HICA_ECOLI
ID HICA_ECOLI Reviewed; 58 AA.
AC P76106; Q2MBB8;
DT 14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Probable mRNA interferase toxin HicA;
DE EC=3.1.-.-;
DE AltName: Full=Endoribonuclease HicA;
DE AltName: Full=Toxin HicA;
GN Name=hicA; Synonyms=yncN; OrderedLocusNames=b4532, JW5230;
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 PREDICTION OF FUNCTION.
RX PubMed=16895922; DOI=10.1093/bioinformatics/btl418;
RA Makarova K.S., Grishin N.V., Koonin E.V.;
RT "The HicAB cassette, a putative novel, RNA-targeting toxin-antitoxin system
RT in archaea and bacteria.";
RL Bioinformatics 22:2581-2584(2006).
RN [4]
RP FUNCTION AS AN MRNA INTERFERASE, INDUCTION, AND OPERON STRUCTURE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=19060138; DOI=10.1128/jb.01013-08;
RA Jorgensen M.G., Pandey D.P., Jaskolska M., Gerdes K.;
RT "HicA of Escherichia coli defines a novel family of translation-independent
RT mRNA interferases in bacteria and archaea.";
RL J. Bacteriol. 191:1191-1199(2009).
RN [5]
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 [6]
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-independent mRNA interferase. Overexpression
CC causes cessation of cell growth and inhibits cell proliferation via
CC inhibition of translation; this blockage is overcome (after 90 minutes)
CC by subsequent expression of antitoxin HicB. Overexpression causes
CC cleavage of a number of mRNAs and tmRNA, in a translation-independent
CC fashion, suggesting this is an mRNA interferase (PubMed:19060138).
CC {ECO:0000269|PubMed:19060138}.
CC -!- SUBUNIT: Probably forms a complex with the antitoxin HicB which
CC inhibits the mRNA interferase activity. {ECO:0000250}.
CC -!- INDUCTION: Induced by amino acid starvation, carbon starvation and when
CC translation is blocked. Induction no longer occurs in the absence of
CC Lon protease suggesting, by homology to other toxin-antitoxin systems,
CC that it may degrade the HicB antitoxin. A member of the hicA-hicB
CC operon. {ECO:0000269|PubMed:19060138}.
CC -!- SIMILARITY: Belongs to the HicA mRNA interferase family. {ECO:0000305}.
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DR EMBL; U00096; AAC74519.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE76438.1; -; Genomic_DNA.
DR PIR; H64895; H64895.
DR RefSeq; NP_415954.2; NC_000913.3.
DR RefSeq; WP_000813794.1; NZ_LN832404.1.
DR PDB; 6HPB; X-ray; 2.28 A; A/C=1-58.
DR PDBsum; 6HPB; -.
DR AlphaFoldDB; P76106; -.
DR SMR; P76106; -.
DR BioGRID; 4259495; 185.
DR BioGRID; 850351; 2.
DR ComplexPortal; CPX-4119; HicAB toxin-antitoxin complex.
DR IntAct; P76106; 2.
DR STRING; 511145.b4532; -.
DR PaxDb; P76106; -.
DR PRIDE; P76106; -.
DR EnsemblBacteria; AAC74519; AAC74519; b4532.
DR EnsemblBacteria; BAE76438; BAE76438; BAE76438.
DR GeneID; 66674712; -.
DR GeneID; 945989; -.
DR KEGG; ecj:JW5230; -.
DR KEGG; eco:b4532; -.
DR PATRIC; fig|1411691.4.peg.831; -.
DR eggNOG; COG1724; Bacteria.
DR HOGENOM; CLU_164851_5_0_6; -.
DR OMA; KRSIMPR; -.
DR BioCyc; EcoCyc:MON0-2673; -.
DR PRO; PR:P76106; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0110001; C:toxin-antitoxin complex; IPI:ComplexPortal.
DR GO; GO:0004521; F:endoribonuclease activity; IMP:EcoCyc.
DR GO; GO:0003729; F:mRNA binding; IEA:InterPro.
DR GO; GO:0006402; P:mRNA catabolic process; IMP:EcoCyc.
DR GO; GO:0040008; P:regulation of growth; IC:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:ComplexPortal.
DR Gene3D; 3.30.920.30; -; 1.
DR InterPro; IPR012933; HicA_mRNA_interferase.
DR InterPro; IPR038570; HicA_sf.
DR Pfam; PF07927; HicA_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..58
FT /note="Probable mRNA interferase toxin HicA"
FT /id="PRO_0000259908"
FT HELIX 3..12
FT /evidence="ECO:0007829|PDB:6HPB"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:6HPB"
FT STRAND 21..28
FT /evidence="ECO:0007829|PDB:6HPB"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:6HPB"
FT HELIX 45..54
FT /evidence="ECO:0007829|PDB:6HPB"
SQ SEQUENCE 58 AA; 6782 MW; C5656B478837BAB6 CRC64;
MKQSEFRRWL ESQGVDVANG SNHLKLRFHG RRSVMPRHPC DEIKEPLRKA ILKQLGLS
