ID   XRE_PSEPK               Reviewed;         159 AA.
AC   Q88K58;
DT   13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Antitoxin Xre {ECO:0000303|PubMed:30315706};
GN   Name=xre {ECO:0000303|PubMed:30315706}; OrderedLocusNames=PP_2433;
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA   Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA   Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA   Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA   Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(2002).
RN   [2] {ECO:0007744|PDB:6GW6}
RP   X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 11-159 IN COMPLEX WITH TOXIN,
RP   PROBABLE FUNCTION AS AN ANTITOXIN, SUBUNIT, DOMAIN, AND PROBABLE
RP   DNA-BINDING.
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=30315706; DOI=10.1111/mmi.14150;
RA   Skjerning R.B., Senissar M., Winther K.S., Gerdes K., Brodersen D.E.;
RT   "The RES domain toxins of RES-Xre toxin-antitoxin modules induce cell
RT   stasis by degrading NAD+.";
RL   Mol. Microbiol. 111:221-236(2019).
CC   -!- FUNCTION: Probable antitoxin component of a type II toxin-antitoxin
CC       (TA) system. In vivo probably neutralizes the toxic effect of cognate
CC       toxin Res. {ECO:0000305|PubMed:30315706}.
CC   -!- SUBUNIT: Homodimer. Forms a complex with cognate toxin Res; the 2 toxin
CC       molecules dimerize and each contacts an Xre homodimer. Most Res-Xre
CC       contacts are between the antitoxin molecule closest to the toxin.
CC       {ECO:0000269|PubMed:30315706}.
CC   -!- DOMAIN: The homodimer can be superposed on the Cro helix-turn-helix
CC       binding domain, suggesting it probably binds DNA and can act as a
CC       transcription factor as is often the case with antitoxins in type II TA
CC       systems (Probable). The C-terminus of the antitoxin inserts into the
CC       putative NAD(+)-binding site of toxin Res, blocking access to the
CC       active site (PubMed:30315706). {ECO:0000269|PubMed:30315706,
CC       ECO:0000305|PubMed:30315706}.
CC   -!- SIMILARITY: Belongs to the MbcA/ParS/Xre antitoxin family.
CC       {ECO:0000305}.
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DR   EMBL; AE015451; AAN68045.1; -; Genomic_DNA.
DR   RefSeq; NP_744581.1; NC_002947.4.
DR   PDB; 6GW6; X-ray; 2.21 A; B/C/E/F=11-159.
DR   PDBsum; 6GW6; -.
DR   AlphaFoldDB; Q88K58; -.
DR   SMR; Q88K58; -.
DR   STRING; 160488.PP_2433; -.
DR   EnsemblBacteria; AAN68045; AAN68045; PP_2433.
DR   KEGG; ppu:PP_2433; -.
DR   PATRIC; fig|160488.4.peg.2578; -.
DR   eggNOG; COG5642; Bacteria.
DR   HOGENOM; CLU_109353_5_0_6; -.
DR   OMA; FVIPQRT; -.
DR   PhylomeDB; Q88K58; -.
DR   BioCyc; PPUT160488:G1G01-2598-MON; -.
DR   Proteomes; UP000000556; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   InterPro; IPR011979; Antitox_Xre.
DR   InterPro; IPR024467; Xre/MbcA/ParS-like_toxin-bd.
DR   Pfam; PF09722; DUF2384; 1.
DR   TIGRFAMs; TIGR02293; TAS_TIGR02293; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA-binding; Reference proteome; Toxin-antitoxin system.
FT   CHAIN           1..159
FT                   /note="Antitoxin Xre"
FT                   /id="PRO_0000448602"
FT   HELIX           12..15
FT                   /evidence="ECO:0007829|PDB:6GW6"
FT   HELIX           17..32
FT                   /evidence="ECO:0007829|PDB:6GW6"
FT   HELIX           40..49
FT                   /evidence="ECO:0007829|PDB:6GW6"
FT   HELIX           53..61
FT                   /evidence="ECO:0007829|PDB:6GW6"
FT   HELIX           67..73
FT                   /evidence="ECO:0007829|PDB:6GW6"
FT   HELIX           76..84
FT                   /evidence="ECO:0007829|PDB:6GW6"
FT   HELIX           91..111
FT                   /evidence="ECO:0007829|PDB:6GW6"
FT   HELIX           114..121
FT                   /evidence="ECO:0007829|PDB:6GW6"
FT   TURN            126..130
FT                   /evidence="ECO:0007829|PDB:6GW6"
FT   HELIX           134..138
FT                   /evidence="ECO:0007829|PDB:6GW6"
FT   HELIX           140..155
FT                   /evidence="ECO:0007829|PDB:6GW6"
SQ   SEQUENCE   159 AA;  18026 MW;  F2E5B97F78074F53 CRC64;
     MSANAEKEHA MLAEVLRDNG YHEYRARLQA LLDIPELASD FEIHTRITDG FAATWLVKLT
     ERGVLTPVER DQIIPLRTLK SRIERDQPLT VDESDRLFRS AHITAMAEAV FGEAGKAKRW
     LSKPKERFSG LTPMQMLTTQ QGTTQVEEML LQIAEGYGL