ID   PARD1_CAUVC             Reviewed;          88 AA.
AC   P58091;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Antitoxin ParD1;
GN   Name=parD1; OrderedLocusNames=CC_0874;
OS   Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=190650;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19089 / CB15;
RX   PubMed=11259647; DOI=10.1073/pnas.061029298;
RA   Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA   Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA   Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA   Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA   Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA   Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT   "Complete genome sequence of Caulobacter crescentus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
RN   [2]
RP   POSSIBLE FUNCTION.
RC   STRAIN=ATCC 19089 / CB15;
RX   PubMed=15718296; DOI=10.1093/nar/gki201;
RA   Pandey D.P., Gerdes K.;
RT   "Toxin-antitoxin loci are highly abundant in free-living but lost from
RT   host-associated prokaryotes.";
RL   Nucleic Acids Res. 33:966-976(2005).
RN   [3]
RP   FUNCTION AS AN ANTITOXIN, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 19089 / CB15;
RX   PubMed=20487277; DOI=10.1111/j.1365-2958.2010.07207.x;
RA   Fiebig A., Castro Rojas C.M., Siegal-Gaskins D., Crosson S.;
RT   "Interaction specificity, toxicity and regulation of a paralogous set of
RT   ParE/RelE-family toxin-antitoxin systems.";
RL   Mol. Microbiol. 77:236-251(2010).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS), AND SUBUNIT.
RC   STRAIN=ATCC 19089 / CB15;
RX   PubMed=20143871; DOI=10.1021/bi902133s;
RA   Dalton K.M., Crosson S.;
RT   "A conserved mode of protein recognition and binding in a ParD-ParE toxin-
RT   antitoxin complex.";
RL   Biochemistry 49:2205-2215(2010).
CC   -!- FUNCTION: Antitoxin component of a type II toxin-antitoxin (TA) system.
CC       Neutralizes the effect of cognate toxin ParE1, but no other RelE or
CC       ParE toxin. May act as a DNA gyrase inhibitor (By similarity).
CC       {ECO:0000250, ECO:0000269|PubMed:20487277}.
CC   -!- SUBUNIT: Homodimer in solution, forms a ParD1(2)-ParE1(2)
CC       heterotetramer. {ECO:0000269|PubMed:20143871}.
CC   -!- DISRUPTION PHENOTYPE: Cannot be disrupted, suggesting it is a
CC       functional antitoxin. No visible phenotype when the parDE1 operon is
CC       deleted. {ECO:0000269|PubMed:20487277}.
CC   -!- SIMILARITY: Belongs to the ParD antitoxin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE005673; AAK22859.1; -; Genomic_DNA.
DR   PIR; G87357; G87357.
DR   RefSeq; NP_419691.1; NC_002696.2.
DR   RefSeq; WP_010918759.1; NC_002696.2.
DR   PDB; 3KXE; X-ray; 2.60 A; C/D=1-88.
DR   PDBsum; 3KXE; -.
DR   AlphaFoldDB; P58091; -.
DR   SMR; P58091; -.
DR   STRING; 190650.CC_0874; -.
DR   EnsemblBacteria; AAK22859; AAK22859; CC_0874.
DR   KEGG; ccr:CC_0874; -.
DR   PATRIC; fig|190650.5.peg.887; -.
DR   eggNOG; COG3609; Bacteria.
DR   HOGENOM; CLU_144805_2_0_5; -.
DR   OMA; HWETFIK; -.
DR   BioCyc; CAULO:CC0874-MON; -.
DR   EvolutionaryTrace; P58091; -.
DR   Proteomes; UP000001816; Chromosome.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0051290; P:protein heterotetramerization; IDA:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 6.10.10.120; -; 1.
DR   InterPro; IPR022789; ParD.
DR   InterPro; IPR038296; ParD_sf.
DR   InterPro; IPR010985; Ribbon_hlx_hlx.
DR   PANTHER; PTHR36582; PTHR36582; 1.
DR   Pfam; PF03693; ParD_antitoxin; 1.
DR   SUPFAM; SSF47598; SSF47598; 1.
DR   TIGRFAMs; TIGR02606; antidote_CC2985; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Reference proteome; Toxin-antitoxin system.
FT   CHAIN           1..88
FT                   /note="Antitoxin ParD1"
FT                   /id="PRO_0000216351"
FT   STRAND          6..8
FT                   /evidence="ECO:0007829|PDB:3KXE"
FT   HELIX           12..22
FT                   /evidence="ECO:0007829|PDB:3KXE"
FT   TURN            23..25
FT                   /evidence="ECO:0007829|PDB:3KXE"
FT   HELIX           30..60
FT                   /evidence="ECO:0007829|PDB:3KXE"
FT   STRAND          63..66
FT                   /evidence="ECO:0007829|PDB:3KXE"
FT   HELIX           69..78
FT                   /evidence="ECO:0007829|PDB:3KXE"
SQ   SEQUENCE   88 AA;  9636 MW;  571769967C364F77 CRC64;
     MASKNTSVVL GDHFQAFIDS QVADGRYGSA SEVIRAGLRL LEENEAKLAA LRAALIEGEE
     SGFIEDFDFD AFIEERSRAS APQGFHEE