HIGB_ECOLI
ID HIGB_ECOLI Reviewed; 104 AA.
AC P64578; P42595; Q2M9C3;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=mRNA interferase toxin HigB;
DE EC=3.1.-.-;
DE AltName: Full=Endoribonuclease HigB;
DE AltName: Full=Toxin HigB;
GN Name=higB; Synonyms=ygjN; OrderedLocusNames=b3083, JW3054;
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 AN MRNA INTERFERASE, INDUCTION, AND OPERON STRUCTURE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=19943910; DOI=10.1111/j.1365-2958.2009.06969.x;
RA Christensen-Dalsgaard M., Jorgensen M.G., Gerdes K.;
RT "Three new RelE-homologous mRNA interferases of Escherichia coli
RT differentially induced by environmental stresses.";
RL Mol. Microbiol. 75:333-348(2010).
RN [4]
RP RETRACTED PAPER.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=21788497; DOI=10.1073/pnas.1100186108;
RA Maisonneuve E., Shakespeare L.J., Joergensen M.G., Gerdes K.;
RT "Bacterial persistence by RNA endonucleases.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13206-13211(2011).
RN [5]
RP RETRACTION NOTICE OF PUBMED:21788497.
RX PubMed=29531044; DOI=10.1073/pnas.1803278115;
RA Maisonneuve E., Shakespeare L.J., Joergensen M.G., Gerdes K.;
RL Proc. Natl. Acad. Sci. U.S.A. 115:E2901-E2901(2018).
CC -!- FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. A
CC probable translation-dependent mRNA interferase. Overexpression causes
CC cessation of cell growth and inhibits cell proliferation via inhibition
CC of translation; this blockage is overcome by subsequent expression of
CC antitoxin HigA. Overexpression causes cleavage of a number of mRNAs in
CC a translation-dependent fashion, suggesting this is an mRNA
CC interferase. {ECO:0000269|PubMed:19943910}.
CC -!- SUBUNIT: Probably forms a complex with the antitoxin HigA which
CC inhibits the mRNA interferase activity. {ECO:0000305|PubMed:19943910}.
CC -!- INTERACTION:
CC P64578; P67701: higA; NbExp=4; IntAct=EBI-1135071, EBI-1131548;
CC -!- INDUCTION: Induced by amino acid starvation and when translation is
CC blocked. Induction is decreased in the absence of the Lon protease
CC suggesting, by homology to other toxin-antitoxin systems, that Lon may
CC degrade the HigA antitoxin. Transcription is negatively regulated by
CC the cognate locus, probably by HigA. A member of the higB-higA operon.
CC {ECO:0000269|PubMed:19943910}.
CC -!- SIMILARITY: Belongs to the HigB mRNA interferase family. {ECO:0000305}.
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DR EMBL; U18997; AAA57884.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76118.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77133.1; -; Genomic_DNA.
DR PIR; H65096; H65096.
DR RefSeq; NP_417554.1; NC_000913.3.
DR RefSeq; WP_000550189.1; NZ_LN832404.1.
DR PDB; 5IFG; X-ray; 2.70 A; A/C=1-104.
DR PDB; 6KML; X-ray; 2.10 A; A/C=1-104.
DR PDB; 6KMQ; X-ray; 2.35 A; A=1-104.
DR PDBsum; 5IFG; -.
DR PDBsum; 6KML; -.
DR PDBsum; 6KMQ; -.
DR AlphaFoldDB; P64578; -.
DR SMR; P64578; -.
DR BioGRID; 4262402; 8.
DR BioGRID; 851907; 1.
DR ComplexPortal; CPX-4121; HigAB toxin-antitoxin complex.
DR IntAct; P64578; 2.
DR STRING; 511145.b3083; -.
DR PaxDb; P64578; -.
DR PRIDE; P64578; -.
DR EnsemblBacteria; AAC76118; AAC76118; b3083.
DR EnsemblBacteria; BAE77133; BAE77133; BAE77133.
DR GeneID; 66506933; -.
DR GeneID; 947591; -.
DR KEGG; ecj:JW3054; -.
DR KEGG; eco:b3083; -.
DR PATRIC; fig|1411691.4.peg.3646; -.
DR EchoBASE; EB2584; -.
DR eggNOG; COG4680; Bacteria.
DR HOGENOM; CLU_153067_0_1_6; -.
DR InParanoid; P64578; -.
DR OMA; VMFFADF; -.
DR PhylomeDB; P64578; -.
DR BioCyc; EcoCyc:G7602-MON; -.
DR BioCyc; MetaCyc:G7602-MON; -.
DR PRO; PR:P64578; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0110001; C:toxin-antitoxin complex; IDA:EcoCyc.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:EcoCyc.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0017148; P:negative regulation of translation; IDA:EcoCyc.
DR GO; GO:0040008; P:regulation of growth; IC:ComplexPortal.
DR GO; GO:0043488; P:regulation of mRNA stability; IDA:EcoCyc.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR InterPro; IPR018669; Toxin_HigB.
DR Pfam; PF09907; HigB_toxin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endonuclease; Hydrolase; Nuclease; Reference proteome;
KW RNA-binding; Stress response; Toxin-antitoxin system.
FT CHAIN 1..104
FT /note="mRNA interferase toxin HigB"
FT /id="PRO_0000169421"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:6KML"
FT HELIX 7..15
FT /evidence="ECO:0007829|PDB:6KML"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:6KML"
FT HELIX 20..32
FT /evidence="ECO:0007829|PDB:6KML"
FT HELIX 38..44
FT /evidence="ECO:0007829|PDB:6KML"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:5IFG"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:6KML"
FT TURN 63..66
FT /evidence="ECO:0007829|PDB:6KML"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:6KML"
FT TURN 75..78
FT /evidence="ECO:0007829|PDB:6KML"
FT STRAND 79..87
FT /evidence="ECO:0007829|PDB:6KML"
FT HELIX 88..96
FT /evidence="ECO:0007829|PDB:6KML"
SQ SEQUENCE 104 AA; 12103 MW; F23FB5F433C52C22 CRC64;
MHLITQKALK DAAEKYPQHK TELVALGNTI AKGYFKKPES LKAVFPSLDN FKYLDKHYVF
NVGGNELRVV AMVFFESQKC YIREVMTHKE YDFFTAVHRT KGKK
