ID   PARE_ECOLX              Reviewed;         103 AA.
AC   Q79EC5;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 38.
DE   RecName: Full=Toxin ParE;
DE   AltName: Full=Gyrase inhibitor ParE;
GN   Name=parE;
OS   Escherichia coli.
OG   Plasmid IncP-alpha RP4, and Plasmid IncP-alpha RK2.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=IncP-alpha RP4;
RX   PubMed=2172207; DOI=10.1128/jb.172.11.6194-6203.1990;
RA   Gerlitz M., Hrabak O., Schwab H.;
RT   "Partitioning of broad-host-range plasmid RP4 is a complex system involving
RT   site-specific recombination.";
RL   J. Bacteriol. 172:6194-6203(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN PLASMID PARTITIONING, AND
RP   DISRUPTION PHENOTYPE.
RC   PLASMID=IncP-alpha RK2;
RX   PubMed=1459960; DOI=10.1128/jb.174.24.8119-8132.1992;
RA   Roberts R.C., Helinski D.R.;
RT   "Definition of a minimal plasmid stabilization system from the broad-host-
RT   range plasmid RK2.";
RL   J. Bacteriol. 174:8119-8132(1992).
RN   [3]
RP   FUNCTION AS A TOXIN.
RX   PubMed=8133518; DOI=10.1006/jmbi.1994.1207;
RA   Roberts R.C., Strom A.R., Helinski D.R.;
RT   "The parDE operon of the broad-host-range plasmid RK2 specifies growth
RT   inhibition associated with plasmid loss.";
RL   J. Mol. Biol. 237:35-51(1994).
RN   [4]
RP   FUNCTION AS A TOXIN, SUBUNIT, AND INTERACTION WITH PARD.
RC   PLASMID=IncP-alpha RK2;
RX   PubMed=8631720; DOI=10.1128/jb.178.5.1420-1429.1996;
RA   Johnson E.P., Strom A.R., Helinski D.R.;
RT   "Plasmid RK2 toxin protein ParE: purification and interaction with the ParD
RT   antitoxin protein.";
RL   J. Bacteriol. 178:1420-1429(1996).
RN   [5]
RP   FUNCTION AS A DNA GYRASE INHIBITOR.
RC   PLASMID=IncP-alpha RK2;
RX   PubMed=12010492; DOI=10.1046/j.1365-2958.2002.02921.x;
RA   Jiang Y., Pogliano J., Helinski D.R., Konieczny I.;
RT   "ParE toxin encoded by the broad-host-range plasmid RK2 is an inhibitor of
RT   Escherichia coli gyrase.";
RL   Mol. Microbiol. 44:971-979(2002).
CC   -!- FUNCTION: Toxin component of a type II toxin-antitoxin (TA) system
CC       involved in plasmid partition. Acts by inhibiting DNA gyrase,
CC       converting supercoiled plasmid DNA into a singly cleaved linear form in
CC       an ATP-dependent fashion. To do so it probably interacts with one of
CC       the gyrase subunits. Gyrase inhibition is prevented by antitoxin ParD,
CC       and is reversed in vitro by incubation with ParD. In cells that have
CC       lost the plasmid filamentation and growth inhibition occur; this is
CC       suppressed when ParD is supplied in trans. The parDE operon alone is
CC       capable of stabilizing an RK2-derived minireplicon under defined growth
CC       conditions in several different Gram-negative bacteria. It does so by
CC       the post-segregational killing (PSK) of plasmid-free cells, also
CC       referred to as a plasmid addiction system.
CC       {ECO:0000269|PubMed:12010492, ECO:0000269|PubMed:1459960,
CC       ECO:0000269|PubMed:8133518, ECO:0000269|PubMed:8631720}.
CC   -!- SUBUNIT: Probably forms a homodimer in solution, interacts with ParD,
CC       possibly as a ParD(2)-ParE(2) heterotetramer, which neutralizes the
CC       toxic activity of ParE. The heterotetramer binds DNA, but not ParE
CC       alone. {ECO:0000269|PubMed:8631720}.
CC   -!- DISRUPTION PHENOTYPE: Loss of this gene blocks plasmid stabilizing
CC       ability. {ECO:0000269|PubMed:1459960}.
CC   -!- MISCELLANEOUS: Plasmid IncP-alpha RK2 is maintained at 5-8 copies per
CC       chromosome.
CC   -!- SIMILARITY: Belongs to the RelE toxin family. {ECO:0000305}.
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DR   EMBL; L05507; AAA92775.1; -; Genomic_DNA.
DR   RefSeq; WP_011205808.1; NZ_NJTR01000057.1.
DR   AlphaFoldDB; Q79EC5; -.
DR   SMR; Q79EC5; -.
DR   BindingDB; Q79EC5; -.
DR   ChEMBL; CHEMBL3313836; -.
DR   GO; GO:0008657; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) inhibitor activity; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0030541; P:plasmid partitioning; IGI:UniProtKB.
DR   GO; GO:0051290; P:protein heterotetramerization; IDA:UniProtKB.
DR   Gene3D; 3.30.2310.20; -; 1.
DR   InterPro; IPR007712; RelE/ParE_toxin.
DR   InterPro; IPR035093; RelE/ParE_toxin_dom_sf.
DR   Pfam; PF05016; ParE_toxin; 1.
PE   1: Evidence at protein level;
KW   Plasmid; Plasmid partition; Toxin-antitoxin system.
FT   CHAIN           1..103
FT                   /note="Toxin ParE"
FT                   /id="PRO_0000408371"
SQ   SEQUENCE   103 AA;  11716 MW;  DCDC13A6056E7132 CRC64;
     MTAYILTAEA EADLRGIIRY TRREWGAAQV RRYIAKLEQG IARLAAGEGP FKDMSELFPA
     LRMARCEHHY VFCLPRAGEP ALVVAILHER MDLMTRLADR LKG