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Database: UniProt
Entry: A0A2R7JRU5_9SPHN
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Original site: A0A2R7JRU5_9SPHN 
ID   A0A2R7JRU5_9SPHN        Unreviewed;       445 AA.
AC   A0A2R7JRU5;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Peptidase S41 {ECO:0000313|EMBL:PTS87695.1};
GN   ORFNames=DBR17_05500 {ECO:0000313|EMBL:PTS87695.1};
OS   Sphingomonas sp. HMWF008.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=2056845 {ECO:0000313|EMBL:PTS87695.1, ECO:0000313|Proteomes:UP000244749};
RN   [1] {ECO:0000313|Proteomes:UP000244749}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMWF008 {ECO:0000313|Proteomes:UP000244749};
RA   Muscarella M.E.;
RL   Submitted (APR-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:PTS87695.1}.
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DR   EMBL; QAIS01000188; PTS87695.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2R7JRU5; -.
DR   Proteomes; UP000244749; 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; IPR041489; PDZ_6.
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; PF17820; PDZ_6; 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:UP000244749};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU004404}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..445
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015358317"
FT   DOMAIN          98..154
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
SQ   SEQUENCE   445 AA;  47687 MW;  DB9A58503435C497 CRC64;
     MSRFTTSLLQ ASAIAAALAI VPVGTSAMAA VDTGTYREMS VFLDVFNRVK AEYVDKVDDK
     VLVKGAIDGM LAALDPHSAY ETGLDYQNLR IQTLGSYGGL GLTVTMEDGA VKVIAPQEDS
     PGWRAGIKSG DYITHINGKL IFGQTLDEAI SAMRGEPGTR IALTLLRPGR PKPIEVALVR
     EKIVQKPVKW SVKDGVGIIN INAFSEHTGD AVTAAIQGIQ KQLGHDPLGY IIDLRDNGGG
     LRDESIAVAD NFLSSGEIVS QRGRDKADIE PFYAESYVKG DLAHGLPIIV LTNAGTASAS
     EIVAGALQDQ HRALVMGERS FGKGSVQTVI DLGDNAALRL TTSRYYTPSG RSVQEGGIEP
     DIAVPQISDP DYKSRPVFRE DDLRRHLINE VKNDNAAIEE DTKPDPRFAA TAEELKAKGI
     DDFQLNYALK TIGRLSGTAQ AVAAK
//
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