YFJZ_ECOLI
ID YFJZ_ECOLI Reviewed; 105 AA.
AC P52141;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Antitoxin YfjZ {ECO:0000303|PubMed:28257056};
GN Name=yfjZ; OrderedLocusNames=b2645, JW2626;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION AS AN ANTITOXIN, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113;
RX PubMed=28257056; DOI=10.3390/toxins9030077;
RA Wen Z., Wang P., Sun C., Guo Y., Wang X.;
RT "Interaction of type IV toxin/antitoxin systems in cryptic prophages of
RT Escherichia coli K-12.";
RL Toxins 9:0-0(2017).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of a hypothetical protein JW2626 from E. coli.";
RL Submitted (JUL-2007) to the PDB data bank.
RN [6]
RP STRUCTURE BY NMR.
RG Northeast structural genomics consortium (NESG);
RT "NMR solution structure of E.coli hypothetical protein YfjZ.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Antitoxin component of a type IV toxin-antitoxin (TA) system.
CC Antitoxin that counteracts the effect of cognate toxin YpjF
CC (PubMed:28257056). Also counteracts the effect of non-cognate toxins
CC CbtA and YfkI (PubMed:28257056). {ECO:0000269|PubMed:28257056}.
CC -!- INDUCTION: Expressed in mid-log phase at considerably lower levels than
CC antitoxin relB. {ECO:0000269|PubMed:28257056}.
CC -!- DISRUPTION PHENOTYPE: Single deletion has no effect on expression of
CC cognate toxin ypjF i.e. the probable operon is not autoregulatory
CC (PubMed:28257056). Single deletion leads to increased biofilm
CC formation, deletion of 3 type IV antitoxin genes (cbeA, yafW, yfjZ) has
CC no effect on cell growth (PubMed:28257056).
CC {ECO:0000269|PubMed:28257056}.
CC -!- MISCELLANEOUS: Encoded in prophage CP4-57. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CbeA/YafW/YfjZ antitoxin family.
CC {ECO:0000305}.
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DR EMBL; U36840; AAA79813.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75693.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16513.1; -; Genomic_DNA.
DR PIR; T08656; T08656.
DR RefSeq; NP_417132.1; NC_000913.3.
DR RefSeq; WP_000072690.1; NZ_LN832404.1.
DR PDB; 2EA9; X-ray; 2.10 A; A=1-105.
DR PDB; 2JN7; NMR; -; A=1-105.
DR PDBsum; 2EA9; -.
DR PDBsum; 2JN7; -.
DR AlphaFoldDB; P52141; -.
DR BMRB; P52141; -.
DR SMR; P52141; -.
DR BioGRID; 4262252; 14.
DR IntAct; P52141; 1.
DR STRING; 511145.b2645; -.
DR PaxDb; P52141; -.
DR PRIDE; P52141; -.
DR EnsemblBacteria; AAC75693; AAC75693; b2645.
DR EnsemblBacteria; BAA16513; BAA16513; BAA16513.
DR GeneID; 947123; -.
DR KEGG; ecj:JW2626; -.
DR KEGG; eco:b2645; -.
DR PATRIC; fig|1411691.4.peg.4093; -.
DR EchoBASE; EB3004; -.
DR eggNOG; ENOG50304F4; Bacteria.
DR HOGENOM; CLU_144696_1_0_6; -.
DR OMA; HDGFTCE; -.
DR PhylomeDB; P52141; -.
DR BioCyc; EcoCyc:G7380-MON; -.
DR EvolutionaryTrace; P52141; -.
DR PRO; PR:P52141; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0051495; P:positive regulation of cytoskeleton organization; IEA:InterPro.
DR InterPro; IPR009320; Antitoxin_CbeA.
DR InterPro; IPR038025; CbeA_sf.
DR Pfam; PF06154; CbeA_antitoxin; 1.
DR SUPFAM; SSF143737; SSF143737; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Toxin-antitoxin system.
FT CHAIN 1..105
FT /note="Antitoxin YfjZ"
FT /id="PRO_0000169285"
FT HELIX 5..8
FT /evidence="ECO:0007829|PDB:2EA9"
FT STRAND 12..23
FT /evidence="ECO:0007829|PDB:2EA9"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:2EA9"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:2EA9"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:2EA9"
FT HELIX 44..65
FT /evidence="ECO:0007829|PDB:2EA9"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:2EA9"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:2EA9"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:2EA9"
FT STRAND 93..102
FT /evidence="ECO:0007829|PDB:2EA9"
SQ SEQUENCE 105 AA; 11737 MW; 3E3838D48C7A527D CRC64;
MSNTTWGLQR DITPRLGARL VQEGNQLHYL ADRASITGKF SDAECPKLDV VFPHFISQIE
SMLTTGELNP RHAQCVTLYH NGFTCEADTL GSCGYVYIAV YPTQR
