HIGA_ECOLI
ID HIGA_ECOLI Reviewed; 138 AA.
AC P67701; P42594; Q2M9C4;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Antitoxin HigA;
GN Name=higA; Synonyms=ygjM; OrderedLocusNames=b3082, JW3053;
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 ANTITOXIN, 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).
CC -!- FUNCTION: Antitoxin component of a type II toxin-antitoxin (TA) system.
CC Functions as an mRNA interferase antitoxin; overexpression prevents
CC HigB-mediated cessation of cell growth and inhibition of cell
CC proliferation. {ECO:0000269|PubMed:19943910}.
CC -!- SUBUNIT: Probably forms a complex with the mRNA interferase HigB which
CC inhibits the mRNA interferase activity. {ECO:0000305}.
CC -!- INTERACTION:
CC P67701; P64578: higB; NbExp=4; IntAct=EBI-1131548, EBI-1135071;
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 this protein. A member of the higB-higA
CC operon. {ECO:0000269|PubMed:19943910}.
CC -!- SIMILARITY: Belongs to the HigA antitoxin family. {ECO:0000305}.
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DR EMBL; U18997; AAA57883.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76117.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77132.1; -; Genomic_DNA.
DR PIR; G65096; G65096.
DR RefSeq; NP_417553.1; NC_000913.3.
DR RefSeq; WP_000560266.1; NZ_LN832404.1.
DR PDB; 5IFG; X-ray; 2.70 A; B/D=1-138.
DR PDB; 6JQ4; X-ray; 2.00 A; A=1-138.
DR PDB; 6KML; X-ray; 2.10 A; B/D=1-138.
DR PDB; 6KMQ; X-ray; 2.35 A; B=1-138.
DR PDBsum; 5IFG; -.
DR PDBsum; 6JQ4; -.
DR PDBsum; 6KML; -.
DR PDBsum; 6KMQ; -.
DR AlphaFoldDB; P67701; -.
DR SMR; P67701; -.
DR BioGRID; 4262401; 7.
DR BioGRID; 851909; 3.
DR ComplexPortal; CPX-4121; HigAB toxin-antitoxin complex.
DR IntAct; P67701; 13.
DR STRING; 511145.b3082; -.
DR PaxDb; P67701; -.
DR PRIDE; P67701; -.
DR EnsemblBacteria; AAC76117; AAC76117; b3082.
DR EnsemblBacteria; BAE77132; BAE77132; BAE77132.
DR GeneID; 66673019; -.
DR GeneID; 947593; -.
DR KEGG; ecj:JW3053; -.
DR KEGG; eco:b3082; -.
DR PATRIC; fig|1411691.4.peg.3647; -.
DR EchoBASE; EB2583; -.
DR eggNOG; COG5499; Bacteria.
DR HOGENOM; CLU_125852_0_0_6; -.
DR OMA; DIAQTWA; -.
DR PhylomeDB; P67701; -.
DR BioCyc; EcoCyc:G7601-MON; -.
DR BioCyc; MetaCyc:G7601-MON; -.
DR PRO; PR:P67701; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0110001; C:toxin-antitoxin complex; IDA:EcoCyc.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:EcoCyc.
DR GO; GO:0040008; P:regulation of growth; IC:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR CDD; cd00093; HTH_XRE; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR InterPro; IPR039060; Antitox_HigA.
DR InterPro; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR PANTHER; PTHR40455; PTHR40455; 1.
DR Pfam; PF01381; HTH_3; 1.
DR SMART; SM00530; HTH_XRE; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR PROSITE; PS50943; HTH_CROC1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Reference proteome; Repressor;
KW Toxin-antitoxin system; Transcription; Transcription regulation.
FT CHAIN 1..138
FT /note="Antitoxin HigA"
FT /id="PRO_0000149763"
FT DOMAIN 84..136
FT /note="HTH cro/C1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT DNA_BIND 95..114
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT HELIX 4..17
FT /evidence="ECO:0007829|PDB:6JQ4"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:6JQ4"
FT HELIX 27..43
FT /evidence="ECO:0007829|PDB:6JQ4"
FT HELIX 49..63
FT /evidence="ECO:0007829|PDB:6JQ4"
FT HELIX 65..76
FT /evidence="ECO:0007829|PDB:6JQ4"
FT HELIX 80..91
FT /evidence="ECO:0007829|PDB:6JQ4"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:6JQ4"
FT HELIX 104..111
FT /evidence="ECO:0007829|PDB:6JQ4"
FT HELIX 119..129
FT /evidence="ECO:0007829|PDB:6JQ4"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:6JQ4"
SQ SEQUENCE 138 AA; 14995 MW; 4A14D9E43480DCB5 CRC64;
MIAIADILQA GEKLTAVAPF LAGIQNEEQY TQALELVDHL LLNDPENPLL DLVCAKITAW
EESAPEFAEF NAMAQAMPGG IAVIRTLMDQ YGLTLSDLPE IGSKSMVSRV LSGKRKLTLE
HAKKLATRFG ISPALFID
