HIGA_PROVU
ID HIGA_PROVU Reviewed; 104 AA.
AC Q7A224; Q52306;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Antitoxin HigA {ECO:0000303|PubMed:24257752};
DE AltName: Full=Antidote protein {ECO:0000312|EMBL:AAC43983.1, ECO:0000312|EMBL:BAB93824.1};
DE AltName: Full=Host inhibition of growth protein A {ECO:0000303|PubMed:24257752, ECO:0000303|PubMed:8645296};
GN Name=higA {ECO:0000312|EMBL:AAC43983.1, ECO:0000312|EMBL:BAB93824.1};
OS Proteus vulgaris.
OG Plasmid Rts1 {ECO:0000312|EMBL:BAB93824.1}.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=585 {ECO:0000312|EMBL:BAB93824.1};
RN [1] {ECO:0000312|EMBL:AAC43983.1}
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:AAD00516.1}
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:BAB93824.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=UR-75 {ECO:0000312|EMBL:BAB93824.1}; 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, AND SUBUNIT.
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 HIGB, FUNCTION,
RP SUBUNIT, DNA-BINDING, 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: Antitoxin component of a type II toxin-antitoxin (TA) system
CC that counteracts the effect of the HigB toxin (PubMed:19423702,
CC PubMed:8645296, PubMed:24257752). Binds to its own promoter and
CC regulates transcription of the higB/higA operon (PubMed:24257752).
CC {ECO:0000269|PubMed:19423702, ECO:0000269|PubMed:24257752,
CC ECO:0000269|PubMed:8645296}.
CC -!- SUBUNIT: Forms a complex with the mRNA interferase HigB which inhibits
CC the mRNA interferase activity (PubMed:19423702). The heterodimer
CC dimerizes to form a HigB-(HigA)2-HigB tetramer that is able to bind to
CC the DNA (PubMed:24257752). {ECO:0000269|PubMed:19423702,
CC ECO:0000269|PubMed:24257752}.
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DR EMBL; U43847; AAC43983.1; -; Genomic_DNA.
DR EMBL; U81366; AAD00516.1; -; Genomic_DNA.
DR EMBL; AP004237; BAB93824.1; -; Genomic_DNA.
DR RefSeq; NP_640222.1; NC_003905.1.
DR RefSeq; WP_011039854.1; NC_003905.1.
DR PDB; 4MCT; X-ray; 2.80 A; A/C=1-104.
DR PDB; 4MCX; X-ray; 2.10 A; A/C/E=1-104.
DR PDB; 6CF1; X-ray; 1.90 A; A/B=1-104.
DR PDB; 6CHV; X-ray; 2.90 A; A/B/C/D/G/H=1-104.
DR PDBsum; 4MCT; -.
DR PDBsum; 4MCX; -.
DR PDBsum; 6CF1; -.
DR PDBsum; 6CHV; -.
DR AlphaFoldDB; Q7A224; -.
DR SMR; Q7A224; -.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IC:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0097351; F:toxin sequestering activity; IDA:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:UniProtKB.
DR CDD; cd00093; HTH_XRE; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR InterPro; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR013430; Toxin_antidote_HigA.
DR PANTHER; PTHR36924; PTHR36924; 1.
DR Pfam; PF01381; HTH_3; 1.
DR SMART; SM00530; HTH_XRE; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR TIGRFAMs; TIGR02607; antidote_HigA; 1.
DR PROSITE; PS50943; HTH_CROC1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Plasmid; Toxin-antitoxin system; Transcription;
KW Transcription regulation.
FT CHAIN 1..104
FT /note="Antitoxin HigA"
FT /id="PRO_0000434130"
FT DOMAIN 13..67
FT /note="HTH cro/C1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT DNA_BIND 24..43
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00257,
FT ECO:0007744|PDB:4MCT, ECO:0007744|PDB:4MCX"
FT SITE 3
FT /note="Interaction with HigB"
FT /evidence="ECO:0000269|PubMed:24257752"
FT SITE 4
FT /note="Interaction with HigB"
FT /evidence="ECO:0000269|PubMed:24257752"
FT HELIX 9..20
FT /evidence="ECO:0007829|PDB:6CF1"
FT HELIX 24..31
FT /evidence="ECO:0007829|PDB:6CF1"
FT HELIX 35..42
FT /evidence="ECO:0007829|PDB:6CF1"
FT HELIX 50..60
FT /evidence="ECO:0007829|PDB:6CF1"
FT HELIX 64..78
FT /evidence="ECO:0007829|PDB:6CF1"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:6CF1"
SQ SEQUENCE 104 AA; 11537 MW; 09CC0CB20F89AEF0 CRC64;
MRQFKVSHPG EMIARDLEDM GVSGRRFAHN IGVTPATVSR LLAGKTALTP SLSIRIAAAL
GSTPEFWLRL QSNYDLRQLE NQIDTSGIVL YGESNEQQQN AQEH
