ID   RES_PSEPK               Reviewed;         145 AA.
AC   Q88K57;
DT   13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Toxin Res {ECO:0000303|PubMed:30315706};
DE            EC=2.4.2.- {ECO:0000250|UniProtKB:P9WLP9};
GN   Name=res {ECO:0000303|PubMed:30315706}; OrderedLocusNames=PP_2434;
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) IN COMPLEX WITH ANTITOXIN, FUNCTION
RP   AS A TOXIN, EXPRESSION IN E.COLI, AND SUBUNIT.
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: Toxic component of a type II toxin-antitoxin (TA) system.
CC       Expression in E.coli inhibits cell growth. In vivo it is probably
CC       neutralized by cognate antitoxin Xre; this has not been shown upon
CC       expression in E.coli (PubMed:30315706). Probably depletes intracellular
CC       NAD(+) (By similarity). {ECO:0000250|UniProtKB:Q7N4H9,
CC       ECO:0000269|PubMed:30315706}.
CC   -!- SUBUNIT: Homodimer. Forms a complex with cognate antitoxin Xre; the 2
CC       toxin molecules dimerize and each contacts an Xre homodimer. Most Res-
CC       Xre contacts are between the antitoxin molecule closest to the toxin.
CC       {ECO:0000269|PubMed:30315706}.
CC   -!- SIMILARITY: Belongs to the MbcT/ParT/Res family. {ECO:0000305}.
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DR   EMBL; AE015451; AAN68046.1; -; Genomic_DNA.
DR   RefSeq; NP_744582.1; NC_002947.4.
DR   RefSeq; WP_003250527.1; NC_002947.4.
DR   PDB; 6GW6; X-ray; 2.21 A; A/D=1-145.
DR   PDBsum; 6GW6; -.
DR   AlphaFoldDB; Q88K57; -.
DR   SMR; Q88K57; -.
DR   STRING; 160488.PP_2434; -.
DR   EnsemblBacteria; AAN68046; AAN68046; PP_2434.
DR   KEGG; ppu:PP_2434; -.
DR   PATRIC; fig|160488.4.peg.2579; -.
DR   eggNOG; COG5654; Bacteria.
DR   HOGENOM; CLU_133611_0_1_6; -.
DR   OMA; VTYCATS; -.
DR   PhylomeDB; Q88K57; -.
DR   BioCyc; PPUT160488:G1G01-2599-MON; -.
DR   Proteomes; UP000000556; Chromosome.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR014914; RES_dom.
DR   Pfam; PF08808; RES; 1.
DR   SMART; SM00953; RES; 1.
PE   1: Evidence at protein level;
KW   3D-structure; NAD; Nucleotidyltransferase; Reference proteome;
KW   Toxin-antitoxin system; Transferase.
FT   CHAIN           1..145
FT                   /note="Toxin Res"
FT                   /id="PRO_0000448607"
FT   STRAND          2..8
FT                   /evidence="ECO:0007829|PDB:6GW6"
FT   STRAND          10..12
FT                   /evidence="ECO:0007829|PDB:6GW6"
FT   HELIX           15..18
FT                   /evidence="ECO:0007829|PDB:6GW6"
FT   STRAND          27..29
FT                   /evidence="ECO:0007829|PDB:6GW6"
FT   STRAND          32..37
FT                   /evidence="ECO:0007829|PDB:6GW6"
FT   HELIX           38..48
FT                   /evidence="ECO:0007829|PDB:6GW6"
FT   HELIX           53..55
FT                   /evidence="ECO:0007829|PDB:6GW6"
FT   STRAND          61..66
FT                   /evidence="ECO:0007829|PDB:6GW6"
FT   HELIX           83..85
FT                   /evidence="ECO:0007829|PDB:6GW6"
FT   HELIX           87..100
FT                   /evidence="ECO:0007829|PDB:6GW6"
FT   STRAND          104..109
FT                   /evidence="ECO:0007829|PDB:6GW6"
FT   STRAND          111..113
FT                   /evidence="ECO:0007829|PDB:6GW6"
FT   STRAND          117..121
FT                   /evidence="ECO:0007829|PDB:6GW6"
FT   HELIX           126..130
FT                   /evidence="ECO:0007829|PDB:6GW6"
FT   STRAND          132..136
FT                   /evidence="ECO:0007829|PDB:6GW6"
SQ   SEQUENCE   145 AA;  16022 MW;  F95428D597CDBD01 CRC64;
     MILWRISAYA DLSGTGGLRV SGRWHQAGRP VVYAATSPPG AMLEVLVHLE IDPEDFPTTM
     RLLRIELPDT VSQAQLPALQ PGWSAQPELT RTLGNRFLDD CSALLLPVPS AIMPSTTNYL
     FNPRHPQAQS AKIQVEDFTP DSRLF