TA family: phd-doc
#OrganismLocus idToxinAntitoxinReplicon
1Bacillus clausii KSM-K161118 ABC1017ABC1016NC_006582
2Brucella melitensis bv. 1 str. 16M511 BMEI1376BMEI1375NC_003317
3Brucella suis 1330644 BR0557BR0558NC_004310
4Campylobacter jejuni RM12211512 CJE1100CJE1101NC_003912
5Candidatus Protochlamydia amoebophila UWE251389 pc1021pc1022NC_005861
6Candidatus Protochlamydia amoebophila UWE251391 pc1456pc1457NC_005861
7Chlorobium tepidum TLS298 CT0333CT0332NC_002932
8Corynebacterium diphtheriae NCTC 131291673 DIP0795DIP0796NC_002935
9Enterococcus faecalis V5831023 EF0379EF0380NC_004668
10Geobacillus kaustophilus HTA4261182 GK1846GK1845NC_006510
11Gloeobacter violaceus PCC 74211451 glr2735gsr2734NC_005125
12Lactobacillus acidophilus NCFM1668 LBA0031LBA0030NC_006814
13Methanosarcina mazei Go1589 MM_0549MM_0550NC_003901
14Nostoc sp. PCC 7120 (Anabaena sp. PCC 7120)454 alr0502alr0501NC_003272
15Pectobacterium atrosepticum SCRI10431099 ECA0253ECA0254NC_004547
16Salmonella enterica subsp. enterica serovar Typhimurium str. LT2442 STM3558STM3559NC_003197
17Salmonella enterica subsp. enterica serovar Typhi str. CT18823 STY1031STY1030NC_003198
18Salmonella enterica subsp. enterica serovar Typhi str. Ty2749 t1909t1910NC_004631
19Staphylococcus epidermidis RP62A1341 SERP1549SERP1550NC_002976
20Streptococcus pneumoniae TIGR4324 SP_0889SP_0888NC_003028
21Streptomyces avermitilis MA-4680 = NBRC 14893410 SAV_829SAV_830NC_003155
22Streptomyces avermitilis MA-4680 = NBRC 14893434 SAV_7087SAV_7086NC_003155
23Streptomyces coelicolor A3(2)559 SCO0412SCO0411NC_003888
24Streptomyces coelicolor A3(2)575 SCO5909SCO5908NC_003888
25Xanthomonas axonopodis pv. citri str. 306736 XAC1194XAC1195NC_003919
26Xanthomonas oryzae KACC103311622 XOO3444XOO3443NC_006834
27Yersinia pestis biovar Microtus str. 910011400 YP_1559YP_1560NC_005810
The phd/doc locus was firstly identified in Prophage P1, which is helpful for a genetical stability of P1. The doc (death on curing) gene encodes a toxin, Doc, and phd (prevent host death) encodes an antitoxin, Phd, that neutralizes Doc.
Conserved Domain
Accession No.NameRelation/involvement in TA lociReference
COG3654DocToxin of probable translational inhibitor systemPubMed:17678530
COG4118PhdAntitoxin to translational inhibitor DocPubMed:17678530
pfam05012DocToxin of probable translational inhibitor systemPubMed:17678530

Structure of DocH66Y in complex with the C-terminal domain of Phd [ PDB ID: 3DD7] [PudMed:18757857]
Structure of DocH66Y dimer. Doc of phage P1 adopts an incomplete Fic fold that is complemented by its antitoxin Phd. [ PDB ID: 3DD9]
Crystal structure of the P1 bacteriophage Doc toxin (F68S) in complex with the Phd antitoxin (L17M/V39A). Northeast Structural Genomics targets ER385-ER386 [ PDB ID: 3KH2] [PudMed:20696400]
(1) Gazit E et al. (1999) Stability and DNA binding of the phd protein of the phage P1 plasmid addictionsystem. J Biol Chem 274(5):2652-7. [PudMed:9915794] experimental
(2) Magnuson R et al. (1998) Corepression of the P1 addiction operon by Phd and Doc. J Bacteriol 180(23):6342-51. [PudMed:9829946] experimental
(3) Magnuson R et al. (1996) Autoregulation of the plasmid addiction operon of bacteriophage P1. J Biol Chem 271(31):18705-10. [PudMed:8702525] experimental
(4) Lehnherr H et al. (1993) Plasmid addiction genes of bacteriophage P1: doc, which causes cell death oncuring of prophage, and phd, which prevents host death when prophage isretained. J Mol Biol 233(3):414-28. [PudMed:8411153] experimental
(5) Lehnherr H et al. (1995) Addiction protein Phd of plasmid prophage P1 is a substrate of the ClpXP serineprotease of Escherichia coli. Proc Natl Acad Sci U S A 92(8):3274-7. [PudMed:7724551] experimental
(6) Arbing MA et al. (2010) Crystal structures of Phd-Doc, HigA, and YeeU establish multiple evolutionary links between microbial growth-regulating toxin-antitoxin systems. Structure 18(8):996-1010. [PudMed:20696400] 3D_structure
(7) Garcia-Pino A et al. (2010) Purification and crystallization of Phd, the antitoxin of the phd/doc operon. Acta Crystallogr Sect F Struct Biol Cryst Commun 66(Pt 2):167-71 . [PudMed:20124714] 3D_structure
(8) Garcia-Pino A et al. (2008) Crystallization of Doc and the Phd-Doc toxin-antitoxin complex. Acta Crystallogr Sect F Struct Biol Cryst Commun 64(Pt 11):1034-8. [PudMed:18997335] 3D_structure
(9) Garcia-Pino A et al. (2008) Doc of prophage P1 is inhibited by its antitoxin partner Phd through foldcomplementation. J Biol Chem 283(45):30821-7. [PudMed:18757857] 3D_structure
(10) Liu M et al. (2008) Bacterial addiction module toxin Doc inhibits translation elongation through itsassociation with the 30S ribosomal subunit. Proc Natl Acad Sci U S A 105(15):5885-90. [PudMed:18398006] experimental
(11) Fico S et al. (2006) TasA-tasB, a new putative toxin-antitoxin (TA) system from Bacillusthuringiensis pGI1 plasmid is a widely distributed composite mazE-doc TA system. BMC Genomics 7:259. [PudMed:17038198]
(12) Cherny I et al. (2005) The YoeB toxin is a folded protein that forms a physical complex with theunfolded YefM antitoxin. Implications for a structural-based differentialstability of toxin-antitoxin systems. J Biol Chem 280(34):30063-72. [PudMed:15980067] experimental
(13) Zhao X et al. (2005) Percolation of the phd repressor-operator interface. J Bacteriol 187(6):1901-12. [PudMed:15743936] experimental
(14) McKinley JE et al. (2005) Characterization of the Phd repressor-antitoxin boundary. J Bacteriol 187(2):765-70. [PudMed:15629948] experimental
(15) Smith JA et al. (2004) Modular organization of the Phd repressor/antitoxin protein. J Bacteriol 186(9):2692-8. [PudMed:15090510] experimental
(16) Pomerantsev AP et al. (2001) Genetic organization of the Francisella plasmid pFNL10. Plasmid 46(3):210-22. [PudMed:11735370]
(17) Gazit E et al. (1999) The Doc toxin and Phd antidote proteins of the bacteriophage P1 plasmidaddiction system form a heterotrimeric complex. J Biol Chem 274(24):16813-8. [PudMed:10358024] experimental
experimental experimental literature
3D_structure protein structure literature