HIGB_PROVU
ID HIGB_PROVU Reviewed; 92 AA.
AC Q7A225; Q52305;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=Endoribonuclease HigB {ECO:0000303|PubMed:19423702};
DE EC=3.1.-.- {ECO:0000269|PubMed:19423702};
DE AltName: Full=Host inhibition of growth protein B {ECO:0000303|PubMed:24257752, ECO:0000303|PubMed:8645296};
DE AltName: Full=Killer protein {ECO:0000303|PubMed:8645296, ECO:0000312|EMBL:AAC43982.1, ECO:0000312|EMBL:BAB93823.1};
DE AltName: Full=Toxin HigB {ECO:0000303|PubMed:19423702, ECO:0000303|PubMed:24257752};
DE AltName: Full=mRNA interferase HigB {ECO:0000305};
GN Name=higB {ECO:0000312|EMBL:AAC43982.1, ECO:0000312|EMBL:BAB93823.1};
OS Proteus vulgaris.
OG Plasmid Rts1 {ECO:0000312|EMBL:AAC43982.1, ECO:0000312|EMBL:BAB93823.1}.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=585 {ECO:0000312|EMBL:BAB93823.1};
RN [1] {ECO:0000312|EMBL:AAC43982.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND OPERON STRUCTURE.
RC PLASMID=Rts1;
RX PubMed=8645296; DOI=10.1006/bbrc.1996.0396;
RA Tian Q.B., Ohnishi M., Tabuchi A., Terawaki Y.;
RT "A new plasmid-encoded proteic killer gene system: cloning, sequencing, and
RT analyzing hig locus of plasmid Rts1.";
RL Biochem. Biophys. Res. Commun. 220:280-284(1996).
RN [2] {ECO:0000312|EMBL:AAD00515.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=Rts1;
RX PubMed=9007009; DOI=10.1006/plas.1996.0041;
RA Yonemitsu H., Fujihashi T., Higuchi H., Hong H., Morishige H., Mochida S.,
RA Kaji A.;
RT "Instability of Rts1 (drug-resistant factor) replicon: stabilization by DNA
RT fragments derived from Rts1.";
RL Plasmid 36:143-152(1996).
RN [3] {ECO:0000312|EMBL:BAB93823.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=UR-75 {ECO:0000312|EMBL:BAB93823.1}; PLASMID=Rts1;
RX PubMed=12029035; DOI=10.1128/jb.184.12.3194-3202.2002;
RA Murata T., Ohnishi M., Ara T., Kaneko J., Han C.-G., Li Y.F., Takashima K.,
RA Nojima H., Nakayama K., Kaji A., Kamio Y., Miki T., Mori H., Ohtsubo E.,
RA Terawaki Y., Hayashi T.;
RT "Complete nucleotide sequence of plasmid Rts1: implications for evolution
RT of large plasmid Genomes.";
RL J. Bacteriol. 184:3194-3202(2002).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND MUTAGENESIS OF HIS-92.
RC PLASMID=Rts1;
RX PubMed=19423702; DOI=10.1074/jbc.m109.008763;
RA Hurley J.M., Woychik N.A.;
RT "Bacterial toxin HigB associates with ribosomes and mediates translation-
RT dependent mRNA cleavage at A-rich sites.";
RL J. Biol. Chem. 284:18605-18613(2009).
RN [5] {ECO:0007744|PDB:4MCT, ECO:0007744|PDB:4MCX}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH HIGA, FUNCTION,
RP SUBUNIT, AND SITES.
RX PubMed=24257752; DOI=10.1074/jbc.m113.512095;
RA Schureck M.A., Maehigashi T., Miles S.J., Marquez J., Cho S.E., Erdman R.,
RA Dunham C.M.;
RT "Structure of the Proteus vulgaris HigB-(HigA)2-HigB toxin-antitoxin
RT complex.";
RL J. Biol. Chem. 289:1060-1070(2014).
CC -!- FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system
CC (PubMed:19423702, PubMed:24257752, PubMed:8645296). A ribosome-
CC associated translation-dependent mRNA interferase. Inhibits translation
CC by sequence-specific cleavage of mRNA. Prefers either in-frame or out-
CC of-frame 5'-AAA-3' codons (lysine). Cleaves also the first three AAAs
CC of stretches of four or more A sequences. 20% of codons containing AA
CC are cleaved and occassionally cuts even at a single A
CC (PubMed:19423702). {ECO:0000269|PubMed:19423702,
CC ECO:0000269|PubMed:24257752}.
