YAFQ_ECOBD
ID YAFQ_ECOBD Reviewed; 92 AA.
AC A0A140NAP5;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 11-MAY-2016, sequence version 1.
DT 25-MAY-2022, entry version 29.
DE RecName: Full=mRNA interferase toxin YafQ;
DE EC=3.1.-.-;
DE AltName: Full=Endoribonuclease YafQ;
DE AltName: Full=Toxin YafQ;
GN Name=yafQ; OrderedLocusNames=ECBD_3397;
OS Escherichia coli (strain B / BL21-DE3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=469008;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B / BL21-DE3;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Anderson I., Sorek R., Rubin E.;
RT "Complete sequence of Escherichia coli BL21(DE3).";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:4ML0, ECO:0007744|PDB:4ML2, ECO:0007744|PDB:4MMG, ECO:0007744|PDB:4MMJ}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) ALONE AND IN COMPLEX WITH DINJ,
RP FUNCTION AS AN RNASE, SUBUNIT, PROBABLE DNA-BINDING, AND MUTAGENESIS OF
RP HIS-23; LYS-48 AND HIS-87.
RC STRAIN=B / BL21-DE3;
RX PubMed=24923448; DOI=10.1074/jbc.m114.559773;
RA Liang Y., Gao Z., Wang F., Zhang Y., Dong Y., Liu Q.;
RT "Structural and functional characterization of Escherichia coli toxin-
RT antitoxin complex DinJ-YafQ.";
RL J. Biol. Chem. 289:21191-21202(2014).
CC -!- FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system
CC (PubMed:24923448). A sequence-specific mRNA endoribonuclease that
CC inhibits translation elongation and induces bacterial stasis
CC (Probable). Cleavage occurs between the second and third residue of the
CC Lys codon followed by a G or A (5'AAA(G/A)3'), is reading-frame
CC dependent and occurs within the 5' end of most mRNAs (By similarity).
CC Ribosome-binding confers the sequence specificity and reading frame-
CC dependence (By similarity). The YafQ-DinJ heterotetramer binds the
CC consensus sequence 5'-TTTGAGCTACA-3' in the dinJ promoter; DinJ also
CC binds DNA but not as well as the YafQ-DinJ complex (PubMed:24923448).
CC {ECO:0000250|UniProtKB:Q47149, ECO:0000269|PubMed:24923448}.
CC -!- SUBUNIT: Monomer in solution, forms a heterotetramer with antitoxin
CC DinJ, with 2 YafQ-DinJ dimers associated via the N-terminus of the DinJ
CC antitoxins (YafQ-(DinJ)2-YafQ) (PubMed:24923448).
CC {ECO:0000269|PubMed:24923448}.
CC -!- SIMILARITY: Belongs to the RelE toxin family. YafQ subfamily.
CC {ECO:0000305}.
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DR EMBL; CP001665; ACT30397.1; -; Genomic_DNA.
DR RefSeq; WP_000615981.1; NZ_CP053602.1.
DR PDB; 4ML0; X-ray; 2.10 A; B/D/F/H/J/L/N/P=1-92.
DR PDB; 4ML2; X-ray; 1.50 A; A=1-92.
DR PDB; 4MMG; X-ray; 1.50 A; A/B=1-92.
DR PDB; 4MMJ; X-ray; 1.80 A; A=1-92.
DR PDBsum; 4ML0; -.
DR PDBsum; 4ML2; -.
DR PDBsum; 4MMG; -.
DR PDBsum; 4MMJ; -.
DR AlphaFoldDB; A0A140NAP5; -.
DR SMR; A0A140NAP5; -.
DR STRING; 469008.B21_00224; -.
DR KEGG; ebd:ECBD_3397; -.
DR PATRIC; fig|469008.15.peg.224; -.
DR eggNOG; COG3041; Bacteria.
DR HOGENOM; CLU_161929_4_1_6; -.
DR OMA; DHRECHV; -.
DR Proteomes; UP000002032; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.2310.20; -; 1.
DR InterPro; IPR007712; RelE/ParE_toxin.
DR InterPro; IPR035093; RelE/ParE_toxin_dom_sf.
DR InterPro; IPR004386; Toxin_YafQ-like.
DR PANTHER; PTHR40588; PTHR40588; 1.
DR Pfam; PF15738; YafQ_toxin; 1.
DR PIRSF; PIRSF006156; YafQ; 1.
DR SUPFAM; SSF143011; SSF143011; 1.
DR TIGRFAMs; TIGR02385; RelE_StbE; 1.
DR TIGRFAMs; TIGR00053; TIGR00053; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Endonuclease; Hydrolase; Nuclease; Repressor;
KW RNA-binding; Toxin-antitoxin system; Transcription;
KW Transcription regulation.
FT CHAIN 1..92
FT /note="mRNA interferase toxin YafQ"
FT /id="PRO_0000440935"
FT ACT_SITE 87
FT /note="Proton donor"
FT /evidence="ECO:0000305"
FT MUTAGEN 23
FT /note="H->Q: Moderate decrease in RNAase activity."
FT /evidence="ECO:0000269|PubMed:24923448"
FT MUTAGEN 48
FT /note="K->A: Moderate decrease in RNAase activity."
FT /evidence="ECO:0000269|PubMed:24923448"
FT MUTAGEN 87
FT /note="H->Q: No RNAase activity, still forms a complex with
FT DinJ."
FT /evidence="ECO:0000269|PubMed:24923448"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:4MMJ"
FT HELIX 10..21
FT /evidence="ECO:0007829|PDB:4MMJ"
FT HELIX 26..37
FT /evidence="ECO:0007829|PDB:4MMJ"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:4MMJ"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:4MMJ"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:4MMJ"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:4MMJ"
FT STRAND 76..85
FT /evidence="ECO:0007829|PDB:4MMJ"
FT HELIX 87..91
FT /evidence="ECO:0007829|PDB:4MMJ"
SQ SEQUENCE 92 AA; 10861 MW; CD880151BD4B8E8C CRC64;
MIQRDIEYSG QFSKDVKLAQ KRHKDMNKLK YLMTLLINNT LPLPAVYKDH PLQSSWKGYR
DAHVEPDWIL IYKLTDKLLR FERTGTHAAL FG
