TA family: parDE
#OrganismLocus idToxinAntitoxinReplicon
1Bartonella henselae str. Houston-11649 BH07010BH07020NC_005956
2Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 12226261 BLON_RS04730BLON_RS04725NC_011593
3Caulobacter crescentus CB15233 CC_2984CC_2985NC_002696
4Caulobacter crescentus CB15228 experimental CC_0873CC_0874NC_002696
5Coxiella burnetii RSA 493317 CBU_0644CBU_0645NC_002971
6Escherichia coli O157:H7 str. EDL933192 Z0510Z0509NC_002655
7Escherichia coli O157:H7 str. Sakai1004 ECs0462ECs0461NC_002695
8Geobacter sulfurreducens PCA1530 GSU0055GSU0056NC_002939
9Geobacter uraniireducens Rf43993 Gura_3915Gura_3916NC_009483
10Gloeobacter violaceus PCC 74211469 gsl4116gsl4117NC_005125
11Gloeobacter violaceus PCC 74211437 gll1910gsl1911NC_005125
12Gloeobacter violaceus PCC 74211432 glr1691gsr1690NC_005125
13Idiomarina loihiensis L2TR1312 IL0911IL0912NC_006512
14Idiomarina loihiensis L2TR1314 IL1289IL1290NC_006512
15Mesorhizobium loti MAFF303099205 msr1301mlr1300NC_002678
16Mesorhizobium loti MAFF303099214 msl3420msl3422NC_002678
17Mycobacterium bovis AF2122/971150 Mb1994cMb1995cNC_002945
18Mycobacterium tuberculosis CDC1551274 MT2200MT2201NC_002755
19Mycobacterium tuberculosis CDC1551263 MT2008MT2009NC_002755
20Mycobacterium tuberculosis H37Rv105 experimental Rv1959cRv1960cNC_000962
21Nitrosomonas europaea ATCC 19718890 NE0261NE0262NC_004757
22Nitrosomonas europaea ATCC 19718938 NE2114NE2115NC_004757
23Nitrosomonas europaea ATCC 19718932 NE1591NE1592NC_004757
24Nitrosomonas europaea ATCC 19718899 NE0552NE0551NC_004757
25Pectobacterium atrosepticum SCRI10431109 ECA2241ECA2242NC_004547
26Pectobacterium atrosepticum SCRI10431107 ECA1466ECA1467NC_004547
27Photorhabdus luminescens subsp. laumondii TTO11225 plu2372plu2371NC_005126
28Photorhabdus luminescens subsp. laumondii TTO11250 plu4785plu4784NC_005126
29Photorhabdus luminescens subsp. laumondii TTO11215 plu2251plu2250NC_005126
30Photorhabdus luminescens subsp. laumondii TTO11214 plu2210plu2211NC_005126
31Photorhabdus luminescens subsp. laumondii TTO11192 plu0625plu0624NC_005126
32Photorhabdus luminescens subsp. laumondii TTO11188 plu0251plu0252NC_005126
33Photorhabdus luminescens subsp. laumondii TTO11218 plu2269plu2270NC_005126
34Photorhabdus luminescens subsp. laumondii TTO11234 plu3316plu3315NC_005126
35Pseudomonas syringae pv. tomato str. DC30001051 PSPTO_0241PSPTO_0240NC_004578
36Rhodopirellula baltica SH 11036 RB10182RB10184NC_005027
37Rhodopirellula baltica SH 11035 RB4643RB4642NC_005027
38Shewanella oneidensis MR-1659 SO_1444SO_1445NC_004347
39Streptococcus agalactiae 2603V/R631 SAG0228SAG0229NC_004116
40Streptococcus agalactiae NEM316887 gbs0221gbs0222NC_004368
41Streptococcus pyogenes M1 GAS747 SPy_1927SPy_1926NC_002737
42Streptococcus pyogenes MGAS103941639 M6_Spy1650M6_Spy1649NC_006086
43Streptococcus pyogenes MGAS103941638 M6_Spy0490M6_Spy0488NC_006086
44Streptococcus pyogenes MGAS315625 SpyM3_1662SpyM3_1661NC_004070
45Streptococcus pyogenes MGAS315619 SpyM3_0394SpyM3_0393NC_004070
46Streptococcus pyogenes MGAS8232996 spyM18_0617spyM18_0616NC_003485
47Streptococcus pyogenes MGAS82321001 spyM18_1995spyM18_1994NC_003485
48Streptococcus pyogenes SSI-1714 SPs1660SPs1659NC_004606
49Streptococcus pyogenes SSI-1713 SPs1460SPs1461NC_004606
50Vibrio cholerae O1 biovar El Tor str. N16961170 experimental VCA0385VCA0386NC_002506
51Vibrio cholerae O1 biovar El Tor str. N16961164 experimental VCA0311VCA0312NC_002506
52Vibrio cholerae O1 biovar El Tor str. N16961169 experimental VCA0359VCA0360NC_002506
53Vibrio parahaemolyticus RIMD 2210633707 VP1885VP1886NC_004603
54Vibrio parahaemolyticus RIMD 2210633706 VP1884VP1885NC_004603
55Vibrio vulnificus CMCP6690 VV1_2525VV1_2526NC_004459
56Xanthomonas axonopodis pv. citri str. 306731 XAC0081XAC0080NC_003919
57Xanthomonas axonopodis pv. citri str. 306741 XAC2428XAC2429NC_003919
58Xanthomonas oryzae KACC103311620 XOO0163XOO0164NC_006834
59Xylella fastidiosa 9a5c159 XF2070XF2071NC_002488
60Xylella fastidiosa 9a5c157 XF2032XF2031NC_002488
61Xylella fastidiosa Temecula1778 PD0960PD0961NC_004556

experimental Data derived from experimental literature
The parDE locus was firstly identified adjacent to the site-specific resolution system of the plasmid RK2.
