140E0C6018A630CE CRC64;
     MLKRIIPIVL GTLFLTGCVY AQFRPSPEGV KLERTLQLIQ GLYVDDVDAS GLTEAAIRGM
     LKELDPHSTY LNKEEVKAMN EPLQGNFDGI GISFNMLTDT LYVMEVISGG PSQKVGIMPG
     DKIIYVNDTL IAGVKKNNQD VVSMLRGPKG TEVNVKVLRR GVPELMPFRI VRDRIPITSI
     DASYMVADDI GYIRLSRFGI TSGDEFRQAE QELRAQGMDH LILDLTDNGG GILQTANDIV
     DEFLGDGKLI VYTEGKNQPR YTMNATGDDE LKGGKLVILV NEASASASEI LAGAIQDWDR
     GVIVGRRTFG KGLVQRQLPL PDGTMIRLTV ARYYTPTGRS IQKPYENGDQ DAYNMDFVNR
     YNHGELFQAD SIHFPDSLKY TTLVNKRTVY GGGGIMPDYF VPIDTTAGTV LHGRLNGLGV
     INKVAIAEVD NHRRELLQKY PDINKFKAEY MITEGVIPKL MKLASEENIE WDEEQFASSR
     PLIFKQLKAL MARDLYDSSA FFRIINEEND IFMEGMKIIS DDNRYQGLLE GVGSNVGQNR
//
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