PARD_ECOLX
ID PARD_ECOLX Reviewed; 83 AA.
AC P22995;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Antitoxin ParD;
GN Name=parD;
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].
RC PLASMID=IncP-alpha RP4;
RX PubMed=8387603; DOI=10.1006/jmbi.1993.1228;
RA Kholodii G.Y., Yurieva O.V., Lomovskaya O.L., Gorlenko Z.M., Mindlin S.Z.,
RA Nikiforov V.G.;
RT "Tn5053, a mercury resistance transposon with integron's ends.";
RL J. Mol. Biol. 230:1103-1107(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN PLASMID PARTITIONING, AND
RP TRANSCRIPTIONAL REGULATION.
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 [4]
RP DNA-BINDING, SUBUNIT, AND MUTAGENESIS OF GLN-12.
RX PubMed=8262949; DOI=10.1016/s0021-9258(19)74224-0;
RA Roberts R.C., Spangler C., Helinski D.R.;
RT "Characteristics and significance of DNA binding activity of plasmid
RT stabilization protein ParD from the broad host-range plasmid RK2.";
RL J. Biol. Chem. 268:27109-27117(1993).
RN [5]
RP FUNCTION AS AN ANTITOXIN.
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 [6]
RP FUNCTION AS AN ANTITOXIN, SUBUNIT, AND INTERACTION WITH PARE.
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 [7]
RP MASS SPECTROMETRY, AND SUBUNIT.
RX PubMed=10661868; DOI=10.1515/bc.1999.181;
RA Oberer M., Lindner H., Glatter O., Kratky C., Keller W.;
RT "Thermodynamic properties and DNA binding of the ParD protein from the
RT broad host-range plasmid RK2/RP4 killing system.";
RL Biol. Chem. 380:1413-1420(1999).
RN [8]
RP FUNCTION AS AN ANTI-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).
RN [9]
RP PRELIMINARY STRUCTURE BY NMR.
RX PubMed=11743881; DOI=10.1042/0264-6021:3610041;
RA Oberer M., Zangger K., Prytulla S., Keller W.;
RT "The anti-toxin ParD of plasmid RK2 consists of two structurally distinct
RT moieties and belongs to the ribbon-helix-helix family of DNA-binding
RT proteins.";
RL Biochem. J. 361:41-47(2002).
RN [10]
RP STRUCTURE BY NMR, AND SUBUNIT.
RX PubMed=17656583; DOI=10.1110/ps.062680707;
RA Oberer M., Zangger K., Gruber K., Keller W.;
RT "The solution structure of ParD, the antidote of the ParDE toxin antitoxin
RT module, provides the structural basis for DNA and toxin binding.";
RL Protein Sci. 16:1676-1688(2007).
CC -!- FUNCTION: Antitoxin component of a type II toxin-antitoxin (TA) system
CC involved in plasmid partition. Inhibits the anti-DNA gyrase activity of
CC toxin ParE; reverses and restores gyrase catalytic activity in vitro.
CC The parDE operon alone is capable of stabilizing an RK2-derived
CC minireplicon under defined growth conditions in several different Gram-
CC negative bacteria. It does so by the post-segregational killing (PSK)
CC of plasmid-free cells, also referred to as a plasmid addiction system.
CC Binds its own promoter, autorepressing it; gentically only ParD is
CC required for full autorepression. {ECO:0000269|PubMed:12010492,
CC ECO:0000269|PubMed:1459960, ECO:0000269|PubMed:8133518,
CC ECO:0000269|PubMed:8631720}.
CC -!- SUBUNIT: Forms a homodimer in solution, interacts with ParD, possibly
CC as a ParD(2)-ParE(2) heterotetramer, which neutralizes the toxic
CC activity of ParE. Both the homodimer and heterotetramer bind DNA,
CC although genetically only ParD is required for full operon repression.
CC Another study has shown that it is a ParD homotetramer that binds the
CC promoter (PubMed:10661868). {ECO:0000269|PubMed:10661868,
CC ECO:0000269|PubMed:17656583, ECO:0000269|PubMed:8262949,
CC ECO:0000269|PubMed:8631720}.
CC -!- MASS SPECTROMETRY: Mass=9126; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10661868};
CC -!- MISCELLANEOUS: Plasmid IncP-alpha RK2 is maintained at 5-8 copies per
CC chromosome.
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DR EMBL; L40585; AAA98334.1; -; Genomic_DNA.
DR EMBL; M59825; AAA26418.1; -; Genomic_DNA.
DR EMBL; L03728; AAA91498.1; -; Genomic_DNA.
DR EMBL; L05507; AAA92774.1; -; Genomic_DNA.
DR PIR; A37141; A37141.
DR PIR; S32830; S32830.
DR RefSeq; WP_011205807.1; NZ_NJTR01000057.1.
DR PDB; 2AN7; NMR; -; A/B=1-83.
DR PDBsum; 2AN7; -.
DR AlphaFoldDB; P22995; -.
DR BMRB; P22995; -.
DR SMR; P22995; -.
DR DIP; DIP-27657N; -.
DR EvolutionaryTrace; P22995; -.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0030541; P:plasmid partitioning; IGI:UniProtKB.
DR GO; GO:0051290; P:protein heterotetramerization; IDA:UniProtKB.
DR DisProt; DP00833; -.
DR Gene3D; 6.10.180.10; -; 1.
DR InterPro; IPR022789; ParD.
DR InterPro; IPR038296; ParD_sf.
DR InterPro; IPR010985; Ribbon_hlx_hlx.
DR Pfam; PF09386; ParD; 1.
DR SUPFAM; SSF47598; SSF47598; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Plasmid; Plasmid partition; Repressor;
KW Toxin-antitoxin system; Transcription; Transcription regulation.
FT CHAIN 1..83
FT /note="Antitoxin ParD"
FT /id="PRO_0000068411"
FT MUTAGEN 12
FT /note="Q->IDLDQ: Binds DNA very poorly, plasmid stability
FT maintained."
FT /evidence="ECO:0000269|PubMed:8262949"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:2AN7"
FT HELIX 10..23
FT /evidence="ECO:0007829|PDB:2AN7"
FT HELIX 27..34
FT /evidence="ECO:0007829|PDB:2AN7"
FT HELIX 42..52
FT /evidence="ECO:0007829|PDB:2AN7"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:2AN7"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:2AN7"
SQ SEQUENCE 83 AA; 9103 MW; FB6A223D3D7DE523 CRC64;
MSRLTIDMTD QQHQSLKALA ALQGKTIKQY ALERLFPGDA DADQAWQELK TMLGNRINDG
LAGKVSTKSV GEILDEELSG DRA
