PARE1_CAUVC
ID PARE1_CAUVC Reviewed; 96 AA.
AC Q9A9T8;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Toxin ParE1;
GN Name=parE1; OrderedLocusNames=CC_0873;
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 A TOXIN, MUTAGENESIS OF 87-GLN--ASN-96 AND 93-ALA--ASN-96, AND
RP 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: Toxic component of a type II toxin-antitoxin (TA) system. Its
CC toxic effect is neutralized by coexpression with cognate antitoxin
CC ParD1 but no other ParD or RelB antitoxin. Low levels of wild-type
CC toxin in the absence of antitoxin decreases the rate of cell growth,
CC and results in death or loss of colony formation abilities and greatly
CC elongated cells. Low levels of a mutant missing the last 4 residues
CC leads to loss of cell division while cell elongation continues.
CC {ECO:0000269|PubMed:20487277}.
CC -!- SUBUNIT: Forms a ParD1(2)-ParE1(2) heterotetramer.
CC {ECO:0000269|PubMed:20143871}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype when deleted singly or as
CC the parDE1 operon. {ECO:0000269|PubMed:20487277}.
CC -!- SIMILARITY: Belongs to the RelE toxin family. {ECO:0000305}.
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DR EMBL; AE005673; AAK22858.1; -; Genomic_DNA.
DR PIR; F87357; F87357.
DR RefSeq; NP_419690.1; NC_002696.2.
DR RefSeq; WP_010918758.1; NC_002696.2.
DR PDB; 3KXE; X-ray; 2.60 A; A/B=1-96.
DR PDBsum; 3KXE; -.
DR AlphaFoldDB; Q9A9T8; -.
DR SMR; Q9A9T8; -.
DR STRING; 190650.CC_0873; -.
DR DNASU; 941174; -.
DR EnsemblBacteria; AAK22858; AAK22858; CC_0873.
DR KEGG; ccr:CC_0873; -.
DR PATRIC; fig|190650.5.peg.886; -.
DR eggNOG; COG3668; Bacteria.
DR HOGENOM; CLU_147162_3_0_5; -.
DR OMA; RILHGRM; -.
DR BioCyc; CAULO:CC0873-MON; -.
DR EvolutionaryTrace; Q9A9T8; -.
DR Proteomes; UP000001816; Chromosome.
DR GO; GO:0051290; P:protein heterotetramerization; IDA:UniProtKB.
DR Gene3D; 3.30.2310.20; -; 1.
DR InterPro; IPR028344; ParE1/4.
DR InterPro; IPR007712; RelE/ParE_toxin.
DR InterPro; IPR035093; RelE/ParE_toxin_dom_sf.
DR Pfam; PF05016; ParE_toxin; 1.
DR PIRSF; PIRSF029218; ParE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Toxin-antitoxin system.
FT CHAIN 1..96
FT /note="Toxin ParE1"
FT /id="PRO_0000408368"
FT MUTAGEN 87..96
FT /note="Missing: No longer toxic; protein is significantly
FT less stable."
FT /evidence="ECO:0000269|PubMed:20487277"
FT MUTAGEN 93..96
FT /note="Missing: Decreased toxicity; protein is less
FT stable."
FT /evidence="ECO:0000269|PubMed:20487277"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:3KXE"
FT HELIX 8..25
FT /evidence="ECO:0007829|PDB:3KXE"
FT HELIX 27..46
FT /evidence="ECO:0007829|PDB:3KXE"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:3KXE"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:3KXE"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:3KXE"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:3KXE"
FT STRAND 69..86
FT /evidence="ECO:0007829|PDB:3KXE"
SQ SEQUENCE 96 AA; 11058 MW; ABE5EEB28FBC1E1C CRC64;
MKPYRLSRRA KADLDDIWTY SEQRWGVEQA ADYARELQAT IEMIAEHPGM GQPDENLRAG
YRRCASGSHV VFYRVGVRVE IIRVLHQSMN ARAHLG