CC -!- SUBUNIT: Forms a complex with the antitoxin HigA which inhibits the
CC mRNA interferase activity (PubMed:19423702). The heterodimer dimerizes
CC to form a HigB-(HigA)2-HigB tetramer that is able to bind to the DNA
CC (PubMed:24257752). {ECO:0000269|PubMed:19423702,
CC ECO:0000269|PubMed:24257752, ECO:0000269|PubMed:8645296}.
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DR EMBL; U43847; AAC43982.1; -; Genomic_DNA.
DR EMBL; U81366; AAD00515.1; -; Genomic_DNA.
DR EMBL; AP004237; BAB93823.1; -; Genomic_DNA.
DR RefSeq; NP_640221.1; NC_003905.1.
DR RefSeq; WP_011039853.1; NC_003905.1.
DR PDB; 4MCT; X-ray; 2.80 A; B/D=1-92.
DR PDB; 4MCX; X-ray; 2.10 A; B/D/F=1-92.
DR PDB; 4PX8; X-ray; 1.25 A; A=2-92.
DR PDB; 4W4G; X-ray; 3.30 A; QY/XY=2-92.
DR PDB; 4YPB; X-ray; 3.40 A; QY/XY=2-91.
DR PDB; 4YY3; X-ray; 3.60 A; Y=2-92.
DR PDB; 4YZV; X-ray; 3.10 A; QY/XY=2-91.
DR PDB; 4ZSN; X-ray; 3.60 A; QY/XY=2-92.
DR PDB; 5IWH; X-ray; 1.10 A; A=2-91.
DR PDB; 5IXL; X-ray; 1.55 A; A/B/C/D/E/F/G/H=2-90.
DR PDBsum; 4MCT; -.
DR PDBsum; 4MCX; -.
DR PDBsum; 4PX8; -.
DR PDBsum; 4W4G; -.
DR PDBsum; 4YPB; -.
DR PDBsum; 4YY3; -.
DR PDBsum; 4YZV; -.
DR PDBsum; 4ZSN; -.
DR PDBsum; 5IWH; -.
DR PDBsum; 5IXL; -.
DR AlphaFoldDB; Q7A225; -.
DR SMR; Q7A225; -.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0043022; F:ribosome binding; IMP:UniProtKB.
DR GO; GO:0030371; F:translation repressor activity; IDA:UniProtKB.
DR GO; GO:0006379; P:mRNA cleavage; IDA:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB.
DR GO; GO:0006401; P:RNA catabolic process; IDA:UniProtKB.
DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IDA:UniProtKB.
DR Gene3D; 3.30.2310.20; -; 1.
DR InterPro; IPR007711; HigB-1.
DR InterPro; IPR035093; RelE/ParE_toxin_dom_sf.
DR PANTHER; PTHR40266; PTHR40266; 1.
DR Pfam; PF05015; HigB-like_toxin; 1.
DR SUPFAM; SSF143011; SSF143011; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endonuclease; Hydrolase; Nuclease; Plasmid; RNA-binding;
KW Toxin-antitoxin system.
FT CHAIN 1..92
FT /note="Endoribonuclease HigB"
FT /id="PRO_0000434129"
FT ACT_SITE 92
FT /evidence="ECO:0000269|PubMed:19423702"
FT SITE 14
FT /note="Interaction with HigA"
FT /evidence="ECO:0000269|PubMed:24257752"
FT SITE 31
FT /note="Interaction with HigA"
FT /evidence="ECO:0000269|PubMed:24257752"
FT MUTAGEN 92
FT /note="H->Q: Loss of toxicity and mRNA cleavage, but still
FT binds to ribosomes."
FT /evidence="ECO:0000269|PubMed:19423702"
FT HELIX 8..16
FT /evidence="ECO:0007829|PDB:5IWH"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:5IWH"
FT HELIX 27..39
FT /evidence="ECO:0007829|PDB:5IWH"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:5IWH"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:5IWH"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:5IWH"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:5IWH"
FT STRAND 72..79
FT /evidence="ECO:0007829|PDB:5IWH"
FT STRAND 82..91
FT /evidence="ECO:0007829|PDB:5IWH"
SQ SEQUENCE 92 AA; 10742 MW; 77EA5B1CEF125D65 CRC64;
MIKSFKHKGL KLLFEKGVTS GVPAQDVDRI NDRLQAIDTA TEIGELNRQI YKLHPLKGDR
EGYWSITVRA NWRITFQFIN GDAYILNYED YH