Conserved Domain
Accession No.NameRelation/involvement in TA lociReference
COG3668ParEToxin of plasmid stabilization systemPubMed:17678530
COG3609COG3609CopG/Arc/MetJ DNA-binding domain, present in RelB, ParD, VapBC and CcdA antitoxinsPubMed:17678530

A Conserved Mode Of Protein Recognition And Binding In A ParD-ParE Toxin-Antitoxin Complex. [ PDB ID: 3KXE] [PudMed:20143871]
Solution structure of the bacterial antidote ParD [ PDB ID: 2AN7] [PudMed:17656583]
(1) Easter CL et al. (1997) Contribution of different segments of the par region to stable maintenance ofthe broad-host-range plasmid RK2. J Bacteriol 179(20):6472-9. [PudMed:9335298] experimental
(2) Johnson EP et al. (1996) Plasmid RK2 toxin protein ParE: purification and interaction with the ParD antitoxin protein. J Bacteriol 178(5):1420-9. [PudMed:8631720] experimental
(3) Jensen RB et al. (1995) Comparison of ccd of F, parDE of RP4, and parD of R1 using a novel conditionalreplication control system of plasmid R1. Mol Microbiol 17(2):211-20. [PudMed:7494470] experimental
(4) Jensen RB et al. (1995) Programmed cell death in bacteria: proteic plasmid stabilization systems. Mol Microbiol 17(2):205-10. [PudMed:7494469]
(5) Yuan J et al. (2011) The three vibrio cholerae chromosome II-encoded ParE toxins degrade chromosome I following loss of chromosome II. J Bacteriol. 193(3):611-9. [PudMed:21115657] experimental
(6) Barbosa LC et al. (2010) Function inferences from a molecular structural model of bacterial ParE toxin. Bioinformation. 4(10):438-40. [PudMed:20975905] in_silico
(7) Yuan J et al. (2010) Vibrio cholerae ParE2 poisons DNA gyrase via a mechanism distinct from other gyrase inhibitors. J Biol Chem. 285(51):40397-408. [PudMed:20952390] experimental
(8) Dalton KM et al. (2010) A conserved mode of protein recognition and binding in a ParD-ParE toxin-antitoxin complex. Biochemistry 49(10):2205-15. [PudMed:20143871] 3D_structure
(9) Oberer M et al. (2007) The solution structure of ParD, the antidote of the ParDE toxin antitoxinmodule, provides the structural basis for DNA and toxin binding. Protein Sci 16(8):1676-88. [PudMed:17656583] 3D_structure
(10) Gvakharia BO et al. (2007) Global transcriptional response of Nitrosomonas europaea to chloroform and chloromethane. Appl Environ Microbiol. 73(10):3440-5. [PudMed:17369330] experimental
(11) Jiang Y et al. (2002) ParE toxin encoded by the broad-host-range plasmid RK2 is an inhibitor of Escherichia coli gyrase. Mol Microbiol 44(4):971-9. [PudMed:12010492] experimental
(12) Oberer M et al. (2002) The anti-toxin ParD of plasmid RK2 consists of two structurally distinctmoieties and belongs to the ribbon-helix-helix family of DNA-binding proteins. Biochem J 361(Pt 1):41-7. [PudMed:11743881] experimental
(13) Cooper TF et al. (2000) Postsegregational killing does not increase plasmid stability but acts tomediate the exclusion of competing plasmids. Proc Natl Acad Sci U S A 97(23):12643-8. [PudMed:11058151] experimental
(14) Oberer M et al. (1999) Thermodynamic properties and DNA binding of the ParD protein from the broadhost-range plasmid RK2/RP4 killing system. Biol Chem 380(12):1413-20. [PudMed:10661868] experimental
experimental experimental literature
in_silico in silico analysis literature
3D_structure protein structure literature