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Database: UniProt
Entry: A0A2Z3JFJ9_9DEIO
LinkDB: A0A2Z3JFJ9_9DEIO
Original site: A0A2Z3JFJ9_9DEIO 
ID   A0A2Z3JFJ9_9DEIO        Unreviewed;       437 AA.
AC   A0A2Z3JFJ9;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=S41 family peptidase {ECO:0000313|EMBL:AWN23812.1};
GN   ORFNames=DKM44_11725 {ECO:0000313|EMBL:AWN23812.1};
OS   Deinococcus irradiatisoli.
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=2202254 {ECO:0000313|EMBL:AWN23812.1, ECO:0000313|Proteomes:UP000245368};
RN   [1] {ECO:0000313|EMBL:AWN23812.1, ECO:0000313|Proteomes:UP000245368}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17bor-2 {ECO:0000313|EMBL:AWN23812.1,
RC   ECO:0000313|Proteomes:UP000245368};
RA   Srinivasan S.;
RT   "Complete Genome Sequence of Deinococcus sp. strain 17bor-2.";
RL   Submitted (MAY-2018) 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; CP029494; AWN23812.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Z3JFJ9; -.
DR   KEGG; dez:DKM44_11725; -.
DR   OrthoDB; 9812068at2; -.
DR   Proteomes; UP000245368; Chromosome.
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   Protease {ECO:0000256|RuleBase:RU004404};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245368};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU004404}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..437
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016380645"
FT   DOMAIN          79..158
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
SQ   SEQUENCE   437 AA;  46441 MW;  F1382FE321E481B8 CRC64;
     MRKRLLLVSG ALAATAAVGY AQFVSYDTAD ITKTANGKAF VQLFGALHQL YLKPLDDNKL
     MNGAIKGMIA SLDDEFTYYV EAQANQTDQE DLTGEFFGIG IQLVASNADG TGAKVDTVFK
     TGSAVQGGVQ AGDVFLKIGD KDVSTLPLND VVRLVRGAKG TKVNITFGRG KSTYTVTLER
     QPVTIVSVEQ TVLPNNVGYI ALSTFYSDKV NEQFAAAVQN MKKKGITKLI LDLRDNGGGL
     LSSGVFVADQ FMQKGPIVSL RDGKGKTQVY DTAKNQPTDY TGQLVVLINK NSASASEIVA
     GALQDTKRAT ILGETSYGKG VAQTPVELVN GAQVRIVANE WLTPNGRQIQ KIGITPDVKV
     EDNRRPLPLN FSGSGVKAGS KLTLDVGGKA VEVVADKDGK FTYTAPPADQ PRSDVQGVAV
     VNPATDAELK AALQQFK
//
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