YPJF_ECOLI
ID YPJF_ECOLI Reviewed; 109 AA.
AC Q46953; Q2MAD2;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Toxin YpjF {ECO:0000303|PubMed:14594833};
GN Name=ypjF; OrderedLocusNames=b2646, JW2627;
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 / 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 [2]
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 [3]
RP FUNCTION AS A TOXIN.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=14594833; DOI=10.1128/jb.185.22.6600-6608.2003;
RA Brown J.M., Shaw K.J.;
RT "A novel family of Escherichia coli toxin-antitoxin gene pairs.";
RL J. Bacteriol. 185:6600-6608(2003).
RN [4]
RP FUNCTION AS A TOXIN, INTERACTION WITH FTSZ AND MREB, AND MUTAGENESIS OF
RP PHE-65.
RX PubMed=28931012; DOI=10.1371/journal.pgen.1007007;
RA Heller D.M., Tavag M., Hochschild A.;
RT "CbtA toxin of Escherichia coli inhibits cell division and cell elongation
RT via direct and independent interactions with FtsZ and MreB.";
RL PLoS Genet. 13:E1007007-E1007007(2017).
RN [5]
RP FUNCTION AS A TOXIN, INTERACTION WITH FTSZ, INDUCTION, AND DISRUPTION
RP 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).
CC -!- FUNCTION: Toxic component of a type IV toxin-antitoxin (TA) system
CC (PubMed:14594833, PubMed:28257056, PubMed:28931012). Acts as a dual
CC toxin inhibitor that blocks cell division and cell elongation in
CC genetically separable interactions with FtsZ and MreB
CC (PubMed:28931012). Overexpression results in inhibition of growth in
CC liquid cultures (PubMed:14594833, PubMed:28257056, PubMed:28931012).
CC Overexpression leads to formation of lemon-shaped cells; inactivated by
CC overexpression of cognate antitoxin YfjZ but not when the 2 genes are
CC coexpressed from the same plasmid (PubMed:28257056). Also neutralized
CC by overexpression of non-cognate antitoxins YafW and CbeA
CC (PubMed:28257056). {ECO:0000269|PubMed:14594833,
CC ECO:0000269|PubMed:28257056, ECO:0000269|PubMed:28931012}.
CC -!- SUBUNIT: Interacts with FtsZ but not MreB (PubMed:28257056). Another
CC group finds interaction with FtsZ and MreB (PubMed:28931012).
CC {ECO:0000269|PubMed:28257056, ECO:0000269|PubMed:28931012}.
CC -!- INTERACTION:
CC Q46953; P0AAY6: ybjN; NbExp=3; IntAct=EBI-9134503, EBI-9138440;
CC -!- INDUCTION: Expressed in mid-log phase at lower levels than toxin relE.
CC {ECO:0000269|PubMed:28257056}.
CC -!- DISRUPTION PHENOTYPE: Single deletion leads to an approximately 100-
CC fold reduction in resistance to oxidative stress, deletion of 3 type IV
CC toxin genes (cbtA, ykfI, ypfJ) leads to a slight reduction in
CC resistance to oxidative stress, has no effect on cell growth.
CC {ECO:0000269|PubMed:28257056}.
CC -!- MISCELLANEOUS: Encoded in prophage CP4-57. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CbtA/YkfI/YpjF toxin family. {ECO:0000305}.
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DR EMBL; U36840; AAA79814.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75694.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76774.1; -; Genomic_DNA.
DR PIR; T08657; T08657.
DR RefSeq; NP_417133.1; NC_000913.3.
DR RefSeq; WP_001094400.1; NZ_LN832404.1.
DR AlphaFoldDB; Q46953; -.
DR BioGRID; 4262253; 11.
DR BioGRID; 851465; 12.
DR IntAct; Q46953; 12.
DR STRING; 511145.b2646; -.
DR PaxDb; Q46953; -.
DR PRIDE; Q46953; -.
DR EnsemblBacteria; AAC75694; AAC75694; b2646.
DR EnsemblBacteria; BAE76774; BAE76774; BAE76774.
DR GeneID; 947131; -.
DR KEGG; ecj:JW2627; -.
DR KEGG; eco:b2646; -.
DR PATRIC; fig|1411691.4.peg.4092; -.
DR EchoBASE; EB4032; -.
DR eggNOG; ENOG5030CTH; Bacteria.
DR HOGENOM; CLU_129204_1_1_6; -.
DR OMA; KYALMLP; -.
DR PhylomeDB; Q46953; -.
DR BioCyc; EcoCyc:G7381-MON; -.
DR PRO; PR:Q46953; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR InterPro; IPR009610; CbtA_toxin.
DR Pfam; PF06755; CbtA_toxin; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Toxin-antitoxin system.
FT CHAIN 1..109
FT /note="Toxin YpjF"
FT /id="PRO_0000169288"
FT MUTAGEN 65
FT /note="F->S: Loss of interaction with FtsZ, no effect on
FT interaction with MreB."
FT /evidence="ECO:0000269|PubMed:28931012"
SQ SEQUENCE 109 AA; 12308 MW; CFF6B952B620C77A CRC64;
MNTLPATISQ AAKPCLSPVA VWQMLLTRLL EQHYGLTLND TPFSDETVIK EHIDAGITLA
DAVNFLVEKY ELVRIDHRGF SWQQQSPYIS VVDILRARRS TGLLKTNVK
